ReviewThe FEBS journal2011
Cytochrome c biogenesis System I.
Review in The FEBS journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
42 citing papers in PubMed, 94 citations in OpenAlex.
- A bacterial NO-binding sensor domain evolved through acquisition of a cytochrome-derived c-type heme-binding motif.bioRxiv : the preprint server for biology · 2026Article
- Genome Analysis Reveals Diversity and Functional Potential of Novel Janthinobacterium Species From Subarctic Soils.MicrobiologyOpen · 2026Article
- Orthogonal chemical genomics approaches reveal genomic targets for increasing anaerobic chemical tolerance inmSystems · 2026Article
- From genes to function: regulation, maturation, and evolution of cytochromeApplied and environmental microbiology · 2025Review
- Unveiling the complete organelle genomes ofFrontiers in plant science · 2025Article
- Structural Insights into Mechanisms Underlying Mitochondrial and Bacterial Cytochrome c Synthases.Biomolecules · 2024Article
- Recurrent evolutionary switches of mitochondrial cytochrome c maturation systems in Archaeplastida.Nature communications · 2024Article
- Structural basis of membrane machines that traffick and attach heme to cytochromes.The Journal of biological chemistry · 2023Article
- A Common Target of Nitrite and Nitric Oxide for Respiration Inhibition in Bacteria.International journal of molecular sciences · 2022Article
- Structures of the CcmABCD heme release complex at multiple states.Nature communications · 2022Article
- Catalysis and Electron Transfer inChemical reviews · 2022Review
- Diversity of CytochromeMicroorganisms · 2022Review
- NapB Restores cytochrome c biosynthesis in bacterial dsbD-deficient mutants.Communications biology · 2022Article
- Long-term enriched methanogenic communities from thermokarst lake sediments show species-specific responses to warming.FEMS microbes · 2020Article
- Complex Oxidation of ApocytochromesApplied and environmental microbiology · 2019Article
- Article
- The CcmC-CcmE interaction during cytochromeThe Journal of biological chemistry · 2018Article
- 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
- Transcriptomic Profiling Suggests That Promysalin Alters the Metabolic Flux, Motility, and Iron Regulation in Pseudomonas putida KT2440.ACS infectious diseases · 2018Article
- Structurally Mapping Endogenous Heme in the CcmCDE Membrane Complex for Cytochrome c Biogenesis.Journal of molecular biology · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Cytochromes c are widespread respiratory proteins characterized by the covalent attachment of heme. The formation of c-type cytochromes requires, in all but a few exceptional cases, the formation of two thioether bonds between the two cysteine sulfurs in a -CXXCH- motif in the protein and the vinyl groups of heme. The vinyl groups of the heme are not particularly activated and therefore the addition reaction does not physiologically occur spontaneously in cells. There are several diverse post-translational modification systems for forming these bonds. Here, we describe the complex multiprotein cytochrome c maturation (Ccm) system (in Escherichia coli comprising the proteins CcmABCDEFGH), also called System I, that performs the heme attachment. System I is found in plant mitochondria, archaea and many Gram-negative bacteria; the systems found in other organisms and organelles are described elsewhere in this minireview series.
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What OpenQuestion holds
Registered trials
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.