ArticleMethods in molecular biology (Clifton, N.J.)2021
Methods to Investigate the Kinetic Profile of Cysteine Desulfurases.
Article in Methods in molecular biology (Clifton, N.J.), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 11 citations in OpenAlex.
- 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 and mechanistic insights into the sulfur transfer protein SufU from Staphylococcus aureus.Journal of inorganic biochemistry · 2026Article
- Adaptation of Fe-S Cluster Assembly to Rising OResearch square · 2026Article
- 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
- A Role for Two Conserved Arginine Residues in Protected Persulfide Transfer by SufE-Dependent SufS Cysteine Desulfurases.Biochemistry · 2025Article
- The structural and functional analysis of mycobacteria cysteine desulfurase-loaded encapsulin.Communications biology · 2024Article
- Persulfide Transfer to SufE Activates the Half-Sites Reactivity of theBiochemistry · 2024Article
- The structure of the SufS-SufE complex reveals interactions driving protected persulfide transfer in iron-sulfur cluster biogenesis.bioRxiv : the preprint server for biology · 2024Article
- Structural and Biochemical Characterization ofACS omega · 2022Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Biological iron-sulfur (Fe-S) clusters are essential protein prosthetic groups that promote a range of biochemical reactions. In vivo, these clusters are synthesized by specialized protein machineries involved in sulfur mobilization, cluster assembly, and cluster transfer to their target proteins. Cysteine desulfurases initiate the first step of sulfur activation and mobilization in cluster biosynthetic pathways. The reaction catalyzed by these enzymes involves the abstraction of sulfur from the amino acid L-cysteine, with concomitant formation of alanine. The presence and availability of a sulfur acceptor modulate the sulfurtransferase activity of this class of enzymes by altering their reaction profile and catalytic turnover rate. Herein, we describe two methods used to probe the reaction profile of cysteine desulfurases through quantification of alanine and sulfide production in these reactions.
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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.