ArticleBiochemical and biophysical research communications2012
Engineering a prokaryotic apocytochrome c as an efficient substrate for Saccharomyces cerevisiae cytochrome c heme lyase.
Article in Biochemical and biophysical research communications, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 10 citations in OpenAlex.
- Inhibitors of cytochromemBio · 2026Article
- Investigation of the Molecular Mechanisms of the Eukaryotic Cytochrome-Biomolecules · 2022Article
- In vitro reconstitution reveals major differences between human and bacterial cytochrome c synthases.eLife · 2021Article
- 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
- Cytochrome c biogenesis System I: an intricate process catalyzed by a maturase supercomplex?Biochimica et biophysica acta · 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
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
Cytochromes c are heme proteins that require multiple maturation components, such as heme lyases, for cofactor incorporation. Saccharomyces cerevisiae has two heme lyases that are specific for apocytochromes c (CCHL) or c(1) (CC(1)HL). CCHL can covalently attach heme b groups to apocytochrome c substrates of eukaryotic but not prokaryotic origin. Besides their conserved Cys-Xxx-Xxx-Cys-His heme-binding motifs, the amino-terminal regions of apocytochrome c substrates appear to be important for CCHL function. In this study, we show for the first time that only two amino acid changes in the amino-terminal region of the non-CCHL substrate apocytochrome c(2) from Rhodobacter capsulatus are necessary and sufficient for efficient holocytochrome c formation by CCHL. This finding led us to propose a consensus sequence located at the amino-terminus of apocytochromes c, and critical for substrate recognition and heme ligation by CCHL.
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Registered trials
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