ReviewMetallomics : integrated biometal science2024
Iron-sulfur protein odyssey: exploring their cluster functional versatility and challenging identification.
Review in Metallomics : integrated biometal science, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers, 1 of them a synthesis that pooled it.
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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
35 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Integrative meta-analysis of RNA-Seq data reveals conserved orthologous gene modules and pathways in wheat and rice in response to plant growth-promoting bacteria.Functional & integrative genomics · 2026Pooled it
- An Aerobic in Vitro Cell Lysate-based Method for Fe-S Cluster Reconstitution in Recombinant Rv1460 Protein from Mycobacterium tuberculosis H37Rv.Applied biochemistry and biotechnology · 2026Article
- Beyond Canonical CO Oxidation: Structural and Evolutionary Insights Into a Non-Canonical Carbon Monoxide Dehydrogenase.Angewandte Chemie (International ed. in English) · 2026Article
- Mössbauer spectroscopy in drug discovery: revealing Fe- and Fe-S cluster dependent targets.Expert opinion on drug discovery · 2026Review
- Multi-omic landscape of Mn(Ⅱ) oxidation in Achromobacter pulmonis ss21: from multicopper oxidase to metabolic support electron transfer.World journal of microbiology & biotechnology · 2026Article
- Optimisation of selection for methane mitigation by integrating production traits with ruminal microbiome-driven breeding in beef cattle.Genetics, selection, evolution : GSE · 2026Article
- Copper oxide nanoparticles: from EU-regulatory landscape and mechanistic toxicity towards a cuproptosis-linked adverse outcome pathway.Archives of toxicology · 2026Review
- FeSseqdb: a curated sequence-level database and interpretable machine learning framework for identifying iron-sulfur proteins.BMC bioinformatics · 2026Article
- Discovery of a [4Fe-4S] cluster in the PRRSV Nsp1α leader protease reveals host-virus interplay in its downstream functions.Science advances · 2026Article
- Rational engineering of facultative anaerobiosis enables commensal survival in the oxygenated gut.bioRxiv : the preprint server for biology · 2026Article
- The structure of the SufBCbioRxiv : the preprint server for biology · 2026Article
- Intricacies in iron-sulfur cluster function and biogenesis: functional versatility, sulfur sources, and enzyme specificity.RSC chemical biology · 2026Review
- Structural basis of FatB-mediated iron uptake via tyrosine/histidine direct coordination accompanying long-distance domain reorganization.Nature communications · 2026Article
- Regulatory networks of iron sulfur cluster biology in cancer mechanisms and therapeutic perspectives.iScience · 2026Review
- Bioavailability of Functional Iron in Protein Microparticles.Nutrients · 2026Article
- Enhancing Synthesis Efficiency in Microbial 1,5-Pentanediol Production Through Transcriptomics-Informed Metabolic Engineering ofMicroorganisms · 2026Article
- The critical role ofApplied and environmental microbiology · 2026Article
- Client recruitment mechanism of the cytosolic Fe-S cluster assembly targeting complex.The EMBO journal · 2026Article
- Iron limitation promotes metabolic cross-feeding between cheese ripening bacteria.The ISME journal · 2026Article
- Discovery of a [4Fe-4S] cluster in the PRRSV Nsp1α leader protease reveals host-virus interplay in its downstream functions.bioRxiv : the preprint server for biology · 2026Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
Iron-sulfur (Fe-S) clusters are an essential and ubiquitous class of protein-bound prosthetic centers that are involved in a broad range of biological processes (e.g. respiration, photosynthesis, DNA replication and repair and gene regulation) performing a wide range of functions including electron transfer, enzyme catalysis, and sensing. In a general manner, Fe-S clusters can gain or lose electrons through redox reactions, and are highly sensitive to oxidation, notably by small molecules such as oxygen and nitric oxide. The [2Fe-2S] and [4Fe-4S] clusters, the most common Fe-S cofactors, are typically coordinated by four amino acid side chains from the protein, usually cysteine thiolates, but other residues (e.g. histidine, aspartic acid) can also be found. While diversity in cluster coordination ensures the functional variety of the Fe-S clusters, the lack of conserved motifs makes new Fe-S protein identification challenging especially when the Fe-S cluster is also shared between two proteins as observed in several dimeric transcriptional regulators and in the mitoribosome. Thanks to the recent development of in cellulo, in vitro, and in silico approaches, new Fe-S proteins are still regularly identified, highlighting the functional diversity of this class of proteins. In this review, we will present three main functions of the Fe-S clusters and explain the difficulties encountered to identify Fe-S proteins and methods that have been employed to overcome these issues.
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Registered trials
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