https://wiki.oroboros.at/api.php?action=feedcontributions&user=Bader+Helga&feedformat=atomBioblast - User contributions [en]2024-03-29T08:19:54ZUser contributionsMediaWiki 1.36.1https://wiki.oroboros.at/index.php?title=Bovine_serum_albumin&diff=94763Bovine serum albumin2015-07-03T09:35:14Z<p>Bader Helga: </p>
<hr />
<div>{{MitoPedia<br />
|abbr=BSA<br />
|description=Bovine serum albumine is a membane stabilizer, oxygen radical scavenger, and binds Ca2+ and free fatty acids, hence the rather expensive essentially free fatty acid free BSA is required in mitochondrial isolation and respiration media. Sigma A 6003 fraction V.<br />
|info=[http://en.wikipedia.org/wiki/Bovine_serum_albumin Wikipedia]<br />
|type=Chemicals<br />
}}<br />
{{MitoPedia methods|type=Chemicals<br />
}}<br />
{{MitoPedia topics|type=Chemicals<br />
}}<br />
{{Labeling<br />
|instruments=Chemicals; Media<br />
|topics=Fatty acid<br />
}}</div>Bader Helgahttps://wiki.oroboros.at/index.php?title=Irving_2015_J_Clin_Endocrinol_Metab&diff=92457Irving 2015 J Clin Endocrinol Metab2015-06-09T13:45:26Z<p>Bader Helga: </p>
<hr />
<div>{{Publication<br />
|title=Irving BA, Lanza IR, Henderson GC, Rao RR, Spiegelman BM, Nair KS (2015) Combined training enhances skeletal muscle mitochondrial oxidative capacity independent of age. J Clin Endocrinol Metab 100:1654-63.<br />
|info=[http://www.ncbi.nlm.nih.gov/pubmed/25599385 PMID: 25599385]<br />
|authors=Irving BA, Lanza IR, Henderson GC, Rao RR, Spiegelman BM, Nair KS<br />
|year=2015<br />
|journal=J Clin Endocrinol Metab<br />
|abstract=Skeletal muscle from sedentary older adults exhibits reduced mitochondrial abundance and oxidative capacity (OXPHOS).<br />
<br />
The primary objective was to determine whether eight weeks of combined training (CT) has more robust effect than, endurance training (ET) or resistance training (RT) on mitochondrial physiology in healthy young (18–30 y) and older (≥65 y) adults.<br />
<br />
Thirty-four young and 31 older adults were randomized to eight weeks of ET, RT,<br />
control/CT. Control subjects completed eight weeks of no exercise (control) followed by eight weeks of CT. Body composition, skeletal muscle strength, and peak oxygen uptake were measured before and after the intervention. Vastus lateralis muscle biopsies were obtained before and 48 h after the intervention. Mitochondrial physiology was evaluated by high-resolution respirometry,<br />
and expression of mitochondrial proteins and transcription factors by quantitative PCR and immunoblotting.<br />
<br />
ET and CT significantly increased oxidative capacity and expression of mitochondrial proteins and transcription factors. All training modalities improved body composition, cardiorespiratory fitness, and skeletal muscle strength. CT induced the most robust improvements in mitochondrial<br />
related outcomes and physical characteristics despite lower training volumes for the ET and RT components. Importantly, most of the adaptations to training occurred independent of age.<br />
<br />
Collectively, these results demonstrate that both ET and CT increase muscle mitochondrial abundance and capacity. Although CT induced the most robust improvements in the outcomesmeasured. In conclusion, CT provides a robust exercise regimen to improve muscle mitochondrial outcomes and physical characteristics independent of age.<br />
|mipnetlab=US PA Danville Irving BA, US MN Rochester Nair KS<br />
}}<br />
{{Labeling<br />
|area=Respiration, mtDNA;mt-genetics, Exercise physiology;nutrition;life style, Patients<br />
|organism=Human<br />
|tissues=Skeletal muscle<br />
|preparations=Isolated mitochondria<br />
|couplingstates=LEAK, OXPHOS, ETS<br />
|substratestates=CI, CII, CIII, CI&II<br />
|instruments=Oxygraph-2k<br />
|additional=MitoFit news, Labels, [Epub ahead of print]<br />
}}<br />
== MitoFit news 2015#7 ==<br />
* 2015-06-09: Combined training and good news for the aging population. »[[MitoFit news]]</div>Bader Helgahttps://wiki.oroboros.at/index.php?title=Capaldi_1973_Biochem_Biophys_Res_Commun&diff=90646Capaldi 1973 Biochem Biophys Res Commun2015-05-29T11:01:15Z<p>Bader Helga: </p>
<hr />
<div>{{Publication<br />
|title=Capaldi RA (1973) On the subunit structure of oligomycin sensitive ATPase. Biochem Biophys Res Commun 53:1331-7.<br />
|info=[http://www.ncbi.nlm.nih.gov/pubmed/4270659 PMID: 4270659]<br />
|authors=Capaldi RA<br />
|year=1973<br />
|journal=Biochem Biophys Res Commun<br />
|abstract=The subunit structure of oligomycin sensitive ATPase has been determined. In addition to the components of F1, and the so-called oligomycin sensitivity conferring protein, there are four other polypeptides of molecular weights 55,000, 29,000, 20,000 and 10,000 which together form the intrinsic membrane portion of the enzymic complex.<br />
|keywords=Oligomycin, ATPase, Subunit structure, Factor 1<br />
}}<br />
{{Labeling<br />
|enzymes=Complex V;ATP synthase<br />
|topics=ATP; ADP; AMP; PCr<br />
|additional=Made history<br />
}}</div>Bader Helgahttps://wiki.oroboros.at/index.php?title=Ragan_1973_J_Biol_Chem&diff=90645Ragan 1973 J Biol Chem2015-05-29T10:53:02Z<p>Bader Helga: </p>
<hr />
<div>{{Publication<br />
|title=Ragan CI, Racker E (1973) Partial resolution of the enzymes catalyzing oxidative phosphorylation XXVII. The reconstitution of the first site of energy conservation. J Biol Chem 248:2563-9.<br />
|info=[http://www.ncbi.nlm.nih.gov/pubmed/4144592?dopt=Abstract PMID: 4144592 Open Access]; [http://www.jbc.org/content/248/7/2563.full.pdf+html PDF]<br />
|authors=Ragan CI, Racker E<br />
|year=1973<br />
|journal=J Biol Chem<br />
|abstract=# The ability to phosphorylate ADP during oxidation of NADH by ubiquinone-1 was restored to the NADH-ubiquinone reductase complex by combining the latter with phospholipids and a hydrophobic protein fraction derived from bovine heart mitochondria.<br />
# Phosphorylation was abolished by rotenone, uncoupling agents, or rutamycin. The efficiency of ATP formation was as high as 0.5 mole per mole of NADH oxidized under optimal conditions.<br />
# Reconstitution of phosphorylation had an absolute requirement for phosphatidylethanolamine and a partial requirement for phosphatidylcholine, a molar ratio of approximately 4:1 being optimal. A much more marked requirement for phosphatidylcholine was observed in the presence of low concentrations of cardiolipin (0.05 to 1.5% of the total phospholipid). In the presence of cardiolipin, an equal molar ratio of phosphatidylethanolamine to phosphatidylcholine gave the highest phosphorylation efficiency.<br />
# The NADH-ubiquinone reductase complex is oriented in the reconstituted vesicles such that approximately 50% of the molecules can react with added NADH. Reaction of all the molecules with NADH occurs in the presence of 0.5% deoxycholate.<br />
# Phosphorylation efficiency can be significantly improved by purification of the vesicles on sucrose density gradients.<br />
|keywords=Oxidative phosphorylation, Energy conservation, Bovine heart submitochondrial particles<br />
}}<br />
{{Labeling<br />
|organism=Bovines<br />
|tissues=Heart<br />
|preparations=Isolated mitochondria<br />
|enzymes=Complex V;ATP synthase<br />
|topics=ATP; ADP; AMP; PCr<br />
|additional=Made history<br />
}}</div>Bader Helgahttps://wiki.oroboros.at/index.php?title=Sauer_1973_Biochem_Biophys_Res_Commun&diff=90643Sauer 1973 Biochem Biophys Res Commun2015-05-29T10:44:36Z<p>Bader Helga: </p>
<hr />
<div>{{Publication<br />
|title=Sauer LA (1973) An NAD- and NADP-dependent malic enzyme with regulatory properties in rat liver and adrenal cortex mitochondrial fractions. Biochem Biophys Res Commun 50:524-31.<br />
|info=[http://www.ncbi.nlm.nih.gov/pubmed/4144006 PMID: 4144006]<br />
|authors=Sauer LA<br />
|year=1973<br />
|journal=Biochem Biophys Res Commun<br />
|abstract=The NAD- and NADP-dependent malic enzymes from rat liver and adrenal mitochondrial fractions were separated and partially purified by gel filtration on Sepharose 6B. Two activity peaks were observed. The first contained a malic enzyme capable of reducing either NAD or NADP. This enzyme showed sigmoid kinetics in plots of activity versus the malate concentration. Succinate was an allosteric activator and ATP was a competitive inhibitor of malate. The second peak showed hyperbolic kinetics in plots of activity versus the malate concentration and was unaffected by either succinate or ATP. The relative activities of the two malic enzymes were quite constant in the adrenal mitochondrial fractions. In the liver mitochondrial fractions, the activity of the first peak varied and was sometimes absent while the activity of the second peak was quite constant. The kinetic properties of the first malic enzyme implicate it as an important regulator of malate oxidation.<br />
}}<br />
{{Labeling<br />
|organism=Rat<br />
|tissues=Nervous system, Liver<br />
|preparations=Enzyme<br />
|additional=Malic enzyme<br />
}}</div>Bader Helgahttps://wiki.oroboros.at/index.php?title=Sauer_1973_FEBS_Lett&diff=90642Sauer 1973 FEBS Lett2015-05-29T10:42:55Z<p>Bader Helga: </p>
<hr />
<div>{{Publication<br />
