Structure of a dioxygen reduction enzyme from Desulfovibrio gigas

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 Angstrom reso...

Full description

Bibliographic Details
Main Author: Frazão, Carlos (author)
Other Authors: Silva, Gabriela (author), Gomes, Claudio (author), Matias, Pedro (author), Coelho, R (author), Sieker, L (author), Macedo, S (author), Liu, MY (author), Oliveira, Solange (author), Teixeira, Miguel (author), Xavier, António V. (author), Rodrigues-Pousada, Claudina (author), Carrondo, M. Arménia (author), LeGall, Jean (author)
Format: article
Language:eng
Published: 2010
Subjects:
ROO
Desulfovibrio gigas
Online Access:http://hdl.handle.net/10174/2099
Country:Portugal
Oai:oai:dspace.uevora.pt:10174/2099
Description
Summary: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 Angstrom 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.

Similar Items