Hartshorne, R. S. ; Richardson, D. J. ; Simon, J. (2006)
Multiple haem lyase genes indicate substrate specificity in cytochrome c biogenesis.
In: Biochemical Society transactions, 34 (Pt 1)
Article, Bibliographie
Abstract
c-Type cytochromes are a widespread class of proteins that play a vital role in the energy-conserving metabolism of prokaryotic and eukaryotic organisms. The key event in cytochrome c biogenesis is the covalent attachment of the haem cofactor to two (or rarely one) cysteine residues arranged in a haem c-binding motif such as CX(2-4)CH, CXXCK or X(3)CH. This reaction is catalysed by the membrane-bound enzyme CCHL (cytochrome c haem lyase). Different CCHLs have been described and some of them are dedicated to distinct haem c-binding motifs of cytochromes that are encoded in the vicinity of the respective CCHL gene. Various bacterial genomes contain multiple copies of CCHL-encoding genes, suggesting the presence of non-conventional or even as yet unrecognized haem c-binding motifs. This assumption is exemplified in the present study using the proteobacterium Wolinella succinogenes as a model organism whose genome encodes three CCHL isoenzymes. The discovery of a novel conserved multihaem cytochrome c (MccA) is described.
| Item Type: | Article |
|---|---|
| Erschienen: | 2006 |
| Creators: | Hartshorne, R. S. ; Richardson, D. J. ; Simon, J. |
| Type of entry: | Bibliographie |
| Title: | Multiple haem lyase genes indicate substrate specificity in cytochrome c biogenesis. |
| Language: | English |
| Date: | 2006 |
| Journal or Publication Title: | Biochemical Society transactions |
| Volume of the journal: | 34 |
| Issue Number: | Pt 1 |
| Abstract: | c-Type cytochromes are a widespread class of proteins that play a vital role in the energy-conserving metabolism of prokaryotic and eukaryotic organisms. The key event in cytochrome c biogenesis is the covalent attachment of the haem cofactor to two (or rarely one) cysteine residues arranged in a haem c-binding motif such as CX(2-4)CH, CXXCK or X(3)CH. This reaction is catalysed by the membrane-bound enzyme CCHL (cytochrome c haem lyase). Different CCHLs have been described and some of them are dedicated to distinct haem c-binding motifs of cytochromes that are encoded in the vicinity of the respective CCHL gene. Various bacterial genomes contain multiple copies of CCHL-encoding genes, suggesting the presence of non-conventional or even as yet unrecognized haem c-binding motifs. This assumption is exemplified in the present study using the proteobacterium Wolinella succinogenes as a model organism whose genome encodes three CCHL isoenzymes. The discovery of a novel conserved multihaem cytochrome c (MccA) is described. |
| Divisions: | 10 Department of Biology > Microbial Energy Conversion and Biotechnology ?? fb10_mikrobiologie ?? 10 Department of Biology |
| Date Deposited: | 07 Dec 2010 15:19 |
| Last Modified: | 05 Mar 2013 09:42 |
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