|title=Sauer LA (1973) Mitochondrial NAD-dependent malic enzyme: a new regulatory enzyme. FEBS Lett 33:251-5.<br />
|info=[http://www.ncbi.nlm.nih.gov/pubmed/4147096 PMID: 4147096 Open Access]<br />
|authors=Sauer LA<br />
|year=1973<br />
|journal=FEBS Lett<br />
}}<br />
{{Labeling<br />
|additional=Made history<br />
}}<br />
== Made history ==<br />
* [[Mitochondria and bioblasts: History]]<br />
* [[Malic enzyme]]</div>Bader Helgahttps://wiki.oroboros.at/index.php?title=Hinkle_1972_J_Biol_Chem&diff=90641Hinkle 1972 J Biol Chem2015-05-29T10:30:32Z<p>Bader Helga: </p>
<hr />
<div>{{Publication<br />
|title=Hinkle PC, Kim JJ, Racker E (1972) Ion transport and respiratory control in vesicles formed from cytochrome oxidase and phospholipids. J Biol Chem 247:1338-9.<br />
|info=[http://www.ncbi.nlm.nih.gov/pubmed/4334497 PMID: 4334497 Open Access]; [http://www.jbc.org/content/247/4/1338.full.pdf+html PDF]<br />
|authors=Hinkle PC, Kim JJ, Racker E<br />
|year=1972<br />
|journal=J Biol Chem<br />
|abstract=Vesicles formed from cytochrome oxidase and phospholipids catalyzed the oxidation of reduced cytochrome c in a manner similar to that of intact mitochondria. A respiration-dependent release of protons and uptake of potassium ions were observed in the presence of valinomycin with reduced 1,4-naphthoquinone-2-sulfonate as reductant for cytochrome c. With ascorbate as reductant 3- to 5-fold stimulation of respiration was observed on addition of uncouplers or ionophorous agents.<br />
|keywords=Ion transport, Respiratory control, Cytochrome oxidase, Phospholipids, Vesicles<br />
}}<br />
{{Labeling<br />
|area=Respiration<br />
|organism=Bovines<br />
|tissues=Heart<br />
|preparations=Isolated mitochondria, SMP<br />
|enzymes=Complex IV;cytochrome c oxidase<br />
|topics=Ion;substrate transport, Substrate<br />
|couplingstates=OXPHOS<br />
|additional=Made history<br />
}}</div>Bader Helgahttps://wiki.oroboros.at/index.php?title=Morris_1972_Brit_J_Hiostory_Sci&diff=90640Morris 1972 Brit J Hiostory Sci2015-05-29T10:15:10Z<p>Bader Helga: </p>
<hr />
<div>{{Publication<br />
|title=Morris RJ (1972) Lavoisier and the caloric theory. Brit J Hiostory Sci 6:1-38.<br />
|info=[http://www.jstor.org/stable/4025260 Brit J Hiostory Sci], [[File:Morris_1972_Brit_J_Hiostory_Sci.pdf]]<br />
|authors=Morris RJ<br />
|year=1972<br />
|journal=Brit J Hiostory Sci<br />
|abstract=Professional historians of science generally recognize the importance of Lavoisier's theory of heat. However, it commonly receives scant Attention in the historical treatment of his chemical theories except perhaps as an example illustrating his conservatism and giving the impression that the caloric theory, although perhaps important in the development of ideas on the nature of heat, is independent of and bears little relationship to his general chemistry or is incidental to an understanding of that chemistry.'<br />
<br />
An examination of Lavoisier's writings suggests that the caloric theory is not merely a milestone in the development of physics; and rather than an omittable appendage, his concept of heat forms an integral part of his chemical system and plays a central, necessary role in his oxidation theory in particular. The purpose of this paper is to give a general description of Lavoisier's ideas on the nature and action of heat, the origin of These ideas, their development, and their relation to his general chemistry, pointing out his conservatism as well as his innovations.<br />
}}<br />
{{Labeling}}<br />
== Link ==<br />
* [[Lavoisier 1783 French Acad Sci|Lavoisier AL, de la Place PS (1783) Mémoir sur la chaleur. Mem Acad R Sci 1780: 355-408. Transl by Guerlac H (1982) Neale Watson, New York.]]</div>Bader Helgahttps://wiki.oroboros.at/index.php?title=Knowles_1971_J_Biol_Chem&diff=90595Knowles 1971 J Biol Chem2015-05-29T07:49:45Z<p>Bader Helga: </p>
<hr />
<div>{{Publication<br />
|title=Knowles AF, Guillory RJ, Racker E (1971) Partial resolution of the enzymes catalyzing oxidative phosphorylation XXIV. A factor required for the binding of mitochondrial adenosine triphosphatase to the inner mitochondrial membrane. J Biol Chem 246:2672-9.<br />
|info=[http://www.ncbi.nlm.nih.gov/pubmed/4251853 PMID: 4251853 Open Access]; [http://www.jbc.org/content/246/8/2672.full.pdf+html PDF]<br />
|authors=Knowles AF, Guillory RJ, Racker E<br />
|year=1971<br />
|journal=J Biol Chem<br />
|abstract=# Submitochondrial particles have been sequentially treated with trypsin, urea, and sonic oscillation at an alkaline pH. These TUA particles required addition of a protein (Fc1) in order to render added ATPase (F1) sensitive to dicyclohexylcarbodiimide. Further resolution was obtained by exposure of TUA particles either to 2 M sodium thiocyanate or to 1.5% silicotungstate. These procedures removed a second soluble protein component (Fc2) which was also required for the sensitivity of ATPase to dicyclohexylcarbodiimide.<br />
# Preparations of Fc2 purified from the sodium thiocyanate extract stimulated the 32Pi-ATP exchange reaction and oxidative phosphorylation in silicotungstate-treated submitochondrial particles.<br />
# Treatment of TUA particles with silicotungstate reduced their ability to bind ATPase (F1). Addition of Fc2 restored the ability to bind ATPase. It is therefore proposed that Fc2 is a component which links the mitochondrial ATP-ase to the inner mitochondrial membrane.<br />
|keywords=Oxidative phosphorylation, Enzymes, ATP, Mitochondrial membrane, Submitochondrial particles<br />
}}<br />
{{Labeling<br />
|topics=ATP; ADP; AMP; PCr<br />
|additional=Made history<br />
}}</div>Bader Helgahttps://wiki.oroboros.at/index.php?title=Racker_1971_J_Biol_Chem&diff=90594Racker 1971 J Biol Chem2015-05-29T07:43:52Z<p>Bader Helga: </p>
<hr />
<div>{{Publication<br />
|title=Racker E, Kandrach A (1971) Reconstitution of the third site of oxidative phosphorylation. J Biol Chem 246:7069-71.<br />
|info=[http://www.ncbi.nlm.nih.gov/pubmed/4331205 PMID: 4331205 Open Access]; [http://www.jbc.org/content/246/22/7069.full.pdf+html PDF]<br />
|authors=Racker E, Kandrach A<br />
|year=1971<br />
|journal=J Biol Chem<br />
|abstract=A complex was reconstituted with hydrophobic proteins from bovine heart mitochondrial membranes, cytochrome c, cytochrome oxidase, phospholipids, and coupling factors. These vesicular structures catalyzed oxidative phosphorylation with reduced N-methylphenazinium methyl sulfate as substrate.<br />
|keywords=Oxidative phosphorylation, Third site, N-methylphenazinium methyl sulfate, Beef heart<br />
}}<br />
{{Labeling<br />
|organism=Bovines, Saccharomyces cerevisiae<br />
|taxonomic group=Fungi<br />
|tissues=Heart<br />
|preparations=Isolated mitochondria<br />
|enzymes=Complex IV;cytochrome c oxidase<br />
|topics=Substrate<br />
|additional=Made history<br />
}}</div>Bader Helgahttps://wiki.oroboros.at/index.php?title=Grav_1970_Eur_J_Biochem&diff=90566Grav 1970 Eur J Biochem2015-05-28T10:22:57Z<p>Bader Helga: </p>
<hr />
<div>{{Publication<br />
|title=Grav HJ, Pedersen JI, Christiansen EN (1970) Conditions ''in vitro'' which affect respiratory control and capacity for respiration-linked phosphorylation in brown adipose tissue mitochondria. Eur J Biochem 12:11-23.<br />
|info=[http://onlinelibrary.wiley.com/doi/10.1111/j.1432-1033.1970.tb00815.x/abstract onlinelibrary.wiley Open Access]<br />
|authors=Grav HJ, Pedersen JI, Christiansen EN<br />
|year=1970<br />
|journal=Eur J Biochem<br />
|abstract=Oxidative phosphorylation in brown adipose tissue mitochondria is greatly influenced by variations in the ''in vitro'' environment. Factors found to be of particular importance were the concentrations of serum albumin, of magnesium and EDTA, and the osmolality and the pH of the medium. The maximal P/O ratios obtained in an isoosmolar medium at pH 6.3, containing 2% serum albumin, 7.5 mM MgCl2, and 7.5 mM EDTA with pyruvate-malate as substrate, and using the glucose-hexokinase trapping system, were 2.8 for newborn guinea-pigs and 2.6 for unweaned rats.<br />
<br />
<br />
Under otherwise equal conditions the P/O ratios obtained with 4-week-old guinea-pigs were higher than those with the newborn.<br />
<br />
<br />
EDTA was a requirement for demonstration of respiratory control in brown adipose tissue mitochondria. Respiration with pyruvate-malate or succinate (+ rotenone), and stimulated by inorganic phosphate and ADP, was found to be sensitive to oligomycin and to carbonyl cyanide phenylhydrazone. However, the small extent of stimulation by the phosphate acceptor system, the incomplete inhibition by oligomycin, and the fact that the respiratory rate after exhaustion of added ADP was higher than that prior to the addition of ADP, suggest that brown adipose tissue mitochondria are loosely coupled.<br />
<br />
<br />
The measured respiratory control ratios all increased from the newborn to the 3-week-old guinea-pigs.<br />
<br />
<br />
Mitochondria from newborn and 6-day-old guinea-pigs exhibited the phenomenon of “reversed acceptor control”. Thus, in the absence of added inorganic phosphate, ADP inhibited the respiration with pyruvate-malate or with succinate. The reversed ADP control was abolished by carbonyl cyanide phenylhydrazone, but was not suppressed by treatment of the mitochondria with oligomycin.<br />
