Structure of a dioxygen reduction enzyme from Desulfovibrio gigas |
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Authors: | Frazão C Silva G Gomes C M Matias P Coelho R Sieker L Macedo S Liu M Y Oliveira S Teixeira M Xavier A V Rodrigues-Pousada C Carrondo M A Le Gall J |
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Affiliation: | Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Av. da República, Apartado 127, 2781-901 Oeiras, Portugal. |
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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. |
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