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. 1991 Feb 15;274(Pt 1):305–307. doi: 10.1042/bj2740305

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

A G McEwan 1, S J Ferguson 1, J B Jackson 1
PMCID: PMC1149954  PMID: 2001248

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.

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Selected References

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