<br />
<br />
Inorganic phosphate affects respiration in a composite manner. With all of the preparations tested, inorganic phosphate stimulated respiration whether exogenous ADP was present or not. In the absence of added ADP, the respiration initially stimulated by inorganic phosphate entered a subsequent inhibitory phase.<br />
<br />
<br />
The implications of these findings to the control of brown adipose tissue thermogenesis are discussed.<br />
}}<br />
{{Labeling<br />
|organism=Guinea pig<br />
|tissues=Fat<br />
|preparations=Isolated mitochondria<br />
|topics=ATP; ADP; AMP; PCr<br />
|couplingstates=LEAK, OXPHOS, ETS<br />
|substratestates=CI, CII<br />
|additional=Succinate, P/O ratio, Magnesium, Ontogenesis, ADP, ATP, Phosphate<br />
}}</div>Bader Helgahttps://wiki.oroboros.at/index.php?title=Klingenberg_1970_Eur_J_Biochem&diff=90565Klingenberg 1970 Eur J Biochem2015-05-28T10:20:37Z<p>Bader Helga: </p>
<hr />
<div>{{Publication<br />
|title=Klingenberg M (1970) Localization of the glycerol-phosphate dehydrogenase in the outer phase of the mitochondrial inner membrane. Eur J Biochem 13:247-52.<br />
|info=[http://www.ncbi.nlm.nih.gov/pubmed/5439930 PMID: 5439930]<br />
|authors=Klingenberg M<br />
|year=1970<br />
|journal=Eur J Biochem<br />
|abstract=Evidence for the localization of the [[Glycerophosphate dehydrogenase complex |mitochondrial glycerol-phosphate dehydrogenase]] in the outer phase of the inner membrane is presented.<br />
# Glycerol-phosphate does not permeate through the inner membrane to the matrix space in a number of mitochondria which actively oxidize glycerol-phosphate.<br />
# The impermeability of the inner membrane to ferricyanide is demonstrated and this forms a basis for elucidating membrane localization of carriers.<br />
# In mitochondria from various tissues ferricyanide can interact directly with glycerolphosphate dehydrogenase but not with succinate dehydrogenase.<br />
# The oxidation of glycerol-phosphate, in contrast to that of succinate, is insensitive to substrate depletion brought about by uncouplers.<br />
# The results are interpreted to show that both the substrate and the acceptor-site of glycerol-phosphate dehydrogenase are exposed to the outer side of the inner membrane. Thus, for the operation of the glycerol-phosphate dehydrogenase, mitochondria do not require translocases for glycerol-phosphate and dihydroxyacetone-phosphate.<br />
}}<br />
{{Labeling<br />
|area=Respiration<br />
|preparations=Isolated mitochondria<br />
|enzymes=Complex II;succinate dehydrogenase<br />
|topics=Uncoupler<br />
|couplingstates=ETS<br />
|substratestates=CGpDH<br />
|additional=Glycerol-phosphate dehydrogenase, Uncoupler<br />
}}</div>Bader Helgahttps://wiki.oroboros.at/index.php?title=MacLennan_1968_Biochemistry&diff=90564MacLennan 1968 Biochemistry2015-05-28T10:18:22Z<p>Bader Helga: </p>
<hr />
<div>{{Publication<br />
|title=MacLennan DH, Tzagoloff A (1968) Studies on the mitochondrial adenosine triphosphatase system IV. Purification and characterization of the oligomycin sensitivity conferring protein. Biochemistry 7:1603-10.<br />
|info=[http://www.ncbi.nlm.nih.gov/pubmed/4234149 PMID: 4234149]<br />
|authors=MacLennan DH, Tzagoloff A<br />
|year=1968<br />
|journal=Biochemistry<br />
|keywords=ATP system IV, Oligomycin<br />
}}<br />
{{Labeling<br />
|topics=ATP; ADP; AMP; PCr<br />
|additional=Made history<br />
}}</div>Bader Helgahttps://wiki.oroboros.at/index.php?title=Schnaitman_1968_J_Cell_Biol&diff=90563Schnaitman 1968 J Cell Biol2015-05-28T10:17:50Z<p>Bader Helga: </p>
<hr />
<div>{{Publication<br />
|title=Schnaitman C, Greenawalt JW (1968) Enzymatic properties of the inner and outer membranes of rat liver mitochondria. J Cell Biol 38:158-75.<br />
|info=[http://www.ncbi.nlm.nih.gov/pubmed/5691970 PMID: 5691970 Open Access]<br />
|authors=Schnaitman C, Greenawalt JW<br />
|year=1968<br />
|journal=J Cell Biol<br />
|abstract=Treatment of rat liver mitochondria with digitonin followed by differential centrifugation was used to resolve the intramitochondrial localization of both soluble and particulate enzymes. Rat liver mitochondria were separated into three fractions: inner membrane plus matrix, outer membrane, and a soluble fraction containing enzymes localized between the membranes plus some solublized outer membrane. Monoamine oxidase, kynurenine hydroxylase, and rotenone-insensitive NADH-cytochrome c reductase were found primarily in the outer membrane fraction. Succinate-cytochrome c reductase, succinate dehydrogenase, cytochrome oxidase, β-hydroxybutyrate dehydrogenase, α-ketoglutarate dehydrogenase, lipoamide dehydrogenase, NAD- and NADH-isocitrate dehydrogenase, glutamate dehydrogenase, aspartate aminotransferase, and ornithine transcarbamoylase were found in the inner membrane-matrix fraction. Nucleoside diphosphokinase was found in both the outer membrane and soluble fractions; this suggests a dual localization. Adenylate kinase was found entirely in the soluble fraction and was released at a lower digitonin concentration than was the outer membrane; this suggests that this enzyme is localized between the two membranes. The inner membrane-matrix fraction was separated into inner membrane and matrix by treatment with the nonionic detergent Lubrol, and this separation was used as a basis for calculating the relative protein content of the mitochondrial components. The inner membrane-matrix fraction retained a high degree of morphological and biochemical integrity and exhibited a high respiratory rate and respiratory control when assayed in a sucrose-mannitol medium containing EDTA.<br />
|keywords=Mitochondrial membranes, Enzymatic properties<br />
}}<br />
{{Labeling<br />
|organism=Rat<br />
|tissues=Liver<br />
|preparations=Isolated mitochondria<br />
|enzymes=Marker enzyme<br />
|additional=Made history<br />
}}</div>Bader Helgahttps://wiki.oroboros.at/index.php?title=Mitchell_1969_Eur_J_Biochem&diff=90562Mitchell 1969 Eur J Biochem2015-05-28T10:16:31Z<p>Bader Helga: </p>
<hr />
<div>{{Publication<br />
|title=Mitchell P, Moyle J (1969) Estimation of membrane potential and pH difference across the cristae membrane of rat liver mitochondria. Eur J Biochem 7:471-84.<br />
|info=[http://www.ncbi.nlm.nih.gov/pubmed/5776240 PMID: 5776240]<br />
|authors=Mitchell P, Moyle J<br />
|year=1969<br />
|journal=Eur J Biochem<br />
|abstract=The cristae membrane or M phase of resting or respiring rat liver mitochondria becomes relatively permeable to K<sup>+</sup> ions in presence of valinomycin. The equilibrium distribution of K<sup>+</sup> ions across the membrane can therefore be used to estimate the membrane potential ΔΨ provided that precautions are taken to minimise swelling of the valinomycin-treated mitochondria. The pH difference ΔpH across the M phase of anaerobic mitochondria has been estimated from the buffering powers of the inner and outer phases and from the change of pH observed on lysing the mitochondria with Triton X-100. When the anaerobic mitochondria (State 5), in presence of β-hydroxybutyrate, are brought to a state of steady respiration either in absence (State 4) or in presence (State 3) of phosphate acceptor, the changes of pH and of pK of the medium recorded with H<sup>+</sup> ion-sensitive and K<sup>+</sup> ion-sensitive electrodes can be used to estimate the changes of ΔΨ and ΔpH across the M phase. The absolute values of ΔΨ and ΔpH have been estimated from the values determined in State 5 and the change of these values in the transition from State 5 to States 4 and 3.<br />
<br />
Continued in Free Text<br />
|keywords=Membrane potential, pH difference, Cristae membrane, Valinomycin, K<sup>+</sup> ions<br />
}}<br />
{{Labeling<br />
|area=Respiration<br />
|organism=Rat<br />
|tissues=Liver<br />
|preparations=Isolated mitochondria<br />
|topics=Coupling efficiency;uncoupling, Ion;substrate transport, mt-Membrane potential, pH<br />
|couplingstates=OXPHOS<br />
|additional=Made history<br />
}}<br />
Abstract Continued<br />
<br />
The total protonmotive force Δp =ΔΨ– 59 ΔpH across the M phase of the mitochondria oxidising β-hydroxybutyrate in State 4 at 25° in a 250 mM sucrose medium near pH 7 is estimated to be about 230 mV, of which the major component is ΔΨ when the effect of translocation of K<sup>+</sup> ions across the M phase is minimised. Under conditions permitting accumulation of a relatively large quantity of cation (State 6), Δp is not significantly different from that in State 4, but the major component is −ZΔpH.<br />
<br />
The effects of changing Δp in mitochondrial suspensions in State 4 with uncoupling agent and with pulses of acid, alkali, calcium salt and ADP have been found to be in accord with the chemiosmotic hypothesis. In particular Δp in State 3 (ADP and Pi present) is estimated to be about 30 mV less than in State 4.</div>Bader Helgahttps://wiki.oroboros.at/index.php?title=Tuena_1969_Eur_J_Biochem&diff=90561Tuena 1969 Eur J Biochem2015-05-28T10:15:53Z<p>Bader Helga: </p>
<hr />
<div>{{Publication<br />
