The carbanion of nitroethane is an inhibitor of, and not a substrate for, flavocytochrome b2 [l-(+)-lactate dehydrogenase]
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Although nitroethane does not bind to the active site of flavocytochrome b2, its anion, ethane nitronate, behaves as a competitive inhibitor, with a Ki of 2.2 mM. No electron transfer can be detected between the nitronate and the enzyme, in contrast with the observations of other workers on D-amino acid oxidase. Propionate is a competitive inhibitor, with a Ki of 28 mM. The significance of these results with respect to the proposed carbanion mechanism and the putative existence of a covalent enzyme-substrate intermediate is discussed.
1996 ◽
Vol 93
(15)
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pp. 7496-7501
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1963 ◽
Vol 67
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pp. 319-320
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2021 ◽
pp. 113448
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1963 ◽
Vol 77
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pp. 20-26
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