https://wiki.oroboros.at/index.php?title=Genova_2018_MiP2018&feed=atom&action=historyGenova 2018 MiP2018 - Revision history2024-03-28T22:53:19ZRevision history for this page on the wikiMediaWiki 1.36.1https://wiki.oroboros.at/index.php?title=Genova_2018_MiP2018&diff=161192&oldid=prevPlangger Mario at 07:43, 20 August 20182018-08-20T07:43:54Z<p></p>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|event=MiP2018</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|event=MiP2018</div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>|abstract=[[Image:MITOEAGLE-logo.jpg|left|100px|link=http://www.mitoglobal.org/index.php/MITOEAGLE|COST Action <del style="font-weight: bold; text-decoration: none;">MITOEAGLE</del>]]</div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>|abstract=[[Image:MITOEAGLE-logo.jpg|left|100px|link=http://www.mitoglobal.org/index.php/MITOEAGLE|COST Action <ins style="font-weight: bold; text-decoration: none;">MitoEAGLE</ins>]]</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>Experimental evidence has ascertained that the major respiratory complexes involved in energy conservation in mitochondria (i.e. complexes I, III and IV) are assembled as stoichiometric supramolecular units (supercomplexes, SCs) based upon specific, though dynamic, interactions. Although SCs have been revealed and characterized in mitochondria from a variety of cell types and organisms, their functional role is less well defined and still open to discussion [1,2]. Our kinetic studies [3] in frozen and thawed bovine heart mitochondria and in reconstituted proteoliposomes favour the concept that electron transfer between Complex I and Complex III is mediated by channelling of electrons through Coenzyme Q<sub>10</sub> (CoQ<sub>10</sub>) molecules bound to the SC I<sub>1</sub>III<sub>2</sub>, thus providing kinetic advantage, in contrast with the previously accepted hypothesis that the transfer of reducing equivalents from Complex I to Complex III occur via random diffusion of CoQ<sub>10</sub> embedded in the inner mitochondrial membrane (pool behaviour). On the contrary, electron transfer from Complex II to Complex III and from Complex III to Complex IV seems to operate by random diffusion of intermediate substrates between the partner enzymes. In particular, our results show that NADH-cytochrome ''c'' and succinate-cytochrome ''c'' oxidoreductase activity are almost completely additive, as it is expected of two independent metabolic routes. Moreover, the rate obtained by simultaneous addition of NADH and succinate is much higher than the rate predicted for a single homogeneous CoQ10 pool. However, when the pressure by the reducing substrates increases due to strong inhibition of Complex III, or when detergents destabilize the SCs, CoQ<sub>10</sub> molecules bound in the SC I<sub>1</sub>III<sub>2</sub> may exchange with free CoQ<sub>10</sub> molecules in the membrane, thus approaching the rates predicted for a single pool. A slow dissociation equilibrium of CoQ<sub>10</sub> from SC I<sub>1</sub>III<sub>2</sub>, and the consequent accessibility of CoQ<sub>10</sub> pool to the same SC, may be a device by which the size of the pool determines saturation of the binding site(s) in the SC and controls oxidation of NAD-linked substrates in physiological conditions, also providing a rationale for the beneficial effect of exogenous CoQ<sub>10</sub> supplementation on mitochondrial bioenergetics. Furthermore, another property provided by the SC I<sub>1</sub>III<sub>2</sub> assembly is the control of the production of reactive oxygen species by Complex I [4], which might be important in the regulation of signal transduction from mitochondria.</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>Experimental evidence has ascertained that the major respiratory complexes involved in energy conservation in mitochondria (i.e. complexes I, III and IV) are assembled as stoichiometric supramolecular units (supercomplexes, SCs) based upon specific, though dynamic, interactions. Although SCs have been revealed and characterized in mitochondria from a variety of cell types and organisms, their functional role is less well defined and still open to discussion [1,2]. Our kinetic studies [3] in frozen and thawed bovine heart mitochondria and in reconstituted proteoliposomes favour the concept that electron transfer between Complex I and Complex III is mediated by channelling of electrons through Coenzyme Q<sub>10</sub> (CoQ<sub>10</sub>) molecules bound to the SC I<sub>1</sub>III<sub>2</sub>, thus providing kinetic advantage, in contrast with the previously accepted hypothesis that the transfer of reducing equivalents from Complex I to Complex III occur via random diffusion of CoQ<sub>10</sub> embedded in the inner mitochondrial membrane (pool behaviour). On the contrary, electron transfer from Complex II to Complex III and from Complex III to Complex IV seems to operate by random diffusion of intermediate substrates between the partner enzymes. In particular, our results show that NADH-cytochrome ''c'' and succinate-cytochrome ''c'' oxidoreductase activity are almost completely additive, as it is expected of two independent metabolic routes. Moreover, the rate obtained by simultaneous addition of NADH and succinate is much higher than the rate predicted for a single homogeneous CoQ10 pool. However, when the pressure by the reducing substrates increases due to strong inhibition of Complex III, or when detergents destabilize the SCs, CoQ<sub>10</sub> molecules bound in the SC I<sub>1</sub>III<sub>2</sub> may exchange with free CoQ<sub>10</sub> molecules in the membrane, thus approaching the rates predicted for a single pool. A slow dissociation equilibrium of CoQ<sub>10</sub> from SC I<sub>1</sub>III<sub>2</sub>, and the consequent accessibility of CoQ<sub>10</sub> pool to the same SC, may be a device by which the size of the pool determines saturation of the binding site(s) in the SC and controls oxidation of NAD-linked substrates in physiological conditions, also providing a rationale for the beneficial effect of exogenous CoQ<sub>10</sub> supplementation on mitochondrial bioenergetics. Furthermore, another property provided by the SC I<sub>1</sub>III<sub>2</sub> assembly is the control of the production of reactive oxygen species by Complex I [4], which might be important in the regulation of signal transduction from mitochondria.</div></td></tr>
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</table>Plangger Mariohttps://wiki.oroboros.at/index.php?title=Genova_2018_MiP2018&diff=160560&oldid=prevKandolf Georg at 11:14, 7 August 20182018-08-07T11:14:15Z<p></p>
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<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>|title=[[Image:<del style="font-weight: bold; text-decoration: none;">MiPsocietyLOGO</del>.<del style="font-weight: bold; text-decoration: none;">JPG</del>|left|90px|<del style="font-weight: bold; text-decoration: none;">Mitochondrial Physiology Society|MiPsociety</del>]] Respiratory supercomplexes: evidence for separate though interconnected compartments of Coenzyme Q<sub>10</sub> in mammalian mitochondria.</div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>|title=[[Image:<ins style="font-weight: bold; text-decoration: none;">GenovaML</ins>.<ins style="font-weight: bold; text-decoration: none;">jpg</ins>|left|90px|<ins style="font-weight: bold; text-decoration: none;">Maria Luisa Genova</ins>]] Respiratory supercomplexes: evidence for separate though interconnected compartments of Coenzyme Q<sub>10</sub> in mammalian mitochondria.</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|info=[[MiP2018]]</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|info=[[MiP2018]]</div></td></tr>
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</table>Kandolf Georghttps://wiki.oroboros.at/index.php?title=Genova_2018_MiP2018&diff=160398&oldid=prevKandolf Georg at 08:01, 6 August 20182018-08-06T08:01:01Z<p></p>
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 08:01, 6 August 2018</td>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|event=MiP2018</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|event=MiP2018</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|abstract=[[Image:MITOEAGLE-logo.jpg|left|100px|link=http://www.mitoglobal.org/index.php/MITOEAGLE|COST Action MITOEAGLE]]</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|abstract=[[Image:MITOEAGLE-logo.jpg|left|100px|link=http://www.mitoglobal.org/index.php/MITOEAGLE|COST Action MITOEAGLE]]</div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>Experimental evidence has ascertained that the major respiratory complexes involved in energy conservation in mitochondria (i.e. complexes I, III and IV) are assembled as stoichiometric supramolecular units (supercomplexes, SCs) based upon specific, though dynamic, interactions. Although SCs have been revealed and characterized in mitochondria from a variety of cell types and organisms, their functional role is less well defined and still open to discussion [1, 2]. Our kinetic studies [3] in frozen and thawed bovine heart mitochondria and in reconstituted proteoliposomes favour the concept that electron transfer between Complex I and Complex III is mediated by channelling of electrons through Coenzyme Q<sub>10</sub> (CoQ<sub>10</sub>) molecules bound to the SC I<sub>1</sub>III<sub>2</sub>, thus providing kinetic advantage, in contrast with the previously accepted hypothesis that the transfer of reducing equivalents from Complex I to Complex III occur via random diffusion of CoQ<sub>10</sub> embedded in the inner mitochondrial membrane (pool behaviour). On the contrary, electron transfer from Complex II to Complex III and from Complex III to Complex IV seems to operate by random diffusion of intermediate substrates between the partner enzymes. In particular, our results show that NADH-cytochrome ''c'' and succinate-cytochrome ''c'' oxidoreductase activity are almost completely additive, as it is expected of two independent metabolic routes. Moreover, the rate obtained by