[Reaction of complex I of the mitochondrial electron transport chain with artificial oxidizers].
The steady-state kinetics of oxidation of the mitochondrial NADH: ubiquinone oxidoreductase (complex I, EC 1.6.99.3) by artificial electron acceptors--p-quinones and inorganic complexes has been investigated. A limiting stage in the NADH: ferricyanide reductase reaction is a reductive half-reaction. Ferricyanide interacts with negative-charged protein groups taking part in the NADH binding. The rate constants of the quinone reduction by complex I vary from 1.10(6) to 4.10(3) M-1s-1. The NADH, NAD+ and ADP-ribose inhibition data indicate that oxidizers in the rotenono-insensitive reaction interact with the redox centre near the NAD+/NADH binding site, most probably with FMN.
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D000246:Adenosine Diphosphate Ribose / Q000037:antagonists & inhibitors; D000818:Animals; D002417:Cattle; D004579:Electron Transport; D005295:Ferrocyanides / Q000378:metabolism; D007700:Kinetics; D008929:Mitochondria, Heart / Q000201:enzymology* / Q000378:metabolism; D009243:NAD / Q000037:antagonists & inhibitors; D016660:NAD(P)H Dehydrogenase (Quinone); D010084:Oxidation-Reduction; D011808:Quinone Reductases / Q000378:metabolism*; D011809:Quinones / Q000378:metabolism*
D005295:Ferrocyanides; D011809:Quinones; D009243:NAD; D000246:Adenosine Diphosphate Ribose; D016660:NAD(P)H Dehydrogenase (Quinone); D011808:Quinone Reductases; C020354:hexacyanoferrate II
Reaktsii kompleksa I mitokhondrial'noĭ tsepi transporta élektronov s iskusstvennymi okisliteliami.