ReviewMicrobiology and molecular biology reviews : MMBR2009
Cytochrome c biogenesis: mechanisms for covalent modifications and trafficking of heme and for heme-iron redox control.
Review in Microbiology and molecular biology reviews : MMBR, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 152 papers.
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Who cites it
152 citing papers in PubMed, 263 citations in OpenAlex.
- Inhibitors of cytochromemBio · 2026Article
- Dynamic Additive Scanning for Precise Control in Electrospray Ionization Mass Spectrometry.ACS measurement science au · 2026Article
- Analysis of putative heme ligands in the System I bacterial cytochromeMicrobiology spectrum · 2026Article
- Genomic and Functional Characterization ofFrontiers in microbiology · 2026Article
- Comparative transcriptomic analysis of perfluoroalkyl substances-induced responses of exponential and stationary phase Escherichia coli.BMC genomics · 2025Article
- Regulation of iron homeostasis by Fur and atypical response regulator SsoR via derepressor-inhibitor oscillation inApplied and environmental microbiology · 2025Article
- From genes to function: regulation, maturation, and evolution of cytochromeApplied and environmental microbiology · 2025Review
- Mechanisms of heme transport in the mitochondria.Biochemical Society transactions · 2025Review
- Cytosolic cytochrome c represses ferroptosis.Cell metabolism · 2025Article
- Article
- Biogenesis of CytochromesACS infectious diseases · 2025Article
- Article
- Pulling back the mitochondria's iron curtain.npj metabolic health and disease · 2025Review
- Novel virulence-related genes that contribute to clinical infections ofGenes & diseases · 2025Article
- Phyllosphere of senescent crops as a microbial NFrontiers in microbiology · 2025Article
- Hydrodynamic flow and benthic boundary layer interactions shape the microbial community in Milos shallow water hydrothermal vents.Frontiers in microbiology · 2025Article
- Recent advances in microbial synthesis of free heme.Applied microbiology and biotechnology · 2024Review
- The Neural Palette of Heme: Altered Heme Homeostasis Underlies Defective Neurotransmission, Increased Oxidative Stress, and Disease Pathogenesis.Antioxidants (Basel, Switzerland) · 2024Review
- Structural Insights into Mechanisms Underlying Mitochondrial and Bacterial Cytochrome c Synthases.Biomolecules · 2024Article
- The predicted secreted proteome of activated sludge microorganisms indicates distinct nutrient niches.mSystems · 2024Article
92 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Heme is the prosthetic group for cytochromes, which are directly involved in oxidation/reduction reactions inside and outside the cell. Many cytochromes contain heme with covalent additions at one or both vinyl groups. These include farnesylation at one vinyl in hemes o and a and thioether linkages to each vinyl in cytochrome c (at CXXCH of the protein). Here we review the mechanisms for these covalent attachments, with emphasis on the three unique cytochrome c assembly pathways called systems I, II, and III. All proteins in system I (called Ccm proteins) and system II (Ccs proteins) are integral membrane proteins. Recent biochemical analyses suggest mechanisms for heme channeling to the outside, heme-iron redox control, and attachment to the CXXCH. For system II, the CcsB and CcsA proteins form a cytochrome c synthetase complex which specifically channels heme to an external heme binding domain; in this conserved tryptophan-rich "WWD domain" (in CcsA), the heme is maintained in the reduced state by two external histidines and then ligated to the CXXCH motif. In system I, a two-step process is described. Step 1 is the CcmABCD-mediated synthesis and release of oxidized holoCcmE (heme in the Fe(+3) state). We describe how external histidines in CcmC are involved in heme attachment to CcmE, and the chemical mechanism to form oxidized holoCcmE is discussed. Step 2 includes the CcmFH-mediated reduction (to Fe(+2)) of holoCcmE and ligation of the heme to CXXCH. The evolutionary and ecological advantages for each system are discussed with respect to iron limitation and oxidizing environments.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.