Structure of a dioxygen reduction enzyme from Desulfovibrio gigas

Carlos Frazão, Gabriela G. F. Silva, Cláudio M. Gomes, Pedro Matias, Ricardo Coelho, Larry Sieker, Sofia Macedo, Ming Y. Liu, Solange Oliveira, Miguel Teixeira, António V. Xavier, Claudina Rodrigues-Pousada, Maria A. Carrondo, Jean Le Gall

Research output: Contribution to journalArticlepeer-review

33 Citations (Scopus)


Desulfovibrio gigas is a strict anaerobe that contains a well-characterized metabolic pathway that enables it to survive transient contacts with oxygen. The terminal enzyme in this pathway, rubredoxin: Oxygen oxidoreductase (ROO) reduces oxygen to water in a direct and safe way. The 2.5 ∅ resolution crystal structure of ROO shows that each monomer of this homodimeric enzyme consists of a novel combination of two domains, a flavodoxin-like domain and a Zn-β-lactamase-like domain that contains a di-iron center for dioxygen reduction. This is the first structure of a member of a superfamily of enzymes widespread in strict and facultative anaerobes, indicating its broad physiological significance.

Original languageEnglish
Pages (from-to)1041-1045
Number of pages5
JournalNature Structural Biology
Issue number11
Publication statusPublished - 18 Nov 2000


  • oxygen oxidoreductase
  • water
  • beta lactamase
  • flavodoxin
  • iron
  • monomer
  • oxidoreductase
  • unclassified drug
  • rubredoxin
  • oxygen


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