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Multiple haem lyase genes indicate substrate specificity in cytochrome c biogenesis
S Hartshorne1, D J Richardson, J Simon
1School of Biological Sciences, University of East Anglia, Norwich NR4 7TJ, UK.
Biochemical Society Transactions
|January 19, 2006
Summary
Cytochrome c biogenesis involves attaching haem cofactors, catalyzed by cytochrome c haem lyase (CCHL). This study reveals a novel multihaem cytochrome c (MccA) in Wolinella succinogenes, expanding our understanding of these vital proteins.
Area of Science:
- Biochemistry
- Molecular Biology
- Microbiology
Background:
- c-Type cytochromes are crucial for energy metabolism in all organisms.
- Their biogenesis requires covalent attachment of haem to cysteine residues, catalyzed by cytochrome c haem lyase (CCHL).
- Bacterial genomes often contain multiple CCHL genes, suggesting diverse haem-binding motifs.
Purpose of the Study:
- To investigate the role of multiple CCHL isoenzymes in Wolinella succinogenes.
- To identify novel cytochrome c biogenesis pathways and motifs.
- To characterize a newly discovered multihaem cytochrome c (MccA).
Main Methods:
- Genomic analysis of Wolinella succinogenes to identify CCHL genes.
- Biochemical assays to study CCHL activity and haem attachment.
- Protein characterization of the novel MccA.
Main Results:
- Wolinella succinogenes encodes three distinct CCHL isoenzymes.
- A novel conserved multihaem cytochrome c, MccA, was discovered.
- Evidence suggests MccA utilizes a non-canonical haem-binding motif.
Conclusions:
- Multiple CCHL isoenzymes contribute to the diversity of cytochrome c structures.
- The discovery of MccA highlights previously unrecognized pathways in cytochrome c biogenesis.
- This work expands the known repertoire of haem c-binding motifs and cytochrome c functions.