Legkun 2014 Abstract IOC 2014-04 Schroecken: Difference between revisions
(Investigation on enzyme activity ratio under "shunt" respiration) |
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{{Abstract | {{Abstract | ||
|title=Legkun (2014) | |title=Legkun G, Motovilov K (2014) Investigation on alternative mechanism of electron transport in the respiratory system. Mitochondr Physiol Network 19.02. | ||
|authors=Legkun G, Motovilov K | |authors=Legkun G, Motovilov K | ||
|year=2014 | |year=2014 | ||
|event=[[ | |event=[[MiPNet19.02 IOC88]] | ||
|abstract= | |abstract=The [[electron transfer-pathway]] might function in many different states including physiological conditions and cannot be considered as united consecutive system. Major side mechanisms of electron transfer are shunt, set by hydrophilic quinones (such as duroquinine and menadione (Vitamin K3) which oxidize NADH and bring electrons to different sites of the respiratory system, establishing thereby alternative ways for electron transfer. Foresaid way is performed by DT-diaphorase, an alternative two-electron quinone reductase that “excludes” Complex I from [[Electron transfer pathway]]. Activity rate ratio of respiratory enzymes under such conditions was investigated on preparation of rat liver mitochondria. It is important to notice that limiting stage of ET-pathway under normal conditions is terminal stage – proton transfer through membrane surface – water boundary. However, under uncoupled conditions another step linked to individual enzyme function becomes limiting. To obtain insight into dependence “shunt” respiration on transmembrane potential, we investigated substrate oxidation depending on uncouplers of different structure (PCP, FCCP et al.) simultaneously with membrane potential of isolated mitochondria. | ||
|link= | |link= | ||
|mammals_and_models= | |mammals_and_models= | ||
| Line 12: | Line 12: | ||
|organism=Rat | |organism=Rat | ||
|tissues=Liver | |tissues=Liver | ||
|preparations=Isolated | |preparations=Isolated mitochondria | ||
|enzymes=Complex I | |enzymes=Complex I | ||
|topics=ADP, Inhibitor, Uncoupler | |||
|instruments=Oxygraph-2k, TPP | |instruments=Oxygraph-2k, TPP | ||
|link= | |link= | ||
|mammals_and_models= | |mammals_and_models= | ||
}} | }} | ||
Latest revision as of 09:43, 3 June 2020
| Legkun G, Motovilov K (2014) Investigation on alternative mechanism of electron transport in the respiratory system. Mitochondr Physiol Network 19.02. |
Link:
Legkun G, Motovilov K (2014)
Event: MiPNet19.02 IOC88
The electron transfer-pathway might function in many different states including physiological conditions and cannot be considered as united consecutive system. Major side mechanisms of electron transfer are shunt, set by hydrophilic quinones (such as duroquinine and menadione (Vitamin K3) which oxidize NADH and bring electrons to different sites of the respiratory system, establishing thereby alternative ways for electron transfer. Foresaid way is performed by DT-diaphorase, an alternative two-electron quinone reductase that “excludes” Complex I from Electron transfer pathway. Activity rate ratio of respiratory enzymes under such conditions was investigated on preparation of rat liver mitochondria. It is important to notice that limiting stage of ET-pathway under normal conditions is terminal stage – proton transfer through membrane surface – water boundary. However, under uncoupled conditions another step linked to individual enzyme function becomes limiting. To obtain insight into dependence “shunt” respiration on transmembrane potential, we investigated substrate oxidation depending on uncouplers of different structure (PCP, FCCP et al.) simultaneously with membrane potential of isolated mitochondria.
Labels: MiParea: Respiration
Organism: Rat
Tissue;cell: Liver
Preparation: Isolated mitochondria
Enzyme: Complex I
Regulation: ADP, Inhibitor, Uncoupler
HRR: Oxygraph-2k, TPP
