ReviewPhilosophical transactions of the Royal Society of London. Series B, Biological sciences2003
C-type cytochromes: diverse structures and biogenesis systems pose evolutionary problems.
Review in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 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.
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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.
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Who cites it
38 citing papers in PubMed, 118 citations in OpenAlex.
- Simulation-guided design of peptide-metal coordination interfaces for next-generation metallo-immunotherapy.Nano convergence · 2026Review
- The Impact of Forever Chemicals on Protein Structure and Function.International journal of molecular sciences · 2026Review
- From genes to function: regulation, maturation, and evolution of cytochromeApplied and environmental microbiology · 2025Review
- Cytochrome "nanowires" are physically limited to sub-picoamp currents that suffice for cellular respiration.Frontiers in chemistry · 2025Article
- Electron transfer in biological systems.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2024Review
- Radical Mediated RapidBiomolecules · 2022Article
- Taxonomic Re-Evaluation and Genomic Comparison of Novel Extracellular Electron Uptake-Capable Rhodovulum visakhapatnamense and Rhodovulum sulfidophilum IsolatesMicroorganisms · 2022Article
- Nature's nitrite-to-ammonia expressway, with no stop at dinitrogen.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2022Review
- Adaptation to Varying Salinity inFrontiers in microbiology · 2022Article
- Role of multiheme cytochromes involved in extracellular anaerobic respiration in bacteria.Protein science : a publication of the Protein Society · 2020Review
- Properties and structure of a low-potential, penta-heme cytochrome cPhotosynthesis research · 2019Article
- Comparison of the backbone dynamics of wild-type Hydrogenobacter thermophilus cytochrome c(552) and its b-type variant.Journal of biomolecular NMR · 2015Article
- Genome sequence of a dissimilatory Fe(III)-reducing bacterium Geobacter soli type strain GSS01(T).Standards in genomic sciences · 2015Article
- Substrate recognition of holocytochrome c synthase: N-terminal region and CXXCH motif of mitochondrial cytochrome c.FEBS letters · 2014Article
- Structural transformations of cytochrome c upon interaction with cardiolipin.Chemistry and physics of lipids · 2014Review
- A novel metatranscriptomic approach to identify gene expression dynamics during extracellular electron transfer.Nature communications · 2013Article
- Characterization of axial and proximal histidine mutations of the decaheme cytochrome MtrA from Shewanella sp. strain ANA-3 and implications for the electron transport system.Journal of bacteriology · 2012Article
- A pivotal heme-transfer reaction intermediate in cytochrome c biogenesis.The Journal of biological chemistry · 2012Article
- Heme cytotoxicity and the pathogenesis of immune-mediated inflammatory diseases.Frontiers in pharmacology · 2012Article
- A novel component of the disulfide-reducing pathway required for cytochrome c assembly in plastids.Genetics · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
C-type cytochromes are a structurally diverse group of haemoproteins, which are related by the occurrence of haem covalently attached to a polypeptide via two thioether bonds formed by the vinyl groups of haem and cysteine side chains in a CXXCH peptide motif. Remarkably, three different post-translational systems for forming these cytochromes have been identified. The evolution of both the proteins themselves and the biogenesis systems poses many questions to which answers are currently being sought. In this article we review the progress that has been made in understanding the need for covalent attachment of haem to proteins in cytochromes c and the complex systems involved in their formation.
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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.