Legkun 2014 Abstract IOC 2014-04 Schroecken

Legkun (2014) ... . Mitochondr Physiol Network 19.02.

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Legkun G, Motovilov K (2014)

Event: IOC 2014-04 Schroecken

Electron Transport Chain might function in many different states including physiological conditions and cannot be considered as united consecutive system. Major side mechanism of electron transport is shunt, set by hydrophilic quinones(such as duroquinine and menadione(Vitamin K3)) which oxidize NADH and bring electrons to different sites of respiratory chain, establishing thereby alternative way for electron transport. Foresaid way is performed by DT-diaphorase, an alternative two-electron quinone reductase that “excludes” Complex I from ETC. 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 ETC under normal conditions is terminal stage – proton transfer through membrane surface – water boundary. However, under uncoupled condition another steps linked to individual enzyme function become limiting stage. To obtain insight into dependence “shunt” respiration on transmembrane potential, we investigate substrate oxidation rate 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 

HRR: Oxygraph-2k, TPP