ReviewJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2008
Iron-sulfur protein folds, iron-sulfur chemistry, and evolution.
Review in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 101 papers.
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Who cites it
101 citing papers in PubMed.
- FeSseqdb: a curated sequence-level database and interpretable machine learning framework for identifying iron-sulfur proteins.BMC bioinformatics · 2026Article
- Supporting activities of cognate redox partners for sterol-metabolizing P450 enzymes in Mycobacterium neoaurum.The Journal of biological chemistry · 2026Article
- Crystallise, poise, capture: a multimodal platform for correlated structural and spectroscopic characterisation of redox enzymes.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2026Article
- Redox cycling nitroxide limits cellular iron availability and selectively inhibits iron-sulfur cluster metabolism.Cell death discovery · 2026Article
- Revisiting Eck and Dayhoff's Building Block Model of Ferredoxin Evolution on Dayhoff's 100th Birthday.Journal of molecular evolution · 2026Article
- Iron-sulfur cluster biogenesis and regulation of intracellular iron homeostasis in Escherichia coli.Metallomics : integrated biometal science · 2025Review
- An iron-sulfur cluster as a new metal center in a flavodiiron protein.Protein science : a publication of the Protein Society · 2025Article
- Crystal Structure of a Thioredoxin-like Ferredoxin Encoded Within a Cobalamin Biosynthetic Operon of Rhodobacter capsulatus.The protein journal · 2025Article
- Electron transfer in biological systems.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2024Review
- Proteomic strategies to interrogate the Fe-S proteome.Biochimica et biophysica acta. Molecular cell research · 2024Review
- Ferredoxins: Functions, Evolution, Potential Applications, and Challenges of Subtype Classification.Current issues in molecular biology · 2024Review
- Advanced Electroanalysis for Electrosynthesis.ACS organic & inorganic Au · 2024Review
- Theoretical hypothesis in a direct electron transfer between non-interacting Fe-S proteins within an artificial fusion.FEMS microbiology letters · 2024Article
- Application of a Synthetic Ferredoxin-Inspired [4Fe4S]-Peptide Maquette as the Redox Partner for an [FeFe]-Hydrogenase.Chembiochem : a European journal of chemical biology · 2023Article
- The Role of Iron in Phytopathogenic Microbe-Plant Interactions: Insights into Virulence and Host Immune Response.Plants (Basel, Switzerland) · 2023Review
- Interactions of reactive sulfur species with metalloproteins.Redox biology · 2023Review
- Article
- Second and Outer Coordination Sphere Effects in Nitrogenase, Hydrogenase, Formate Dehydrogenase, and CO Dehydrogenase.Chemical reviews · 2022Review
- Catalysis and Electron Transfer inChemical reviews · 2022Review
- Mineral Element Insiders and Outliers Play Crucial Roles in Biological Evolution.Life (Basel, Switzerland) · 2022Article
41 more citing papers are in PubMed but not listed here.
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Abstract
An inventory of unique local protein folds around Fe-S clusters has been derived from the analysis of protein structure databases. Nearly 50 such folds have been identified, and over 90% of them harbor low-potential [2Fe-2S](2+,+) or [4Fe-4S](2+,+) clusters. In contrast, high-potential Fe-S clusters, notwithstanding their structural diversity, occur in only three different protein folds. These observations suggest that the extant population of Fe-S protein folds has to a large extent been shaped in the reducing iron- and sulfur-rich environment that is believed to have predominated on this planet until approximately two billion years ago. High-potential active sites are then surmised to be rarer because they emerged later, in a more oxidizing biosphere, in conditions where iron and sulfide had become poorly available, Fe-S clusters were less stable, and in addition faced competition from heme iron and copper active sites. Among the low-potential Fe-S active sites, protein folds hosting [4Fe-4S](2+,+) clusters outnumber those with [2Fe-2S](2+,+) ones by a factor of 3 at least. This is in keeping with the higher chemical stability and versatility of the tetranuclear clusters, compared with the binuclear ones. It is therefore suggested that, at least while novel Fe-S sites are evolving within proteins, the intrinsic chemical stability of the inorganic moiety may be more important than the stabilizing effect of the polypeptide chain. The discovery rate of novel Fe-S-containing protein folds underwent a sharp increase around 1995, and has remained stable to this day. The current trend suggests that the mapping of the Fe-S fold space is not near completion, in agreement with predictions made for protein folds in general. Altogether, the data collected and analyzed here suggest that the extant structural landscape of Fe-S proteins has been shaped to a large extent by primeval geochemical conditions on one hand, and iron-sulfur chemistry on the other.
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