Structure of a dioxygen reduction enzyme from Desulfovibrio gigas.
pmid: 11062560
handle: 10174/2099
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 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.
- Universidade Nova de Lisboa Portugal
- University of Évora Portugal
Models, Molecular, Binding Sites, Iron, Molecular Sequence Data, Flavodoxin, Water, Crystallography, X-Ray, Ligands, ROO, Recombinant Proteins, beta-Lactamases, Protein Structure, Tertiary, Oxygen, Desulfovibrio, Amino Acid Sequence, Desulfovibrio gigas, Oxidoreductases, Dimerization, Oxidation-Reduction, Sequence Alignment, Phylogeny
Models, Molecular, Binding Sites, Iron, Molecular Sequence Data, Flavodoxin, Water, Crystallography, X-Ray, Ligands, ROO, Recombinant Proteins, beta-Lactamases, Protein Structure, Tertiary, Oxygen, Desulfovibrio, Amino Acid Sequence, Desulfovibrio gigas, Oxidoreductases, Dimerization, Oxidation-Reduction, Sequence Alignment, Phylogeny
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