Structure of a dioxygen reduction enzyme from Desulfovibrio gigas

dc.contributor.authorFrazão, Carlos
dc.contributor.authorSilva, Gabriela
dc.contributor.authorGomes, Claudio
dc.contributor.authorMatias, Pedro
dc.contributor.authorCoelho, R
dc.contributor.authorSieker, L
dc.contributor.authorMacedo, S
dc.contributor.authorLiu, MY
dc.contributor.authorOliveira, Solange
dc.contributor.authorTeixeira, Miguel
dc.contributor.authorXavier, António V.
dc.contributor.authorRodrigues-Pousada, Claudina
dc.contributor.authorCarrondo, M. Arménia
dc.contributor.authorLeGall, Jean
dc.date.accessioned2010-09-27T14:40:55Z
dc.date.available2010-09-27T14:40:55Z
dc.date.issued2000
dc.description.abstractDesulfovibrio 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.en
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dc.identifier.pagina1041-1045en
dc.identifier.revistaNATURE STRUCTURAL BIOLOGYen
dc.identifier.scientificarea552en
dc.identifier.urihttp://hdl.handle.net/10174/2099
dc.identifier.volume7en
dc.language.isoeng
dc.peerreviewedyesen
dc.rightsopenAccessen
dc.subjectROOen
dc.subjectDesulfovibrio gigasen
dc.titleStructure of a dioxygen reduction enzyme from Desulfovibrio gigasen
dc.typearticleen

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