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

Research output: Contribution to journalArticle


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.


  • Jannette Carey
  • Jiri Brynda
  • Julie Wolfova
  • Rita Grandori
  • Tobias Gustavsson
  • Ruediger Ettrich
  • Ivana Kuta Smatanova
Research areas and keywords

Subject classification (UKÄ) – MANDATORY

  • Biological Sciences


  • vitamin K, menaquinone, peripheral membrane proteins, soluble quinones, membrane quinones, chemotherapeutics, shikimate
Original languageEnglish
Pages (from-to)2301-2305
JournalProtein Science
Issue number10
Publication statusPublished - 2007
Publication categoryResearch