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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 Å 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-β-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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Figure 1: Oxygen scavenging by ROO.
Figure 2: ROO is a modular enzyme.
Figure 3: 3 ROO catalytic site.

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Acknowledgements

We thank the University of Georgia fermentation plant for growing the bacteria, G. Leonard and V. Stojanoff (ESRF, Grenoble) and A. Thompson (EMBL, Grenoble) for help with data collection, M. Regalla (ITQB) for HPLC flavin analysis. This work was supported by grants from the NIH and PRAXIS XXI.

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Correspondence to Maria A. Carrondo.

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Frazão, C., Silva, G., Gomes, C. et al. Structure of a dioxygen reduction enzyme from Desulfovibrio gigas . Nat Struct Mol Biol 7, 1041–1045 (2000). https://doi.org/10.1038/80961

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