|title=Tuena M, Gómez-Puyou A, Peña A, Chávez E, Sandoval F (1969) Effect of ATP on the oxidation of succinate in rat brain mitochondria. Eur J Biochem 11:283-90.<br />
|info=[http://www.ncbi.nlm.nih.gov/pubmed/?term=PMID%3A+5360409 PMID: 5360409]<br />
|authors=Tuena M, Gomez-Puyou A, Pena A, Chavez E, Sandoval F<br />
|year=1969<br />
|journal=Eur J Biochem<br />
}}<br />
{{Labeling<br />
|organism=Rat<br />
|tissues=Nervous system<br />
|preparations=Isolated mitochondria<br />
|substratestates=CII<br />
|additional=Succinate, ATP<br />
}}</div>Bader Helgahttps://wiki.oroboros.at/index.php?title=Estabrook_1967_Methods_Enzymol&diff=90560Estabrook 1967 Methods Enzymol2015-05-28T10:14:14Z<p>Bader Helga: </p>
<hr />
<div>{{Publication<br />
|title=Estabrook RW (1967) Mitochondrial respiratory control and the polarographic measurement of ADP:O ratios. Methods Enzymol 10:41-7.<br />
|info=[http://www.sciencedirect.com/science/article/pii/0076687967100104 ScienceDirect]<br />
|authors=Estabrook RW<br />
|year=1967<br />
|journal=Methods Enzymol<br />
|abstract=.. The convenience and simplicity of the polarographic 'oxygen electrode' technique for measuring rapid changes in the rate of oxygen utilization by cellular and subcellular systems is now leading to its more general application in many laboratories. The types and design of oxygen electrodes vary, depending on the invetigator's ingenuity and specific requirements of the system under investigation.<br />
}}<br />
{{Labeling<br />
|area=Respiration<br />
|tissues=Liver<br />
|preparations=Isolated mitochondria<br />
|couplingstates=LEAK, OXPHOS<br />
|additional=Respiration, Made history<br />
}}<br />
''Publisher Summary''<br />
<br />
This chapter discusses the mitochondrial respiratory control and the polarographic measurement of ADP : O ratios. The polarographic oxygen electrode technique is used for measuring rapid changes in the rate of oxygen utilization by cellular and subcellular systems. Although the polarographic method measures changes in oxygen concentration of photosynthetic systems, yeast cells, and nerve, but the oxygen electrode technique is applied to a study the mitochondrial respiration and oxidative phosphorytation. The principle of the oxygen electrode has been summarized, and the design of the vibrating oxygen electrode for use with speetrophotometric studies is illustrated. The oxygen electrode apparatus can be calibrated in a number of ways. A more accurate calibration of oxygen content can be obtained by gas equilibration with various nitrogen-oxygen mixtures. When tightly coupled mitochondria are suspended in an isotonic buffer, a slow rate of oxygen uptake is measured in the presence of substrate and absence of ADP. Addition of ADP causes an immediate increase in the rate of oxygen utilization. The concentration of oxygen utilized is proportional to the amount of ADP phosphorylated to ATP. The type of oxygen electrode tracings is presented from which an ADP : O ratio (equivalent to a P : O ratio) can be directly calculated.</div>Bader Helgahttps://wiki.oroboros.at/index.php?title=Schnaitman_1967_J_Cell_Biol&diff=90559Schnaitman 1967 J Cell Biol2015-05-28T10:11:02Z<p>Bader Helga: </p>
<hr />
<div>{{Publication<br />
|title=Schnaitman C, Erwin VG, Greenawalt JW (1967) The submitochondrial localization of monoamine oxidase. An enzymatic marker for the outer membrane of rat liver mitochondria. J Cell Biol 32:719-35.<br />
|info=[http://www.ncbi.nlm.nih.gov/pubmed/4291912 PMID: 4291912 Open Access]<br />
|authors=Schnaitman C, Erwin VG, Greenawalt JW<br />
|year=1967<br />
|journal=J Cell Biol<br />
|abstract=Controlled osmotic lysis (water-washing) of rat liver mitochondria results in a mixed population of small vesicles derived mainly from the outer mitochondrial membrane and of larger bodies containing a few cristae derived from the inner membrane. These elements have been separated on Ficoll and sucrose gradients. The small vesicles were rich in monoamine oxidase, and the large bodies were rich in cytochrome oxidase. Separation of the inner and outer membranes has also been accomplished by treating mitochondria with digitonin in an isotonic medium and fractionating the treated mitochondria by differential centrifugation. Treatment with low digitonin concentrations released monoamine oxidase activity from low speed mitochondrial pellets, and this release of enzymatic activity was correlated with the loss of the outer membrane as seen in the electron microscope. The low speed mitochondrial pellet contained most of the cytochrome oxidase and malate dehydrogenase activities of the intact mitochondria, while the monoamine oxidase activity could be recovered in the form of small vesicles by high speed centrifugation of the low speed supernatant. The results indicate that monoamine oxidase is found only in the outer mitochondrial membrane and that cytochrome oxidase is found only in the inner membrane. Digitonin treatment released more monoamine oxidase than cytochrome oxidase from sonic particles, thus indicating that digitonin preferentially degrades the outer mitochondrial membrane.<br />
|keywords=Monoamine oxidase, Outer mitochondrial membrane<br />
}}<br />
{{Labeling<br />
|organism=Rat<br />
|tissues=Liver<br />
|preparations=Isolated mitochondria<br />
|enzymes=Marker enzyme<br />
|additional=Made history<br />
}}</div>Bader Helgahttps://wiki.oroboros.at/index.php?title=Sottocasa_1967_J_Cell_Biol&diff=90558Sottocasa 1967 J Cell Biol2015-05-28T10:09:52Z<p>Bader Helga: </p>
<hr />
<div>{{Publication<br />
|title=Sottocasa GL, Kuylenstierna, Ernster L, Bergstrand A (1967) An electron-transport system associated with the outer membrane of liver mitochondria. A biochemical and morphological study. J Cell Biol 32:415-38.<br />
|info=[http://www.ncbi.nlm.nih.gov/pubmed/10976232 PMID: 10976232 Open Access]<br />
|authors=Sottocasa GL, Kuylenstierna, Ernster L, Bergstrand A<br />
|year=1967<br />
|journal=J Cell Biol<br />
|abstract=Preparations of rat-liver mitochondria catalyze the oxidation of exogenous NADH by added cytochrome c or ferricyanide by a reaction that is insensitive to the respiratory chain inhibitors, antimycin A, amytal, and rotenone, and is not coupled to phosphorylation. Experiments with tritiated NADH are described which demonstrate that this "external" pathway of NADH oxidation resembles stereochemically the NADH-cytochrome c reductase system of liver microsomes, and differs from the respiratory chain-linked NADH dehydrogenase. Enzyme distributation data are presented which substantiate the conclusion that microsomal contamination cannot account for the rotenone-insensitive NADH-cytochrome c reductase activity observed with the mitochondria. A procedure is developed, based on swelling and shrinking of the mitochondria followed by sonication and density gradient centrifugation, which permits the separation of two particulate subfractions, one containing the bulk of the respiratory chain components, and the other the bulk of the rotenone-insensitive NADH-cytochrome c reductase system. Morphological evidence supports the conclusion that the former subfraction consists of mitochondria devoid of outer membrane, and that the latter represents derivatives of the outer membrane. The data indicate that the electron-transport system associated with the mitochondrial outer membrane involves catalytic components similar to, or identical with, the microsomal NADH-cytochrome b5 reductase and cytochrome b5.<br />
|keywords=Mitochondrial outer membrane, Electron transport, NADH<br />
}}<br />
{{Labeling<br />
|organism=Rat<br />
|tissues=Liver<br />
|preparations=Isolated mitochondria<br />
|enzymes=Complex IV;cytochrome c oxidase<br />
|additional=Made history<br />
}}</div>Bader Helgahttps://wiki.oroboros.at/index.php?title=Jagendorf_1966_Proc_Natl_Acad_Sci_USA&diff=90557Jagendorf 1966 Proc Natl Acad Sci USA2015-05-28T10:07:56Z<p>Bader Helga: </p>
<hr />
<div>{{Publication<br />
|title=Jagendorf AT, Uribe E (1966) ATP formation caused by acid-base transition of spinach chloroplasts. Proc Natl Acad Sci USA 55:170-7.<br />
|info=[http://www.ncbi.nlm.nih.gov/pubmed/5220864 PMID: 5220864 Open Access]; [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC285771/pdf/pnas00140-0184.pdf PDF]<br />
|authors=Jagendorf AT, Uribe E<br />
|year=1966<br />
|journal=Proc Natl Acad Sci USA<br />
|abstract=Chloroplasts form a limited amount of ATP without illumination or oxygen if made first acid, then basic. The yields are greatly increased by having an appropriate organic acid present in the acid stage. Lack of specificity of the acid suggests it does not serve as a substrate for a specific enzyme. The highest yields obtained regularly have been 1 ATP for every 4 chlorophylls (i.e., 100 ATP per cytochrome f, or 40 µmoles ATP per gram of protein). Formation of ATP is sensitive to known uncouplers of photosynthetic phosphorylation, and the kinetics of either decay of the intermediate or of phosphorylation at pH 8 are the same as those for the high-energy condition induced by illumination at pH 6. The yield of ATP depends in part on the actual pH differential between the two experimental stages. The data are suggested to be consistent with a model in which the high energy condition consists of a pH gradient across the grana disk membranes.<br />
