ArticleMetallomics : integrated biometal science2011
Comparing substrate specificity between cytochrome c maturation and cytochrome c heme lyase systems for cytochrome c biogenesis.
Article in Metallomics : integrated biometal science, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 34 citations in OpenAlex.
- Heme in Bacterial Pathogenesis and as an Antimicrobial Target.Chemical reviews · 2025Review
- Structural Insights into Mechanisms Underlying Mitochondrial and Bacterial Cytochrome c Synthases.Biomolecules · 2024Article
- Helicobacter pylori and Campylobacter jejuni bacterial holocytochrome c synthase structure-function analysis reveals conservation of heme binding.Communications biology · 2024Article
- Genetically Encoded Fluorescent Probe for Detection of Heme-Induced Conformational Changes in Cytochrome c.Biosensors · 2023Article
- Cryo-EM of CcsBA reveals the basis for cytochrome c biogenesis and heme transport.Nature chemical biology · 2022Article
- In vitro reconstitution reveals major differences between human and bacterial cytochrome c synthases.eLife · 2021Article
- Discovery of a functional, contracted heme-binding motif within a multiheme cytochrome.The Journal of biological chemistry · 2019Article
- Influence of heme c attachment on heme conformation and potential.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018Article
- Engineered holocytochromeProceedings of the National Academy of Sciences of the United States of America · 2017Article
- Molecular Basis Behind Inability of Mitochondrial Holocytochrome c Synthase to Mature Bacterial Cytochromes: DEFINING A CRITICAL ROLE FOR CYTOCHROME c α HELIX-1.The Journal of biological chemistry · 2016Article
- Mitochondrial cytochrome c biogenesis: no longer an enigma.Trends in biochemical sciences · 2015Review
- Mechanisms of mitochondrial holocytochrome c synthase and the key roles played by cysteines and histidine of the heme attachment site, Cys-XX-Cys-His.The Journal of biological chemistry · 2014Article
- Substrate recognition of holocytochrome c synthase: N-terminal region and CXXCH motif of mitochondrial cytochrome c.FEBS letters · 2014Article
- The role of key residues in structure, function, and stability of cytochrome-c.Cellular and molecular life sciences : CMLS · 2014Review
- Human mitochondrial holocytochrome c synthase's heme binding, maturation determinants, and complex formation with cytochrome c.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Recombinant expression, biophysical characterization, and cardiolipin-induced changes of two Caenorhabditis elegans cytochrome c proteins.Biochemistry · 2013Article
- Protein Machineries Involved in the Attachment of Heme to Cytochrome c: Protein Structures and Molecular Mechanisms.Scientifica · 2013Review
- Engineering a prokaryotic apocytochrome c as an efficient substrate for Saccharomyces cerevisiae cytochrome c heme lyase.Biochemical and biophysical research communications · 2012Article
- Thiol redox requirements and substrate specificities of recombinant cytochrome c assembly systems II and III.Biochimica et biophysica acta · 2012Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Hemes c are characterized by their covalent attachment to a polypeptide via a widely conserved CXXCH motif. There are multiple biological systems that facilitate heme c biogenesis. System I, the cytochrome c maturation (CCM) system, is found in many bacteria and is commonly employed in the maturation of bacterial cytochromes c in Escherichia coli-based expression systems. System III, cytochrome c heme lyase (CCHL), is an enzyme found in the mitochondria of many eukaryotes and is used for heterologous expression of mitochondrial holocytochromes c. To test CCM specificity, a series of Hydrogenobacter thermophilus cytochrome c(552) variants was successfully expressed and matured by the CCM system with CX(n)CH motifs where n = 1-4, further extending the known substrate flexibility of the CCM system by successful maturation of a bacterial cytochrome c with a novel CXCH motif. Horse cytochrome c variants with both expanded and contracted attachment motifs (n = 1-3) were also tested for expression and maturation by both CCM and CCHL, allowing direct comparison of CCM and CCHL substrate specificities. Successful maturation of horse cytochrome c by CCHL with an extended CXXXCH motif was observed, demonstrating that CCHL shares the ability of CCM to mature hemes c with extended heme attachment motifs. In contrast, two single amino acid mutants were found in horse cytochrome c that severely limit maturation by CCHL, yet were efficiently matured with CCM. These results identify potentially important residues for the substrate recognition of CCHL.
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