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Structure of a dioxygen reduction enzyme from Desulfovibrio gigas.

Authors: Frazão, Carlos; Silva, Gabriela; Gomes, Claudio; Matias, Pedro; Coelho, R; Sieker, L; Macedo, S; +7 Authors

Structure of a dioxygen reduction enzyme from Desulfovibrio gigas.

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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Keywords

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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citations
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
217
Top 10%
Top 1%
Top 1%
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