Cytochrome c biogenesis: the Ccm system
Open accessAbstract
Cytochromes of c-type contain covalently attached hemes that are formed via thioether bonds between the vinyls of heme b and cysteines within C(1)XXC(2)H motifs of apocytochromes. In diverse organisms this post-translational modification relies on membrane-associated specific biogenesis proteins, referred to as cytochrome c maturation (Ccm) systems. A highly complex version of these systems, Ccm or System I, is found in Gram-negative bacteria, archaea and plant mitochondria. We describe emerging functional interactions between the Ccm components categorized into three conserved modules, and present a mechanistic view of the molecular basis of ubiquitous vinyl-2 approximately Cys(1) and vinyl-4 approximately Cys(2) heme b-apocytochrome thioether bonds in c-type cytochromes.
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These proteins belong to the cytochrome c maturation (Ccm) system I, which is composed of eight constituents (CcmABCDEFGH).
“These proteins belong to the cytochrome c maturation (Ccm) system I, which is composed of eight constituents (CcmABCDEFGH)33,34.”
From AF2Complex predicts direct physical interactions in multimeric proteins with deep learning (2022) · cites this paper as [33]
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- Authors
- Sanders, C., Turkarslan, S., Lee, D.-W., & Daldal, F.
- Affiliations
- Kutztown University (US)
- University of Pennsylvania (US)
- Corresponding author
- Daldal, Fevzi
- Venue
- Trends in Microbiology
- Publisher
- Elsevier BV
- Published
- 2010-06
- Volume
- 18
- Issue
- 6
- Pages
- 266-274
- ISSN
- 0966-842X (ISSN-L)
- PMC
- PMC2916975
- OpenAlex
- W2089527589
- Cited by
- 197
- References
- 65
- Citations by year
- 2026: 7 · 2025: 10 · 2024: 11 · 2023: 17 · 2022: 18 · 2021: 18 · 2020: 11 · 2019: 8 · 2018: 5 · 2017: 6 · 2016: 7 · 2015: 10 · 2014: 7 · 2013: 16 · 2012: 16
- FWCI
- 0.68
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Trends in Microbiology (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute of General Medical Sciences (GM38237, R01GM038237)
- Topics
- Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › Metalloenzymes and iron-sulfur proteins
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Keywords
- cytochrome c biogenesis, c-type cytochromes, heme b, post-translational modification, Gram-negative bacteria, archaea, plant mitochondria, heme attachment
- MeSH terms
- Rhodophyta, Archaea, Bacteria, Bacterial Outer Membrane Proteins, Bacterial Proteins, Cysteine, Heme, Mitochondria, Plant Proteins, Plants, Protein Processing, Post-Translational, Sulfides, Archaeal Proteins, Cytochromes c
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