simultaneous addition of NADH and succinate is much higher than the rate predicted for a single homogeneous CoQ10 pool. However, when the pressure by the reducing substrates increases due to strong inhibition of Complex III, or when detergents destabilize the SCs, CoQ<sub>10</sub> molecules bound in the SC I<sub>1</sub>III<sub>2</sub> may exchange with free CoQ<sub>10</sub> molecules in the membrane, thus approaching the rates predicted for a single pool. A slow dissociation equilibrium of CoQ<sub>10</sub> from SC I<sub>1</sub>III<sub>2</sub>, and the consequent accessibility of CoQ<sub>10</sub> pool to the same SC, may be a device by which the size of the pool determines saturation of the binding site(s) in the SC and controls oxidation of NAD-linked substrates in physiological conditions, also providing a rationale for the beneficial effect of exogenous CoQ<sub>10</sub> supplementation on mitochondrial bioenergetics. Furthermore, another property provided by the SC I<sub>1</sub>III<sub>2</sub> assembly is the control of the production of reactive oxygen species by Complex I [4], which might be important in the regulation of signal transduction from mitochondria.</div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>Experimental evidence has ascertained that the major respiratory complexes involved in energy conservation in mitochondria (i.e. complexes I, III and IV) are assembled as stoichiometric supramolecular units (supercomplexes, SCs) based upon specific, though dynamic, interactions. Although SCs have been revealed and characterized in mitochondria from a variety of cell types and organisms, their functional role is less well defined and still open to discussion [1,2]. Our kinetic studies [3] in frozen and thawed bovine heart mitochondria and in reconstituted proteoliposomes favour the concept that electron transfer between Complex I and Complex III is mediated by channelling of electrons through Coenzyme Q<sub>10</sub> (CoQ<sub>10</sub>) molecules bound to the SC I<sub>1</sub>III<sub>2</sub>, thus providing kinetic advantage, in contrast with the previously accepted hypothesis that the transfer of reducing equivalents from Complex I to Complex III occur via random diffusion of CoQ<sub>10</sub> embedded in the inner mitochondrial membrane (pool behaviour). On the contrary, electron transfer from Complex II to Complex III and from Complex III to Complex IV seems to operate by random diffusion of intermediate substrates between the partner enzymes. In particular, our results show that NADH-cytochrome ''c'' and succinate-cytochrome ''c'' oxidoreductase activity are almost completely additive, as it is expected of two independent metabolic routes. Moreover, the rate obtained by simultaneous addition of NADH and succinate is much higher than the rate predicted for a single homogeneous CoQ10 pool. However, when the pressure by the reducing substrates increases due to strong inhibition of Complex III, or when detergents destabilize the SCs, CoQ<sub>10</sub> molecules bound in the SC I<sub>1</sub>III<sub>2</sub> may exchange with free CoQ<sub>10</sub> molecules in the membrane, thus approaching the rates predicted for a single pool. A slow dissociation equilibrium of CoQ<sub>10</sub> from SC I<sub>1</sub>III<sub>2</sub>, and the consequent accessibility of CoQ<sub>10</sub> pool to the same SC, may be a device by which the size of the pool determines saturation of the binding site(s) in the SC and controls oxidation of NAD-linked substrates in physiological conditions, also providing a rationale for the beneficial effect of exogenous CoQ<sub>10</sub> supplementation on mitochondrial bioenergetics. Furthermore, another property provided by the SC I<sub>1</sub>III<sub>2</sub> assembly is the control of the production of reactive oxygen species by Complex I [4], which might be important in the regulation of signal transduction from mitochondria.</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|editor=[[Plangger M]], [[Kandolf G]],</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|editor=[[Plangger M]], [[Kandolf G]],</div></td></tr>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>{{Labeling</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>{{Labeling</div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div><del style="font-weight: bold; text-decoration: none;">|area=mt-Structure;fission;fusion</del></div></td><td colspan="2"></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|organism=Bovines</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|organism=Bovines</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|tissues=Heart</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|tissues=Heart</div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>|enzymes=Supercomplex</div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>|enzymes=<ins style="font-weight: bold; text-decoration: none;">Complex I, Complex II;succinate dehydrogenase, Complex III, Complex IV;cytochrome c oxidase, </ins>Supercomplex</div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div><del