|keywords=ATP formation, Acid-base transition, Chloropplasts<br />
}}<br />
{{Labeling<br />
|taxonomic group=Plants<br />
|preparations=Chloroplasts<br />
|topics=ATP; ADP; AMP; PCr, Coupling efficiency;uncoupling, mt-Membrane potential, pH<br />
|additional=Made history<br />
}}</div>Bader Helgahttps://wiki.oroboros.at/index.php?title=Lee_1964_Biochim_Biophys_Acta&diff=90556Lee 1964 Biochim Biophys Acta2015-05-28T10:03:54Z<p>Bader Helga: </p>
<hr />
<div>{{Publication<br />
|title=Lee CP, Ernster L (1964) Equilibrium studies of the energy-dependent and non-energy-dependent pyridine nucleotide transhydrogenase reactions. Biochim Biophys Acta 81:187-90.<br />
|info=[http://www.sciencedirect.com/science/article/pii/0926656964903530 ScienceDirect]<br />
|authors=Lee CP, Ernster L<br />
|year=1964<br />
|journal=Biochim Biophys Acta<br />
|abstract=No Abstract supplied.<br />
|keywords=Pyridine nucleotide transhydrogenase<br />
}}<br />
{{Labeling<br />
|additional=Made history<br />
}}</div>Bader Helgahttps://wiki.oroboros.at/index.php?title=Lee_1964_Nature&diff=90555Lee 1964 Nature2015-05-28T10:02:02Z<p>Bader Helga: </p>
<hr />
<div>{{Publication<br />
|title=Lee CP, Azzone GF, Ernster L (1964) Evidence for energy-coupling in non-phosphorylating electron transport particles from beef-heart mitochondria. Nature 201:152-5.<br />
|info=[http://www.ncbi.nlm.nih.gov/pubmed?term=Lee%20CP%2C%20Azzone%20GF%2C%20Ernster%20L PMID: 14118261]<br />
|authors=Lee CP, Azzone GF, Ernster L<br />
|year=1964<br />
|journal=Nature<br />
|abstract=No Abstract supplied.<br />
|keywords=Energy coupling, Non-phosphorylating electron transport<br />
}}<br />
{{Labeling<br />
|organism=Bovines<br />
|tissues=Heart<br />
|preparations=Isolated mitochondria<br />
|additional=Made history<br />
}}</div>Bader Helgahttps://wiki.oroboros.at/index.php?title=Moore_1964_Biochem_Biophys_Res_Commun&diff=90554Moore 1964 Biochem Biophys Res Commun2015-05-28T10:01:28Z<p>Bader Helga: </p>
<hr />
<div>{{Publication<br />
|title=Moore C, Pressman BC (1964) Mechanism of action of valinomycin on mitochondria. Biochem Biophys Res Commun 15:562-7.<br />
|info=[http://www.sciencedirect.com/science/article/pii/0006291X64905054 ScienceDirect]<br />
|authors=Moore C, Pressman BC<br />
|year=1964<br />
|journal=Biochem Biophys Res Commun<br />
|abstract=No Abstract supplied.<br />
|keywords=Valinomycin, Mitochondria<br />
}}<br />
{{Labeling<br />
|additional=Made history<br />
}}</div>Bader Helgahttps://wiki.oroboros.at/index.php?title=Mueller_1964_J_Chem_Educ&diff=90553Mueller 1964 J Chem Educ2015-05-28T09:58:54Z<p>Bader Helga: </p>
<hr />
<div>{{Publication<br />
|title=Mueller OH (1964) The development of polarography and polarographic instruments. J Chem Educ 41:320.<br />
|info=[http://pubs.acs.org/doi/abs/10.1021/ed041p320 J Chem Educ]<br />
|authors=Muller OH<br />
|year=1964<br />
|journal=J Chem Educ<br />
|abstract=Dr. Jaroslav Heyrovskj, of the Charles' University of Prague, published in 1922 his first paper on studies with a dropping mercury electrode. This led to the development of polarography, a basically new method of analysis, that eventually won him a Nobel Prize in 1959. However, the origins of polarography may be traced back to 1873 when Lippmann designed his capillary electrometer.<br />
|keywords=Respirometry, History<br />
}}<br />
{{Labeling<br />
|area=Instruments;methods<br />
}}</div>Bader Helgahttps://wiki.oroboros.at/index.php?title=Oesper_1964_J_Chem_Educ&diff=90552Oesper 1964 J Chem Educ2015-05-28T09:58:26Z<p>Bader Helga: </p>
<hr />
<div>{{Publication<br />
|title=Oesper P (1964) The history of the Warburg apparatus: Some reminiscences on its use. J Chem Educ 41:294.<br />
|info=[http://pubs.acs.org/doi/abs/10.1021/ed041p294 DOI: 10.1021/ed041p294]<br />
|authors=Oesper P<br />
|year=1964<br />
|journal=J Chem Educ<br />
|abstract=The Warburg apparatus is a device for measuring the pressure of a gas at constant volume and constant temperature so that the pressure is a measure of the quantity of gas and changes in pressure reflect the production or absorption of gas. <br />
<br />
|keywords=Respirometry, History<br />
}}<br />
{{Labeling<br />
|area=Instruments;methods<br />
}}<br />
* See [http://www.oroboros.at/index.php?respirometry-history Warburg apparatus @OROBOROS].</div>Bader Helgahttps://wiki.oroboros.at/index.php?title=Danielson_1963_Biochem_Z&diff=90550Danielson 1963 Biochem Z2015-05-28T09:40:58Z<p>Bader Helga: </p>
<hr />
<div>{{Publication<br />
|title=Danielson L, Ernster L (1963) Energy-dependent reduction of triphosphopyridine nucleotide by reduced diphosphopyridine nucleotide, coupled to the energy-transfer system of the respiratory chain. Biochem Z 338:188-205.<br />
|info=[http://www.ncbi.nlm.nih.gov/pubmed/14087291 PMID: 14087291]<br />
|authors=Danielson L, Ernster L<br />
|year=1963<br />
|journal=Biochem Z<br />
|abstract=No Abstract supplied.<br />
|keywords=Triphosphopyridine nucleotide, Diphosphopyridine nucleotide, Energy-transfer, Respiratory chain<br />
}}<br />
{{Labeling<br />
|couplingstates=OXPHOS<br />
|additional=Made history<br />
}}</div>Bader Helgahttps://wiki.oroboros.at/index.php?title=Klingenberg_1963_Biochem_Z&diff=90549Klingenberg 1963 Biochem Z2015-05-28T09:40:16Z<p>Bader Helga: </p>
<hr />
<div>{{Publication<br />
|title=Klingenberg M, von Haefen H (1963) Hydrogen pathway in mitochondria I. Hydrogen transfer from succinate to acetoacetate. Biochem Z 337:120-45.<br />
|info=[http://www.ncbi.nlm.nih.gov/pubmed?term=Klingenberg%20M%2C%20Hafen%20H PMID: 14033543]<br />
|authors=Klingenberg M, von Haefen H<br />
|year=1963<br />
|journal=Biochem Z<br />
|abstract=No Abstract supplied.<br />
|keywords=Hydrogen, Succinate, Acetoacetate<br />
}}<br />
{{Labeling<br />
|enzymes=Complex II;succinate dehydrogenase<br />
|additional=Made history<br />
}}</div>Bader Helgahttps://wiki.oroboros.at/index.php?title=Lehninger_1963_Biochem_Biophys_Res_Commun&diff=90548Lehninger 1963 Biochem Biophys Res Commun2015-05-28T09:39:45Z<p>Bader Helga: </p>
<hr />
<div>{{Publication<br />
|title=Lehninger AL, Rossi CS, Greenawalt JW (1963) Respiration-dependent accumulation of inorganic phosphate and Ca<sup>2+</sup> ions by rat liver mitochondria. Biochem Biophys Res Commun 10:444-8.<br />
|info=[http://www.ncbi.nlm.nih.gov/pubmed/13929376 PMID: 13929376]<br />
|authors=Lehninger AL, Rossi CS, Greenawalt JW<br />
|year=1963<br />
|journal=Biochem Biophys Res Commun<br />
|abstract=No Abstract<br />
|keywords=Inorganic phosphate, Calcium ions<br />
}}<br />
{{Labeling<br />
|area=Respiration<br />
|organism=Rat<br />
|tissues=Liver<br />
|topics=Calcium, Ion;substrate transport, Pi<br />
|couplingstates=OXPHOS<br />
|additional=Made history<br />
}}</div>Bader Helgahttps://wiki.oroboros.at/index.php?title=Rossi_1963_Biochem_Z&diff=90547Rossi 1963 Biochem Z2015-05-28T09:38:02Z<p>Bader Helga: </p>
<hr />
<div>{{Publication<br />
|title=Rossi CS, Lehninger AL (1963) Stoichiometric relationships between accumulation of ions by mitochondria and the energy-coupling sites in the respiratory chain. Biochem Z 338:698-713.<br />
|info=[http://www.ncbi.nlm.nih.gov/pubmed/14087335 PMID: 14087335]<br />
|authors=Rossi CS, Lehninger AL<br />
|year=1963<br />
|journal=Biochem Z<br />
|abstract=No Abstract supplied.<br />
|keywords=Stoichiometry, Ion accumulation, Energy-coupling sites, Respiratory chain<br />
}}<br />
{{Labeling<br />
|additional=Made history<br />
}}</div>Bader Helgahttps://wiki.oroboros.at/index.php?title=Hatefi_1962_J_Biol_Chem-XLI&diff=90546Hatefi 1962 J Biol Chem-XLI2015-05-28T09:33:25Z<p>Bader Helga: </p>
<hr />
<div>{{Publication<br />
|title=Hatefi Y, Haavik AG, Griffiths DE (1962) Studies on the electron transfer system XLI. Reduced coenzyme Q (QH2)-cytochrome c reductase. J Biol Chem 237:1681-5.<br />
|info=[http://www.ncbi.nlm.nih.gov/pubmed/13905328 PMID: 13905328 Open Access]; [http://www.jbc.org/content/237/5/1681.long PDF]<br />
|authors=Hatefi Y, Haavik AG, Griffiths DE<br />
|year=1962<br />
|journal=J Biol Chem<br />
|abstract=The preparation from beef heart mitochondria and the properties, of a highly active and stable enzyme system, capable of catalyzing the reduction of cytochrome c by reduced coenzyme Q2 are described. The enzyme complex contains cytochrome b and cytochrome c1 in high concentration, and is free of cytochrome c oxidase, cytochrome c, flavoproteins, and the citric acid cycle dehydrogenases. The activity of the enzyme corresponds to a QO2, of about 320,000 at 38°. This activity is strongly inhibited by antimycin A, 2-nonyl-4-hydroxy-quinoline-N-oxide, and 2-alkyl-3-hydroxynaphthoquinone. Amytal, thenoyltrifluoroacetone, and a number of specific metal-chelating compounds are ineffective as inhibitors.<br />
|keywords=[[Q-junction]], Coenzyme Q, Reduced coenzyme Q (QH2), Cytochrome c reductase, Beef heart<br />
}}<br />
{{Labeling<br />
|organism=Bovines<br />
|tissues=Heart<br />
|preparations=Isolated mitochondria<br />
|enzymes=Complex IV;cytochrome c oxidase<br />
|topics=Substrate<br />
|couplingstates=ETS<br />
