Crystallographic analyses of NADH peroxidase Cys42Ala and Cys42Ser mutants: active site structures, mechanistic implications, and an unusual environment of Arg 303.

Abstract excerpt

NADH peroxidase from Enterococcus faecalis is a tetrameric flavoenzyme of 201,400 Da which employs Cys 42 as a redox-active center cycling between sulfhydryl (Cys-SH) and sulfenic acid (Cys-SOH) states along the catalytic pathway. The role of the active site cysteine 42 in NADH peroxidase has been elucidated using biochemical and crystallographic techniques. Here we describe the crystal structures of two active...

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