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ToolsErlendsson, Lýour S., Acheson, Richard M., Hederstedt, Lars and Le Brun, Nick E. (2003) Bacillus subtilis ResA is a thiol-disulfide oxidoreductase involved in cytochrome c synthesis. Journal of Biological Chemistry, 278 (20). pp. 17852-17858. ISSN 0021-9258
Full text not available from this repository.Abstract
Covalent attachment of heme to apocytochromes c in bacteria occurs on the outside of the cytoplasmic membrane and requires two reduced cysteinyls at the heme binding site. A constructed ResA-deficient Bacillus subtilis strain was found to lack c-type cytochromes. Cytochrome c synthesis was restored in the mutant by: (i) in trans expression of resA; (ii) deficiency in BdbD, a thioldisulfide oxidoreductase that catalyzes formation of an intramolecular disulfide bond in apocytochrome c after transfer of the polypeptide across the cytoplasmic membrane; or (iii) by addition of the reductant dithiothreitol to the growth medium. In vivo studies of ResA showed that it is membrane-associated with its thioredoxin-like domain on the outside of the cytoplasmic membrane. Analysis of a soluble form of the protein revealed two redox reactive cysteine residues with a midpoint potential of about -340 mV at pH 7. We conclude that ResA, probably together with another thiol-disulfide oxidoreductase, CcdA, is required for the reduction of the cysteinyls in the heme binding site of apocytochrome c.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | biochemistry,molecular biology,cell biology ,/dk/atira/pure/subjectarea/asjc/1300/1303 |
| Faculty \ School: | Faculty of Science > School of Chemical Sciences and Pharmacy (former - to 2009) Faculty of Science > School of Chemistry (former - to 2024) |
| UEA Research Groups: | Faculty of Science > Research Centres > Centre for Molecular and Structural Biochemistry Faculty of Science > Research Groups > Chemistry of Life Processes |
| Related URLs: | |
| Depositing User: | LivePure Connector |
| Date Deposited: | 18 Jun 2025 09:30 |
| Last Modified: | 18 Jun 2025 09:30 |
| URI: | https://ueaeprints.uea.ac.uk/id/eprint/99600 |
| DOI: | 10.1074/jbc.M300103200 |
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