ArticleFEBS letters2014
Substrate recognition of holocytochrome c synthase: N-terminal region and CXXCH motif of mitochondrial cytochrome c.
Article in FEBS letters, 2014. 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.
- Biogenesis of CytochromesACS infectious diseases · 2025Article
- Structural Insights into Mechanisms Underlying Mitochondrial and Bacterial Cytochrome c Synthases.Biomolecules · 2024Article
- Biogenesis of cytochromesbioRxiv : the preprint server for biology · 2024Article
- Helicobacter pylori and Campylobacter jejuni bacterial holocytochrome c synthase structure-function analysis reveals conservation of heme binding.Communications biology · 2024Article
- In vitro reconstitution reveals major differences between human and bacterial cytochrome c synthases.eLife · 2021Article
- Divergent CytochromemBio · 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
- Effects of protein structure on iron-polypeptide vibrational dynamic coupling in cytochrome c.Biochemistry · 2015Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Holocytochrome c synthase (HCCS) attaches heme covalently to mitochondrial respiratory cytochromes c. Little is known about the reaction of heme attachment to apocytochromes c by HCCS, although recently it has been established that the CXXCH motif and the N-terminus of the apocytochrome polypeptide are important protein-protein recognition motifs. Here, we explore further the important features of the N-terminal sequence and investigate what variations in the CXXCH residues are productively recognised by HCCS in its substrate.
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