WrbA bridges bacterial flavodoxins and eukaryotic NAD(P)H:quinone oxidoreductases
Jannette Carey1, Jiri Brynda, Julie Wolfová
1Chemistry Department, Princeton University, Princeton, New Jersey 08544-1009, USA. jcarey@princeton.edu
Abstract:
The crystal structure of the flavodoxin-like protein WrbA with oxidized FMN bound reveals a close relationship to mammalian NAD(P)H:quinone oxidoreductase, Nqo1. Structural comparison of WrbA, flavodoxin, and Nqo1 indicates how the twisted open-sheet fold of flavodoxins is elaborated to form multimers that extend catalytic function from one-electron transfer between protein partners using FMN to two-electron reduction of xenobiotics using FAD. The structure suggests a novel physiological role for WrbA and Nqo1.
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