|additional=Made history<br />
}}</div>Bader Helgahttps://wiki.oroboros.at/index.php?title=Kuboyama_1962_Biochem_Biophys_Res_Commun-IX&diff=90545Kuboyama 1962 Biochem Biophys Res Commun-IX2015-05-28T09:30:09Z<p>Bader Helga: </p>
<hr />
<div>{{Publication<br />
|title=Kuboyama M, Takemori S, King TE (1962) Reconstitution of respiratory chain enzyme systems IX. Cytochrome c-cytochrome oxidase complex of heart muscle. Biochem Biophys Res Commun 9:534-9.<br />
|info=[http://www.ncbi.nlm.nih.gov/pubmed/13927261 PMID: 13927261]<br />
|authors=Kuboyama M, Takemori S, King TE<br />
|year=1962<br />
|journal=Biochem Biophys Res Commun<br />
|abstract=No Abstract supplied.<br />
|keywords=Cytochrome c, Cytochrome oxidase<br />
}}<br />
{{Labeling<br />
|tissues=Heart<br />
|enzymes=Complex IV;cytochrome c oxidase<br />
|topics=Cyt c<br />
|additional=Made history<br />
}}</div>Bader Helgahttps://wiki.oroboros.at/index.php?title=Schwartz_1962_Circ_Res&diff=90544Schwartz 1962 Circ Res2015-05-28T09:26:54Z<p>Bader Helga: </p>
<hr />
<div>{{Publication<br />
|title=Schwartz A, Lee KS (1962) Study of heart mitochondria and glycolytic metabolism in experimentally induced cardiac failure. Circ Res 10:321-32.<br />
|info=[http://www.ncbi.nlm.nih.gov/pubmed/13909670 PMID: 13909670 Open Access]<br />
|authors=Schwartz A, Lee KS<br />
|year=1962<br />
|journal=Circ Res<br />
}}<br />
{{Labeling<br />
|area=mt-Awareness<br />
|organism=Guinea pig<br />
|tissues=Heart<br />
|preparations=Isolated mitochondria<br />
}}<br />
'''Abstract'''<br />
<br />
Studies were made on the biochemical activity of mitochondria and of homogenates obtained from normal hearts and from hearts after experimentally induced failure. The principal types of failure investigated were: "chronic" congestive failure and acute failure in the guinea pig. The "chronic" failure was induced in from 2 to 10 days by a partial constriction of the ascending aorta, while the acute type of failure was induced by a more severe aortic constriction of a similar type. Various physiological parameters were studied. The "chronic" animals exhibited tachycardia, elevated right ventricular systolic pressure and a significant depression of myocardial contractility. In addition, a highly significant increase in cardiac tissue mass was observed. Passive congestion of the liver, spleen, kidneys, and lungs was evident.<br />
<br />
Mitochondria isolated from the hearts of guinea pigs in "chronic" failure exhibited a significant depression of metabolic activity. Thus phosphorylation associated with the oxidation of glutamate, succinate, or α-ketoglutarate was uncoupled in mitochondria isolated from the "failed" heart. Cardiac glycosides administered to animals with experimental cardiac failure did not alter the uncoupled state of the mitochondria, although these agents effected a significant improvement in cardiac contractility. The ATPase activity of the "failed" mitochondria was normal. Experiments concerning the localization of the site or sites of uncoupling of oxidative phosphorylation in the "failed" mitochondria revealed that the defect probably resided in the phosphorylation step associated with the electron transfer between cytochrome C to oxygen.<br />
<br />
Homogenates prepared from hearts of chronically failing animals were markedly depressed with respect to oxygen and glucose consumption and lactic acid formation.<br />
<br />
Mitochondria isolated from acutely failed guinea pig hearts exhibited a "mild" uncoupling of oxidative phosphorylation manifested as a decrease in responsiveness to a phosphate acceptor system. This was a graded effect, increasing in severity with increasing duration of aortic constriction.<br />
<br />
On the basis of the present study, it is possible that uncoupling of oxidative phosphorylation in heart mitochondria may play a role in the development of congestive cardiac failure.</div>Bader Helgahttps://wiki.oroboros.at/index.php?title=Vasington_1962_J_Biol_Chem&diff=90542Vasington 1962 J Biol Chem2015-05-28T09:23:35Z<p>Bader Helga: </p>
<hr />
<div>{{Publication<br />
|title=Vasington FD, Murphy JV (1962) Ca<sup>++</sup> uptake by rat kidney mitochondria and its dependence on respiration and phosphorylation. J Biol Chem 237:2670-7.<br />
|info=[http://www.ncbi.nlm.nih.gov/pubmed/13925019?dopt=Abstract PMID: 13925019 Open Access]; [http://www.jbc.org/content/237/8/2670.full.pdf+html PDF]<br />
|authors=Vasington FD, Murphy JV<br />
|year=1962<br />
|journal=J Biol Chem<br />
|abstract=Rat kidney mitochondria bind large quantities of Ca<sup>++</sup>. Maximal Ca<sup>++</sup> binding requires the presence o f a respiratory substrate such as isocitrate or succinate, as well as adenosine triphosphate (ATP), inorganic orthophosphate (Pi), and Mg<sup>++</sup>. No Ca<sup>++</sup> is bound in the absence of ATP, whereas if Pi or Mg<sup>++</sup> is omitted, the amount of Ca<sup>++</sup> bound is decreased 40 to 70%. Adenosine diphosphate (ADP) can substitute partially for ATP, presumably through formation of ATP by adenylate kinase, but other nucleoside di- and triphosphates tested are essentially inactive.<br />
<br />
Respiratory inhibitors such as Amytal, antimycin A, cyanide, and azide inhibit Ca<sup>++</sup> binding, as do uncoupling agents such as dinitrophenol, dicoumarol, and gramicidin. Significantly, Ca<sup>++</sup> is bound by mitochondria even in the presence of uncoupling quantities of Ca<sup>++</sup>. Dinitrophenol and other uncoupling agents therefore block Ca<sup>++</sup> binding under conditions in which phosphorylation is already uncoupled by Ca<sup>++</sup>. <br />
<br />
Endogenous Ca<sup>++</sup> is released from mitochondria incubated in the absence of ATP or ADP or in the presence of antimycin A, dinitrophenol, or HgC12, suggesting that similar factors influence the retention of endogenous Ca<sup>++</sup> and the uptake of exogenous Ca<sup>++</sup>. Ca<sup>++</sup> binding is stimulated by 0.05 to 0.15 M Na<sup>+</sup> or K<sup>+</sup> and 0.05 to 0.25 M Li<sup>+</sup>, whereas NH4<sup>+</sup>, Rb<sup>+</sup>, and Cs<sup>+</sup> have little effect or are inhibitory at these concentrations; at higher concentrations, all of the alkali metal cations become inhibitory.<br />
|keywords=Ca<sup>++</sup> uptake, Respiration, Phosphorylation<br />
}}<br />
{{Labeling<br />
|area=Respiration<br />
|organism=Rat<br />
|tissues=Kidney<br />
|preparations=Isolated mitochondria<br />
|topics=ADP, Calcium, Coupling efficiency;uncoupling, Inhibitor, Ion;substrate transport<br />
|additional=Made history<br />
}}</div>Bader Helgahttps://wiki.oroboros.at/index.php?title=Brierley_1962_Proc_Natl_Acad_Sci_USA&diff=90541Brierley 1962 Proc Natl Acad Sci USA2015-05-28T09:18:24Z<p>Bader Helga: </p>
<hr />
<div>{{Publication<br />
|title=Brierley GP, Bachmann PE, Green DE (1962) Active transport of inorganic phosphate and magnesium ions by beef heart mitochondria. Proc Natl Acad Sci U S A 48:1928-35.<br />
|info=[http://www.ncbi.nlm.nih.gov/pubmed/?term=PMID%3A+14015424 PMID: 14015424 Open Access]; [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC221100/pdf/pnas00234-0054.pdf PDF]<br />
|authors=Brierley GP, Bachmann PE, Green DE<br />
|year=1962<br />
|journal=Proc Natl Acad Sci U S A<br />
|abstract=No abstract supplied.<br />
|keywords=Inorganic phosphate, Magnesium ions, Active transport<br />
}}<br />
{{Labeling<br />
|organism=Bovines<br />
|tissues=Heart<br />
|preparations=Isolated mitochondria<br />
|topics=ADP, Ion;substrate transport<br />
|additional=Made history<br />
}}</div>Bader Helgahttps://wiki.oroboros.at/index.php?title=Ernster_1962_Nature&diff=90539Ernster 1962 Nature2015-05-28T09:14:40Z<p>Bader Helga: </p>
<hr />
<div>{{Publication<br />
|title=Ernster L (1962) Reaction pathways of succinate-linked acetoacetate reduction in tissue homogenates and isolated mitochondria. Nature 193:1050-2.<br />
|info=[http://www.ncbi.nlm.nih.gov/pubmed/13890667 PMID: 13890667]<br />
|authors=Ernster L<br />
|year=1962<br />
|journal=Nature<br />
|abstract=No abstract supplied.<br />
|keywords=Acetoacetate reduction, Succinate, Reaction pathways<br />
}}<br />
{{Labeling<br />
|preparations=Homogenate, Isolated mitochondria<br />
|enzymes=Complex II;succinate dehydrogenase<br />
|additional=Made history<br />
}}</div>Bader Helgahttps://wiki.oroboros.at/index.php?title=Fernandez-Moran_1962_Circulation&diff=90538Fernandez-Moran 1962 Circulation2015-05-28T09:13:56Z<p>Bader Helga: </p>
<hr />
<div>{{Publication<br />
|title=Fernandez-Moran H (1962) Cell-membrane ultrastructure. Low-temperature electron microscopy and x-ray diffraction studies of lipoprotein components in lamellar systems. Circulation 26:1039-65.<br />
|info=[http://www.ncbi.nlm.nih.gov/pubmed/?term=PMID%3A+13944801 PMID: 13944801]; [http://circ.ahajournals.org/content/26/5/1039.full.pdf+html pdf]<br />
|authors=Fernandez-Moran H<br />
|year=1962<br />
|journal=Circulation<br />
