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

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.

SUBMITTER: McEwan AG 

PROVIDER: S-EPMC1149954 | biostudies-other | 1991 Feb

REPOSITORIES: biostudies-other