[Dynamic organization of the electron transport chain in bacterial membrane by radiation inactivation].
A complete cross-linking of proteins in isolated Micrococcus lysodeikticus membranes under effect of glutaric aldehyde causes 50% inhibition of the NADH-oxidase activity. Using the irradiation inactivation procedure, it was demonstrated that the size of the irradiation target for NADH-oxidase coincides with that for NADH-dehydrogenase and makes up to about 50 KD. In glutaric aldehyde-treated membranes the target size for NADH-oxidase is 3 times more than that, i.e. 150 KD. It is assumed that the effective electron transfer is mediated by a carrier assembly united into a supramolecular complex with a terminal life-time. Different assemblies exchange their components due to lateral diffusion of proteins in the membrane, which can account for the small size of the irradiation target for the oxidase activity.
D002462:Cell Membrane / Q000201:enzymology / Q000528:radiation effects; D004579:Electron Transport / Q000528:radiation effects; D007700:Kinetics; D008837:Micrococcus / Q000201:enzymology / Q000528:radiation effects*; D009097:Multienzyme Complexes / Q000378:metabolism; D009245:NADH Dehydrogenase / Q000378:metabolism; D009247:NADH, NADPH Oxidoreductases / Q000378:metabolism
D009097:Multienzyme Complexes; C023107:NADH oxidase; D009247:NADH, NADPH Oxidoreductases; D009245:NADH Dehydrogenase
Issledovanie dinamicheskoĭ organizatsii élektrontransportnoĭ tsepi v bakterial'noĭ membrane metodom radiatsionnoĭ inaktivatsii.