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J Biol Chem, Vol. 274, Issue 15, 9911-9914, April 9, 1999

COMMUNICATION
Characterization of DorC from Rhodobacter capsulatus, a c-type Cytochrome Involved in Electron Transfer to Dimethyl Sulfoxide Reductase

Anthony L. Shaw, Alejandro Hochkoeppler^¶, Patrizia Bonora^¶, Davide Zannoni^¶, Graeme R. Hanson^**, and Alastair G. McEwan

From the  Department of Microbiology and ^** Centre for Magnetic Resonance, The University of Queensland, Brisbane 4072, Australia and the ^¶ Dipartimento di Biologia, Università di Bologna, 40126 Bologna, Italy

The dorC gene of the dimethyl sulfoxide respiratory (dor) operon of Rhodobacter capsulatus encodes a pentaheme c-type cytochrome that is involved in electron transfer from ubiquinol to periplasmic dimethyl sulfoxide reductase. DorC was expressed as a C-terminal fusion to an 8-amino acid FLAG epitope and was purified from detergent-solubilized membranes by ion exchange chromatography and immunoaffinity chromatography. The DorC protein had a subunit M_r = 46,000, and pyridine hemochrome analysis indicated that it contained 5 mol heme c/mol DorC polypeptide, as predicted from the derived amino acid sequence of the dorC gene. The reduced form of DorC exhibited visible absorption maxima at 551.5 nm (-band), 522 nm (-band), and 419 nm (Soret band). Redox potentiometry of the heme centers of DorC identified five components (n = 1) with midpoint potentials of 34, 128, 184, 185, and 276 mV. Despite the low redox potentials of the heme centers, DorC was reduced by duroquinol and was oxidized by dimethyl sulfoxide reductase.

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Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.

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