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Biochem J. 1991 Feb 15;274 ( Pt 1):305-7.

Purification and properties of dimethyl sulphoxide reductase from Rhodobacter capsulatus. A periplasmic molybdoenzyme.

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1
School of Biochemistry, University of Birmingham, U.K.

Abstract

Dimethyl sulphoxide reductase was purified from the photosynthetic bacterium Rhodobacter capsulatus. The enzyme is composed of a single polypeptide of Mr 82,000 and contains a pterin-type molybdenum cofactor as the only detectable prosthetic group. The oxidized molybdenum cofactor of dimethyl sulphoxide reductase is a weak chromophore and exhibits broad absorption bands in the u.v.-visible-absorption spectral region. A distinct spectrum was generated upon addition of dithionite.

PMID:
2001248
PMCID:
PMC1149954
[Indexed for MEDLINE]
Free PMC Article
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