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...

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Detalhes bibliográficos
Autor principal: Frazão, Carlos (author)
Outros Autores: 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)
Formato: article
Idioma:eng
Publicado em: 2010
Assuntos:
ROO
Desulfovibrio gigas
Texto completo:http://hdl.handle.net/10174/2099
País:Portugal
Oai:oai:dspace.uevora.pt:10174/2099
Descrição
Resumo: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.

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