ArticleThe Journal of biological chemistry2010
Iron-sulfur (Fe-S) cluster assembly: the SufBCD complex is a new type of Fe-S scaffold with a flavin redox cofactor.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.
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Who cites it
65 citing papers in PubMed.
- 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
- Coordination of the Fe-S cluster biogenesis network by the sRNA RyhB inRNA biology · 2025Article
- A minimal SufBMicrobiology spectrum · 2025Article
- Gut bacterial dysbiosis in pediatric severe malaria associates with post-discharge mortality.Nature communications · 2025Article
- SmsB-SmsC machinery inApplied and environmental microbiology · 2025Article
- Characterization of a mechanistic connection between persulfide transfer and ATP hydrolysis in the SufBC2D scaffold of the Suf Fe-S cluster assembly pathway.Metallomics : integrated biometal science · 2025Article
- High-throughput fitness experiments reveal specific vulnerabilities of human-adapted Salmonella during stress and infection.Nature genetics · 2024Article
- In silico biotechnological potential of Bacillus sp. strain MHSD_37 bacterial endophyte.BMC genomics · 2024Article
- From the outer space to the inner cell: deconvoluting the complexity ofMicrobiology spectrum · 2024Article
- One-PotACS synthetic biology · 2023Article
- Research progress on the biosynthesis and delivery of iron-sulfur clusters in the plastid.Plant cell reports · 2023Review
- TheeLife · 2023Article
- Peptide Selenocysteine Substitutions Reveal Direct Substrate-Enzyme Interactions at Auxiliary Clusters in RadicalJournal of the American Chemical Society · 2023Article
- Structural and Biochemical Characterization ofBiomolecules · 2023Article
- Leveraging Substrate Promiscuity of a RadicalACS central science · 2022Article
- Structural diversity of cysteine desulfurases involved in iron-sulfur cluster biosynthesis.Biophysics and physicobiology · 2022Article
- Review
- Mitochondrial iron-sulfur clusters: Structure, function, and an emerging role in vascular biology.Redox biology · 2021Review
- Identification of a PadR-type regulator essential for intracellular pathogenesis of Burkholderia pseudomallei.Scientific reports · 2021Article
5 more citing papers are in PubMed but not listed here.
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8 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Assembly of iron-sulfur (Fe-S) clusters and maturation of Fe-S proteins in vivo require complex machineries. In Escherichia coli, under adverse stress conditions, this process is achieved by the SUF system that contains six proteins as follows: SufA, SufB, SufC, SufD, SufS, and SufE. Here, we provide a detailed characterization of the SufBCD complex whose function was so far unknown. Using biochemical and spectroscopic analyses, we demonstrate the following: (i) the complex as isolated exists mainly in a 1:2:1 (B:C:D) stoichiometry; (ii) the complex can assemble a [4Fe-4S] cluster in vitro and transfer it to target proteins; and (iii) the complex binds one molecule of flavin adenine nucleotide per SufBC(2)D complex, only in its reduced form (FADH(2)), which has the ability to reduce ferric iron. These results suggest that the SufBC(2)D complex functions as a novel type of scaffold protein that assembles an Fe-S cluster through the mobilization of sulfur from the SufSE cysteine desulfurase and the FADH(2)-dependent reductive mobilization of iron.
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