Legkun 2014 Abstract IOC 2014-04 Schroecken

Legkun G, Motovilov K (2014) Investigation on alternative mechanism of electron transport in the respiratory system. Mitochondr Physiol Network 19.02.

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Legkun G, Motovilov K (2014)

Event: IOC88

The electron transfer system 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 ETS. 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 ETS 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"Isolated Mitochondria" is not in the list (Intact organism, Intact organ, Permeabilized cells, Permeabilized tissue, Homogenate, Isolated mitochondria, SMP, Chloroplasts, Enzyme, Oxidase;biochemical oxidation, ...) of allowed values for the "Preparation" property.  Enzyme: Complex I  Regulation: ADP, Inhibitor, Uncoupler 

HRR: Oxygraph-2k, TPP