style="font-weight: bold; text-decoration: none;">|pathways=S</del></div></td><td colspan="2"></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>}}</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>}}</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Affiliations ==</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Affiliations ==</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>Tioli G(1), Falasca AI(2), Lenaz G(1), Genova ML(1)</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>Tioli G(1), Falasca AI(2), Lenaz G(1), Genova ML(1)</div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>::::#Dept Biomedical Neuromotor Sciences, Alma Mater Studiorum Univ Bologna</div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>::::#Dept Biomedical Neuromotor Sciences, Alma Mater Studiorum<ins style="font-weight: bold; text-decoration: none;">, </ins>Univ Bologna</div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>::::#Dept Food Drug<del style="font-weight: bold; text-decoration: none;">; </del>Univ Parma<del style="font-weight: bold; text-decoration: none;">, </del>Italy. - marialuisa.genova@unibo.it</div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>::::#Dept Food Drug<ins style="font-weight: bold; text-decoration: none;">, </ins>Univ Parma<ins style="font-weight: bold; text-decoration: none;">; </ins>Italy. - marialuisa.genova@unibo.it</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== References ==</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== References ==</div></td></tr>
</table>Kandolf Georghttps://wiki.oroboros.at/index.php?title=Genova_2018_MiP2018&diff=160387&oldid=prevPlangger Mario at 07:34, 6 August 20182018-08-06T07:34:03Z<p></p>
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 07:34, 6 August 2018</td>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>{{Abstract</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>{{Abstract</div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>|title=[[Image:MiPsocietyLOGO.JPG|left|90px|Mitochondrial Physiology Society|MiPsociety]]</div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>|title=[[Image:MiPsocietyLOGO.JPG|left|90px|Mitochondrial Physiology Society|MiPsociety]] <ins style="font-weight: bold; text-decoration: none;">Respiratory supercomplexes: evidence for separate though interconnected compartments of Coenzyme Q<sub>10</sub> in mammalian mitochondria.</ins></div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|info=[[MiP2018]]</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|info=[[MiP2018]]</div></td></tr>
<tr><td colspan="2"></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;">|authors=Tioli G, Falasca AI, Lenaz G, Genova ML</ins></div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|year=2018</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|year=2018</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|event=MiP2018</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|event=MiP2018</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|abstract=[[Image:MITOEAGLE-logo.jpg|left|100px|link=http://www.mitoglobal.org/index.php/MITOEAGLE|COST Action MITOEAGLE]]</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|abstract=[[Image:MITOEAGLE-logo.jpg|left|100px|link=http://www.mitoglobal.org/index.php/MITOEAGLE|COST Action MITOEAGLE]]</div></td></tr>
<tr><td colspan="2"></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;">Experimental evidence has ascertained that the major respiratory complexes involved in energy conservation in mitochondria (i.e. complexes I, III and IV) are assembled as stoichiometric supramolecular units (supercomplexes, SCs) based upon specific, though dynamic, interactions. Although SCs have been revealed and characterized in mitochondria from a variety of cell types and organisms, their functional role is less well defined and still open to discussion [1, 2]. Our kinetic studies [3] in frozen and thawed bovine heart mitochondria and in reconstituted proteoliposomes favour the concept that electron transfer between Complex I and Complex III is mediated by channelling of electrons through Coenzyme Q<sub>10</sub> (CoQ<sub>10</sub>) molecules bound to the SC I<sub>1</sub>III<sub>2</sub>, thus providing kinetic advantage, in contrast with the previously accepted hypothesis that the transfer of reducing equivalents from Complex I to Complex III occur via random diffusion of CoQ<sub>10</sub> embedded in the inner mitochondrial membrane (pool behaviour). On the contrary, electron transfer from Complex II to Complex III and from Complex III to Complex IV seems to operate by random diffusion of intermediate substrates between the partner enzymes. In particular, our results show that NADH-cytochrome ''c'' and succinate-cytochrome ''c'' oxidoreductase activity are almost completely additive, as it is expected of two independent metabolic routes. Moreover, the rate obtained by simultaneous addition of NADH and succinate is much higher than the rate predicted for a single homogeneous CoQ10 