Structure of a dioxygen reduction enzyme from Desulfovibrio gigas View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2000-11-01

AUTHORS

C Frazão, G Silva, C M Gomes, P Matias, R Coelho, L Sieker, S Macedo, M Y Liu, S Oliveira, M Teixeira, A V Xavier, C Rodrigues-Pousada, M A Carrondo, J Le Gall

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. More... »

PAGES

1041-1045

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/80961

DOI

http://dx.doi.org/10.1038/80961

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1034621086

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/11062560


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