We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Structure of a dioxygen reduction enzyme from Desulfovibrio gigas.
- Authors
Frazão, C; Silva, G; Gomes, C M; Matias, P; Coelho, R; Sieker, L; Macedo, S; Liu, M Y; Oliveira, S; Teixeira, M; Xavier, A V; Rodrigues-Pousada, C; Carrondo, M A; Le Gall, J
- Abstract
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 A 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-beta-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.
- Publication
Nature structural biology, 2000, Vol 7, Issue 11, p1041
- ISSN
1072-8368
- Publication type
Journal Article
- DOI
10.1038/80961