Article
Oxygen reactivity of an NADH oxidase C42S mutant: evidence for a C(4a)-peroxyflavin intermediate and a rate-limiting conformational change.
Biochemistry - 16 Jun 1998
Mallett T C, Claiborne A
Abstract excerpt
The flavoprotein NADH oxidase (O2 --> 2H2O) from Enterococcus faecalis 10C1 contains a cysteinyl redox center, in addition to FAD. We have proposed a cysteine-sulfenic acid (Cys-SOH) structure for the oxidized form of Cys42; the presence of this redox center is consistent with the stoichiometries reported for earlier reductive titrations of wild-type oxidase, and we have proposed that Cys42-SH plays a key role in...
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