Structure of a dioxygen reduction enzyme from Desulfovibrio gigas

Citation
C. Frazao et al., Structure of a dioxygen reduction enzyme from Desulfovibrio gigas, NAT ST BIOL, 7(11), 2000, pp. 1041-1045
Citations number
33
Categorie Soggetti
Biochemistry & Biophysics
Journal title
NATURE STRUCTURAL BIOLOGY
ISSN journal
10728368 → ACNP
Volume
7
Issue
11
Year of publication
2000
Pages
1041 - 1045
Database
ISI
SICI code
1072-8368(200011)7:11<1041:SOADRE>2.0.ZU;2-X
Abstract
Desulfovibrio gigas is a strict anaerobe that contains a well-characterized metabolic pathway that enables it to survive transient contacts with oxyge n. The terminal enzyme in this pathway, rubredoxin:oxygen oxidoreductase (R OO) reduces oxygen to water in a direct and safe way. The 2.5 Angstrom reso lution crystal structure of ROO shows that each monomer of this homodimeric enzyme consists of a novel combination of two domains, a flavodoxin-like d omain and a Zn-beta -lactamase-like domain that contains a di-iron center f or dioxygen reduction. This is the first structure of a member of a superfa mily of enzymes widespread in strict and facultative anaerobes, indicating its broad physiological significance.