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  • Title: Purification and properties of dimethyl sulphoxide reductase from Rhodobacter capsulatus. A periplasmic molybdoenzyme.
    Author: McEwan AG, Ferguson SJ, Jackson JB.
    Journal: Biochem J; 1991 Feb 15; 274 ( Pt 1)(Pt 1):305-7. PubMed ID: 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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