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- W2013996976 abstract "Considerable quantitative variations in the competitive inhibition of NADH oxidase activity of bovine heart submitochondrial particles (SMP) by different samples of NAD+ were observed. ADP-ribose (ADPR) was identified as the inhibitory contaminating substance responsible for variations in the inhibition observed. ADPR competitively inhibits NADH oxidation with Ki values (25°C, pH 8.0) of 26 μM, 30 μM, and 180 μM for SMP, purified Complex I and three-subunit NADH dehydrogenase (FP), respectively. ADPR decreases NADH-induced flavin reduction and prolongs the cyclic bleaching of FP during aerobic oxidation of NADH. Ki for inhibition of the rotenone-sensitive NADH oxidase in SMP by ADPR does not depend on Δμ̄H+. The initial rate of the energy-dependent NAD+ reduction by succinate is insensitive to ADPR. The inhibitor increases the steady-state level of NAD+ reduction reached during aerobic succinate-supported reverse electron transfer catalyzed by tightly coupled SMP. The results obtained are consistent with the proposal on different nucleotide-binding sites operating in the direct and reverse reactions catalyzed by the mitochondrial NADH-ubiquinone reductase." @default.
- W2013996976 created "2016-06-24" @default.
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- W2013996976 date "1997-07-01" @default.
- W2013996976 modified "2023-09-26" @default.
- W2013996976 title "A competitive inhibition of the mitochondrial NADH-ubiquinone oxidoreductase (Complex I) by ADP-ribose" @default.
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- W2013996976 doi "https://doi.org/10.1016/s0005-2728(97)00029-7" @default.
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