Oxygen reactivity of an NADH oxidase C42S mutant: evidence for a C(4a)-peroxyflavin intermediate and a rate-limiting conformational change.

doi:10.1021/bi9803630

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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...

Topics

Enterococcus faecalis
Flavins
Multienzyme Complexes
Mutation
NADH, NADPH Oxidoreductases
Oxidation-Reduction
Protein Conformation
Structure-Activity Relationship

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