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- W2419297345 abstract "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." @default.
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- W2419297345 date "1990-02-15" @default.
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- W2419297345 title "The carbanion of nitroethane is an inhibitor of, and not a substrate for, flavocytochrome <i>b</i>2 [<scp>l</scp>-(+)-lactate dehydrogenase]" @default.
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- W2419297345 doi "https://doi.org/10.1042/bj2660301" @default.
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