Tools
ToolsYu, Jun and Le Brun, Nick E. (1998) Studies of the cytochrome subunits of menaquinone:Cytochrome c reductase (bc complex) of Bacillus subtilis. Evidence for the covalent attachment of heme to the cytochrome b subunit. Journal of Biological Chemistry, 273 (15). pp. 8860-8866. ISSN 0021-9258
Full text not available from this repository.Abstract
The menaquinone:cytochrome c reductase, or bc complex of Bacillus subtilis belongs to a third class of bc-type complex, distinct bc1 and b6f classes. Using a mutagenesis approach, we demonstrate that the cytochrome b (QcrB) and c (QcrC) subunits of the complex give rise to bands at 22 and 29 kDa, respectively, after denaturing electrophoresis; that both subunits are required for proper complex assembly and/or stability; and that subunits retain one heme molecule under denaturing conditions. This unusual property of a b-type cytochrome was investigated further. We present evidence for the existence of a covalent linkage between the polypeptide and heme b(H) and of an important role for Cys43 in binding of heme b(H). It is proposed that heme is also covalently attached to the cytochrome b subunit of b6f complexes of chloroplasts and cyanobacteria.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | biochemistry,molecular biology,cell biology ,/dk/atira/pure/subjectarea/asjc/1300/1303 |
| Faculty \ School: | 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/99606 |
| DOI: | 10.1074/jbc.273.15.8860 |
Actions (login required)
 |
View Item |