WrbA bridges bacterial flavodoxins and eukaryotic NAD(P)H:quinone oxidoreductases

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.