|abstract=The combined electron-microscope and biochemical evidence regarding mitochondria and mitochondrial fractions, although still preliminary in character, indicates that all the functional enzymatic components of the electron-transport chain are compactly arranged in the "elementary particle," which may therefore be regarded as the ultimate unit of mitochondrial function. New data have also been obtained on the hydrated lipoprotein matrix, the recently isolated structural protein, solubilized pure lipid fractions, cytochromes, and other constituent elements of the respiratory-enzyme assemblies.<br />
|keywords=Mitochondrial structure, Electron microscopy, X-ray diffraction<br />
}}<br />
{{Labeling<br />
|additional=Made history<br />
}}</div>Bader Helgahttps://wiki.oroboros.at/index.php?title=Fernandez-Moran_1962_Circulation&diff=90535Fernandez-Moran 1962 Circulation2015-05-28T09:09:45Z<p>Bader Helga: </p>
<hr />
<div>{{Publication<br />
|title=Fernandez-Moran H (1962) Cell-membrane ultrastructure. Low-temperature electron microscopy and x-ray diffraction studies of lipoprotein components in lamellar systems. Circulation 26:1039-65.<br />
|info=[http://circ.ahajournals.org/content/26/5/1039.full.pdf+html PMID: 13944801 Open Access]<br />
|authors=Fernandez-Moran H<br />
|year=1962<br />
|journal=Circulation<br />
|abstract=The combined electron-microscope and biochemical evidence regarding mitochondria and mitochondrial fractions, although still preliminary in character, indicates that all the functional enzymatic components of the electron-transport chain are compactly arranged in the "elementary particle," which may therefore be regarded as the ultimate unit of mitochondrial function. New data have also been obtained on the hydrated lipoprotein matrix, the recently isolated structural protein, solubilized pure lipid fractions, cytochromes, and other constituent elements of the respiratory-enzyme assemblies.<br />
|keywords=Mitochondrial structure, electron microscopy, x-ray diffraction<br />
}}<br />
{{Labeling<br />
|additional=Made history<br />
}}</div>Bader Helgahttps://wiki.oroboros.at/index.php?title=Fowler_1962_Biochim_Biophys_Acta&diff=90534Fowler 1962 Biochim Biophys Acta2015-05-28T09:09:28Z<p>Bader Helga: </p>
<hr />
<div>{{Publication<br />
|title=Fowler LR, Richardson LH, Hatefi Y (1962) A rapid method for the preparation of highly purified cytochrome oxidase. Biochim Biophys Acta 64:170-3.<br />
|info=[http://www.ncbi.nlm.nih.gov/pubmed?term=Fowler%20LR%2C%20Richardson%20SH%2C%20Hatefi%20Y PMID: 13958990]<br />
|authors=Fowler LR, Richardson LH, Hatefi Y<br />
|year=1962<br />
|journal=Biochim Biophys Acta<br />
|abstract=No Abstract supplied.<br />
|keywords=Cytochrome oxidase<br />
}}<br />
{{Labeling<br />
|additional=Made history<br />
}}</div>Bader Helgahttps://wiki.oroboros.at/index.php?title=Klingenberg_1961_Biochem_Z-II&diff=90533Klingenberg 1961 Biochem Z-II2015-05-28T09:05:43Z<p>Bader Helga: </p>
<hr />
<div>{{Publication<br />
|title=Klingenberg M, Schollmeyer P (1961) On the reversibility of oxidative phosphorylation II. Effect of adenosine triphosphate on the respiratory chain of respiring mitochondria. Biochem Z 335:231-42.<br />
|info=[http://www.ncbi.nlm.nih.gov/pubmed/14457018 PMID: 14457018]<br />
|authors=Klingenberg M, Schollmeyer P<br />
|year=1961<br />
|journal=Biochem Z<br />
|abstract=No Abstract supplied.<br />
|keywords=Oxidative phosphorylation, ATP<br />
}}<br />
{{Labeling<br />
|topics=ATP; ADP; AMP; PCr<br />
|couplingstates=OXPHOS<br />
|additional=Made history<br />
}}</div>Bader Helgahttps://wiki.oroboros.at/index.php?title=Klingenberg_1961_Biochem_Z-III&diff=90532Klingenberg 1961 Biochem Z-III2015-05-28T09:04:51Z<p>Bader Helga: </p>
<hr />
<div>{{Publication<br />
|title=Klingenberg M, Schollmeyer P (1961) On the reversibility of oxidative phosphorylation III. Effect of adenosine triphosphate on the respiratory chain in respiratory inhibited mitochondria. Biochem Z 335:243-62.<br />
|info=[http://www.ncbi.nlm.nih.gov/pubmed/14457019 PMID: 14457019]<br />
|authors=Klingenberg M, Schollmeyer P<br />
|year=1961<br />
|journal=Biochem Z<br />
|abstract=No abstract supplied.<br />
|keywords=Oxidative phosphorylation, ATP, Respiratory inhibition<br />
}}<br />
{{Labeling<br />
|topics=ATP; ADP; AMP; PCr<br />
|couplingstates=OXPHOS<br />
|additional=Made history<br />
}}</div>Bader Helgahttps://wiki.oroboros.at/index.php?title=Mitchell_1961_Nature&diff=90531Mitchell 1961 Nature2015-05-28T09:03:36Z<p>Bader Helga: </p>
<hr />
<div>{{Publication<br />
|title=Mitchell P (1961) Coupling of phosphorylation to electron and hydrogen transfer by a chemi-osmotic type of mechanism. Nature 191:144-8.<br />
|info=[http://www.ncbi.nlm.nih.gov/pubmed/13771349 PMID: 13771349]<br />
|authors=Mitchell P<br />
|year=1961<br />
|journal=Nature<br />
|keywords=Oxidative phosphorylation, Electron transfer, Hydrogen transfer<br />
}}<br />
{{Labeling<br />
|additional=Made history<br />
}}</div>Bader Helgahttps://wiki.oroboros.at/index.php?title=Wollenberger_1961_J_Biophys_Biochem_Cytol&diff=90530Wollenberger 1961 J Biophys Biochem Cytol2015-05-28T09:02:44Z<p>Bader Helga: </p>
<hr />
<div>{{Publication<br />
|title=Wollenberger A, Schulze W (1961) Mitochondrial alterations in the myocardium of dogs with aortic stenosis. J Biophys Biochem Cytol 10:285-8.<br />
|info=[http://www.ncbi.nlm.nih.gov/pubmed/13786416 PMID: 13786416 Open Access]<br />
|authors=Wollenberger A, Schulze W<br />
|year=1961<br />
|journal=J Biophys Biochem Cytol<br />
|abstract=No abstract supplied.<br />
}}<br />
{{Labeling<br />
|area=mt-Medicine<br />
|organism=Dog<br />
|tissues=Heart<br />
|diseases=Cardiovascular<br />
}}</div>Bader Helgahttps://wiki.oroboros.at/index.php?title=Azzone_1961_J_Biol_Chem&diff=90528Azzone 1961 J Biol Chem2015-05-28T08:57:23Z<p>Bader Helga: </p>
<hr />
<div>{{Publication<br />
|title=Azzone GF, Ernster L (1961) Demonstration of a requirement of high energy phosphate for the aerobic oxidation of succinate in liver mitochondria. J Biol Chem 236:1518-25.<br />
|info=[http://www.ncbi.nlm.nih.gov/pubmed/13685481 PMID: 13685481 Open Access]<br />
|authors=Azzone GF, Ernster L<br />
|year=1961<br />
|journal=J Biol Chem<br />
|abstract=Preincubation of rat liver mitochondria in a sucrose-KCl medium in the presence of 2 to 3 mM arsenate and 0.06 mM Dicumarol or 0.1 mM 2,4dinitrophenol for 3 to 4 minutes results in a marked depression of the succinoxidase capacity. No depression is found when the preincubation is made in the presence of Amytal, cysteine sulfinate, or inorganic phosphate. Addition of adenosine triphosphate after the preincubation stimulates succinate oxidation several-fold. The effect of adenosine triphosphate is not duplicated by cysteine sulfinate, inorganic phosphate, ethylenediaminetetraacetate, adenosine 5’-phosphate, cytidine triphosphate, uridine triphosphate, inosine triphosphate, or guanidine triphosphate. Similar results are obtained with mitochondria pretreated with dinitrophenol and adenosine 5’-phosphate.<br />
<br />
The data are consistent with the conclusion that conditions leading to a depletion of the endogenous content of mitochondrial high energy phosphate result in a reversible depression of the succinoxidase capacity. <br />
<br />
The concept is developed that the aerobic oxidation of succinate in intact liver mitochondria requires an activation by high energy phosphate. Some implications of this concept regarding the enzymic organization of mitochondrial electron transport and oxidative phosphorylation are discussed.<br />
|keywords=Succinate oxidation, High energy phosphate, ATP<br />
}}<br />
{{Labeling<br />
|organism=Rat<br />
|tissues=Liver<br />
|preparations=Isolated mitochondria<br />
|enzymes=Complex II;succinate dehydrogenase<br />
|topics=ATP; ADP; AMP; PCr, Substrate;glucose;TCA cycle<br />
|couplingstates=OXPHOS, ETS<br />
|substratestates=CII<br />
|additional=Made history<br />
}}</div>Bader Helgahttps://wiki.oroboros.at/index.php?title=Chance_1961_J_Biol_Chem-I&diff=90526Chance 1961 J Biol Chem-I2015-05-28T08:54:31Z<p>Bader Helga: </p>
<hr />
<div>{{Publication<br />
|title=Chance B, Hollunger G (1961) The interaction of energy and electron transfer reactions in mitochondria I. General properties and nature of the products of succinate-linked reduction of pyridine nucleotide. J Biol Chem 236:1534-43.<br />
|info=[http://www.ncbi.nlm.nih.gov/pubmed/13692277 PMID: 13692277 Open Access]<br />
|authors=Chance B, Hollunger G<br />
|year=1961<br />
|journal=J Biol Chem<br />
|abstract=A thermodynamically improbable reduction of pyridine nucleotide caused by the addition of succinate to isolated mitochondria has been demonstrated. The material so reduced exhibits kinetic responses, some of which can suggest its consideration as a member of the respiratory chain, but a quantitative examination of the kinetics of oxidation and reduction shows that only a small portion of the total respiratory activity in succinate oxidation passes through the diphosphopyridine nucleotide-linked pathway. <br />
<br />
The nature of the reduction product has been examined in heart, liver, and guinea pig kidney mitochondria and is found to be material absorbing at 340 mµ and having a fluorescence emission maximum at 440 mµ. Direct chemical assays on kidney mitochondria indicate that the reduced material is diphosphopyridine nucleotide. A preliminary evaluation of various hypotheses to explain this result leads us tentatively to reject hypotheses based upon a single pool of mitochondrial pyridine nucleotide in which diphosphopyridine nucleotide and succinate compete for oxidizing equivalents from the cytochrome chain. <br />
