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

Shaw, Anthony L., Hochkoeppler, Alejandro, Bonora, Patrizia, Zannoni, Davide, Hanson, Graeme R. and Mcewan, Alastair G. (1999) Characterization of DorC from Rhodobacter capsulatus, a c-type Cytochrome Involved in Electron Transfer to Dimethylsulfoxide Reductase. Communication, 274 15: 9911-9914. doi:10.1074/jbc.274.15.9911

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Author Shaw, Anthony L.
Hochkoeppler, Alejandro
Bonora, Patrizia
Zannoni, Davide
Hanson, Graeme R.
Mcewan, Alastair G.
Title Characterization of DorC from Rhodobacter capsulatus, a c-type Cytochrome Involved in Electron Transfer to Dimethylsulfoxide Reductase
Formatted title
Characterization of DorC from Rhodobacter capsulatus, a c-type Cytochrome Involved in Electron Transfer to Dimethyl Sulfoxide Reductase
Journal name Communication   Check publisher's open access policy
ISSN 1083-351X
0021-9258
Publication date 1999-04-09
Sub-type Article (original research)
DOI 10.1074/jbc.274.15.9911
Open Access Status File (Publisher version)
Volume 274
Issue 15
Start page 9911
End page 9914
Total pages 4
Place of publication USA
Publisher The American Society of Biochemistry & Molecular Biology .
Collection year 1999
Language eng
Subject C1
270199 Biochemistry and Cell Biology not elsewhere classified
780105 Biological sciences
Abstract 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 Mr = 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 (alpha -band), 522 nm (beta -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.
Q-Index Code C1

Document type: Journal Article
Sub-type: Article (original research)
Collections: School of Chemistry and Molecular Biosciences
Centre for Advanced Imaging Publications
 
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