pool. However, when the pressure by the reducing substrates increases due to strong inhibition of Complex III, or when detergents destabilize the SCs, CoQ<sub>10</sub> molecules bound in the SC I<sub>1</sub>III<sub>2</sub> may exchange with free CoQ<sub>10</sub> molecules in the membrane, thus approaching the rates predicted for a single pool. A slow dissociation equilibrium of CoQ<sub>10</sub> from SC I<sub>1</sub>III<sub>2</sub>, and the consequent accessibility of CoQ<sub>10</sub> pool to the same SC, may be a device by which the size of the pool determines saturation of the binding site(s) in the SC and controls oxidation of NAD-linked substrates in physiological conditions, also providing a rationale for the beneficial effect of exogenous CoQ<sub>10</sub> supplementation on mitochondrial bioenergetics. Furthermore, another property provided by the SC I<sub>1</sub>III<sub>2</sub> assembly is the control of the production of reactive oxygen species by Complex I [4], which might be important in the regulation of signal transduction from mitochondria.</ins></div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|editor=[[Plangger M]], [[Kandolf G]],</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|editor=[[Plangger M]], [[Kandolf G]],</div></td></tr>
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<tr><td colspan="2"></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;">|area=mt-Structure;fission;fusion</ins></div></td></tr>
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<tr><td colspan="2"></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;">|tissues=Heart</ins></div></td></tr>
<tr><td colspan="2"></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;">|enzymes=Supercomplex</ins></div></td></tr>
<tr><td colspan="2"></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;">|pathways=S</ins></div></td></tr>
<tr><td colspan="2"></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>}}</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Affiliations ==</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== Affiliations ==</div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div> </div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;">Tioli G(1), Falasca AI(2), Lenaz G(1), Genova ML(1)</ins></div></td></tr>
<tr><td colspan="2"></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;">::::#Dept Biomedical Neuromotor Sciences, Alma Mater Studiorum Univ Bologna</ins></div></td></tr>
<tr><td colspan="2"></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;">::::#Dept Food Drug; Univ Parma, Italy. - marialuisa.genova@unibo.it</ins></div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><br/></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== References ==</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>== References ==</div></td></tr>
<tr><td colspan="2"></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;">::::#Lenaz G, Tioli G, Falasca AI, Genova ML (2017) Respiratory supercomplexes in mitochondria, in: Mechanisms of primary energy transduction in biology (Ed. M. Wikström) The royal society of chemistry, London (UK) 12:296-337.</ins></div></td></tr>
<tr><td colspan="2"></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;">::::#Fedor JG, Hirst J (2018) Mitochondrial supercomplexes do not enhance catalysis by quinone channeling. Cell Metab 28:1-7.</ins></div></td></tr>
<tr><td colspan="2"></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;">::::#Lenaz G, Tioli G, Falasca AI, Genova ML (2016) Complex I function in mitochondrial supercomplexes. Biochim Biophys Acta 1857:991-1000.</ins></div></td></tr>
<tr><td colspan="2"></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;">::::#Maranzana E, Barbero G, Falasca AI, Lenaz G, Genova ML (2013) Mitochondrial respiratory supercomplex association limits production of reactive oxygen species from complex I. Antioxid Redox Signal 19:1469-80.</ins></div></td></tr>
</table>Plangger Mariohttps://wiki.oroboros.at/index.php?title=Genova_2018_MiP2018&diff=160382&oldid=prevPlangger Mario: Created page with "{{Abstract |title=MiPsociety |info=MiP2018 |year=2018 |event=MiP2018 |abstract=Image:MITOEAGLE-lo..."2018-08-06T07:07:35Z<p>Created page with "{{Abstract |title=<a href="/index.php/File:MiPsocietyLOGO.JPG" title="File:MiPsocietyLOGO.JPG">left|90px|Mitochondrial Physiology Society|MiPsociety</a> |info=<a href="/index.php/MiP2018" class="mw-redirect" title="MiP2018">MiP2018</a> |year=2018 |event=MiP2018 |abstract=Image:MITOEAGLE-lo..."</p>
<p><b>New page</b></p><div>{{Abstract<br />
|title=[[Image:MiPsocietyLOGO.JPG|left|90px|Mitochondrial Physiology Society|MiPsociety]]<br />
|info=[[MiP2018]]<br />
|year=2018<br />
|event=MiP2018<br />
|abstract=[[Image:MITOEAGLE-logo.jpg|left|100px|link=http://www.mitoglobal.org/index.php/MITOEAGLE|COST Action MITOEAGLE]]<br />
|editor=[[Plangger M]], [[Kandolf G]],<br />
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== Affiliations ==<br />
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== References ==</div>Plangger Mario