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 A resolution...

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Veröffentlicht in:Nature structural & molecular biology 2000-11, Vol.7 (11), p.1041-1045
Hauptverfasser: Carrondo, Maria A, Frazão, Carlos, Silva, Gabriela, Gomes, Cláudio M, Matias, Pedro, Coelho, Ricardo, Sieker, Larry, Macedo, Sofia, Liu, Ming Y, Oliveira, Solange, Teixeira, Miguel, Xavier, António V, Rodrigues-Pousada, Claudina, Le Gall, Jean
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Sprache:eng
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Zusammenfassung: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.
ISSN:1072-8368
1545-9993
2331-365X
1545-9985
DOI:10.1038/80961