<br />
Further indication of the complexities of this reaction is that respiration can be initiated by succinate without measurable pyridine nucleotide reduction and that a transition from aerobiosis in state 3 to anaerobiosis (state 5) can lead to a higher oxidation level of pyridine nucleotide than was observed aerobically in state 4. These observations suggest that the presence of adenosine 5’-diphosphate inhibits pyridine nucleotide reduction under both aerobic and anaerobic conditions and support the possibility that an energy-linked reaction may be involved.<br />
|keywords=Energy transfer, Eletcron transfer, Succinate, Pyridine nucleotide, ADP<br />
}}<br />
{{Labeling<br />
|area=Respiration<br />
|organism=Guinea pig<br />
|tissues=Heart, Liver, Kidney<br />
|preparations=Isolated mitochondria<br />
|topics=ADP<br />
|couplingstates=OXPHOS<br />
|substratestates=CII<br />
|additional=Made history<br />
}}</div>Bader Helgahttps://wiki.oroboros.at/index.php?title=Chance_1961_J_Biol_Chem-III&diff=90525Chance 1961 J Biol Chem-III2015-05-28T08:53:19Z<p>Bader Helga: </p>
<hr />
<div>{{Publication<br />
|title=Chance B, Hollunger G (1961) The interaction of energy and electron transfer reactions in mitochondria III. Substrate requirements for pyridine nucleotide reduction in mitochondria. J Biol Chem 236:1555-61.<br />
|info=[http://www.ncbi.nlm.nih.gov/pubmed/13692278 PMID: 13692278 Open Access]<br />
|authors=Chance B, Hollunger G<br />
|year=1961<br />
|journal=J Biol Chem<br />
|abstract=# A specific succinate requirement for energy-linked reduction of mitochondrial pyridine nucleotide is demonstrated in pigeon heart and guinea pig kidney mitochondria.<br />
# The succinate used in this reduction can be generated in the oxidation of malate plus glutamate or of α-ketoglutarate. <br />
# The role of succinate is identified by the specific inhibitory responses of the reaction to malonate, phosphate, and fumarate. <br />
# At least two kinds of mitochondrial pyridine nucleotide are shown to be reducible in State 4: (a) about one-third in the absence of added succinate in a malonate-insensitive reaction in the presence of a substrate such as malate plus glutamate and (b) about two-thirds in the presence of added succinate in a malonate-sensitive, energy-linked reaction. These two kinds of pyridine nucleotide may be considered to be compartmented.<br />
|keywords=Pyridine nucleotide, Succinate<br />
}}<br />
{{Labeling<br />
|organism=Guinea pig<br />
|taxonomic group=Birds<br />
|tissues=Heart, Kidney<br />
|preparations=Isolated mitochondria<br />
|enzymes=Complex II;succinate dehydrogenase<br />
|topics=Substrate;glucose;TCA cycle<br />
|couplingstates=OXPHOS<br />
|additional=Made history<br />
}}</div>Bader Helgahttps://wiki.oroboros.at/index.php?title=DeLuca_1961_Proc_Natl_Acad_Sci_USA&diff=90524DeLuca 1961 Proc Natl Acad Sci USA2015-05-28T08:50:52Z<p>Bader Helga: </p>
<hr />
<div>{{Publication<br />
|title=DeLuca HF, Engstrom GW (1961) Calcium uptake by rat kidney mitochondria. Proc Natl Acad Sci USA 47:1744-50.<br />
|info=[http://www.ncbi.nlm.nih.gov/pubmed/13885269 PMID: 13885269 Open Access]<br />
|authors=DeLuca HF, Engstrom GW<br />
|year=1961<br />
|journal=Proc Natl Acad Sci USA<br />
|abstract=Rat kidney mitochondria take up large quantities of calcium by a process requiring ATP, magnesium ions, and an oxidizable substrate. Although the process requires ATP, it is not directly dependent upon oxidative phosphorylation or upon the operation of the entire electron transport chain. The rate of calcium uptake is not enhanced by vitamin D. It is inhibited strongly by dicumarol, antimycin A and 2,3-dimercaptopropanol and less strongly by phloridzin and p-chloromercuribenzoate, but not by dinitrophenol, azide, cyanide, oligomycin, and iodoacetate at the concentrations tested. The mitochondria apparently can bind about 15 calcium ions per molecule of ATP utilized.<br />
|keywords=Calcium, Mitochondria<br />
}}<br />
{{Labeling<br />
|organism=Rat<br />
|tissues=Kidney<br />
|preparations=Isolated mitochondria<br />
|topics=ATP; ADP; AMP; PCr, Ion;substrate transport<br />
|additional=Made history<br />
}}</div>Bader Helgahttps://wiki.oroboros.at/index.php?title=Beinert_1960_Biochem_Biophys_Res_Commun&diff=90522Beinert 1960 Biochem Biophys Res Commun2015-05-28T08:46:27Z<p>Bader Helga: </p>
<hr />
<div>{{Publication<br />
|title=Beinert H, Sands RH (1960) Studies on succinic and DPNH dehydrogenase preparations by paramagnetic resonance (EPR) spectroscopy. Biochem Biophys Res Commun 3:41-6.<br />
|info=[http://www.sciencedirect.com/science/article/pii/0006291X60901005 ScienceDirect]<br />
|authors=Beinert H, Sands RH<br />
|year=1960<br />
|journal=Biochem Biophys Res Commun<br />
|abstract=No Abstract<br />
|keywords=Succinic dehydrogenase, DPNH dehydrogenase, EPR spectoscopy<br />
}}<br />
{{Labeling<br />
|enzymes=Complex II;succinate dehydrogenase<br />
|additional=Made history<br />
}}</div>Bader Helgahttps://wiki.oroboros.at/index.php?title=Klingenberg_1960_Biochem_Z&diff=90521Klingenberg 1960 Biochem Z2015-05-28T08:45:42Z<p>Bader Helga: </p>
<hr />
<div>{{Publication<br />
|title=Klingenberg M, Schollmeyer P (1960) On the reversibility of oxidative phosphorylation. Adenosine triphosphate-dependent respiratory control and reduction of diphosphopyridine nucleotide in mitochondria. Biochem Z 333:335-51.<br />
|info=[http://www.ncbi.nlm.nih.gov/pubmed/13756883 PMID: 13756883]<br />
|authors=Klingenberg M, Schollmeyer P<br />
|year=1960<br />
|journal=Biochem Z<br />
|abstract=No Abstract<br />
[Article in German]<br />
|keywords=Oxidative phosphorylation, ATP, Diphosphopyridine nucleotide<br />
}}<br />
{{Labeling<br />
|topics=ATP; ADP; AMP; PCr<br />
|couplingstates=OXPHOS<br />
|additional=Made history<br />
}}</div>Bader Helgahttps://wiki.oroboros.at/index.php?title=Pullman_1960_J_Biol_Chem&diff=90518Pullman 1960 J Biol Chem2015-05-28T08:39:33Z<p>Bader Helga: </p>
<hr />
<div>{{Publication<br />
|title=Pullman ME, Penefsky HS, Datta A, Racker E (1960) Partial resolution of the enzymes catalyzing oxidative phosphorylation. I. Purification and properties of soluble dinitrophenol-stimulated adenosine triphosphatase. J Biol Chem 235:3322-9.<br />
|info=[http://www.jbc.org/content/235/11/3322.full.pdf+html PMID: 13738472 Open Access]<br />
|authors=Pullman ME, Penefsky HS, Datta A, Racker E<br />
|year=1960<br />
|journal=J Biol Chem<br />
|abstract=# The purification o f a soluble ATPase from beef heart mitochondria is described. The activity is dependent on Mg++ and is stimulated by 2,4-dinitrophenol. The enzyme cleaves the terminal phosphate of ATP and is inhibited by ADP. The activity is therefore assayed in the presence of an ATP regenerating system. <br />
# The enzyme is cold labile. Although stable at room temperature, the enzyme rapidly loses activity at 4°. ATP, which protects the enzyme against inactivation by heat and dialysis, does not prevent the cold inactivation. <br />
# Attempts to demonstrate an exchange between either Pi32 or C14-ADP and ATP in the presence of the enzyme were unsuccessful. <br />
# The properties of the purified enzyme are discussed in relation to particulate mitochondrial ATPase and to myosin ATPase.<br />
|keywords=Oxidative phosphorylation, Enzymes, Dinitrophenol, ATP, Beef heart<br />
}}<br />
{{Labeling<br />
|organism=Bovines<br />
|tissues=Heart<br />
|preparations=Isolated mitochondria<br />
|enzymes=Complex V;ATP synthase<br />
|topics=ATP; ADP; AMP; PCr, Temperature<br />
|couplingstates=OXPHOS<br />
|additional=Made history<br />
}}</div>Bader Helgahttps://wiki.oroboros.at/index.php?title=Buecher_1958_Angew_Chem&diff=90517Buecher 1958 Angew Chem2015-05-28T08:37:58Z<p>Bader Helga: </p>
<hr />
<div>{{Publication<br />
|title=Buecher T, Klingenberg M (1958) Wege des Wasserstoffs in der lebendigen Organisation. Angew Chem 70:552-70.<br />
|info=[http://onlinelibrary.wiley.com/doi/10.1002/ange.19580701707/abstract Wiley Online Library]<br />
|authors=Buecher T, Klingenberg M<br />
|year=1958<br />
|journal=Angew Chem<br />
|abstract=Die Wechselbeziehungen innerhalb des Netzwerks von Redox-Reaktionen, das sich ueber einen großen Teil der metabolisch wesentlichen Funktionen lebender Zellen erstreckt, werden eroertert. Anschließend an die Darlegung grundsaetzlicher Gegebenheiten bei der Zerlegung der Brennstoffe werden einige Gruppen von Redox-Systemen in verschiedenen Raeumen der Zellen und Gewebe in ihren Beziehungen zur Biosynthese, zur Bioenergetik und zur Zellatmung behandelt. Neuere Ergebnisse aus dem Arbeitskreis der Verfasser stehen dabei im Vordergrund. Die Beispiele zeigen, wie weitgehend die Entwicklung der Problematik der dynamischen Biochemie an den Fortschritt der Cytologie gebunden ist.<br />
|keywords=Wasserstoff, Biosynthese, Bioenergetik, Zellatmung<br />
}}<br />
{{Labeling<br />
|additional=Made history<br />
}}</div>Bader Helga