ArticleMethods in enzymology2018
Biochemical Approaches for Understanding Iron-Sulfur Cluster Regeneration in Escherichia coli Lipoyl Synthase During Catalysis.
Article in Methods in enzymology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 22 citations in OpenAlex.
- Mössbauer spectroscopy in drug discovery: revealing Fe- and Fe-S cluster dependent targets.Expert opinion on drug discovery · 2026Review
- Intricacies in iron-sulfur cluster function and biogenesis: functional versatility, sulfur sources, and enzyme specificity.RSC chemical biology · 2026Review
- NCOA4 initiates ferritinophagy by avidly binding GATE16 using two short linear interaction motifs.Life science alliance · 2026Article
- The [4Fe-4S] Cluster of HydF Is Essential for [FeFe]-Hydrogenase Maturation.Journal of the American Chemical Society · 2025Article
- Proteomic strategies to interrogate the Fe-S proteome.Biochimica et biophysica acta. Molecular cell research · 2024Review
- Development of aniScience · 2023Article
- FDX1 regulates cellular protein lipoylation through direct binding to LIAS.bioRxiv : the preprint server for biology · 2023Article
- Functional spectrum and specificity of mitochondrial ferredoxins FDX1 and FDX2.Nature chemical biology · 2023Article
- Journey on the Radical SAM Road as an Accidental Pilgrim.ACS bio & med chem Au · 2022Review
- Eukaryotic TYW1 Is a Radical SAM Flavoenzyme.Biochemistry · 2021Article
- Biochemical Approaches to Probe the Role of the Auxiliary Iron-Sulfur Cluster of Lipoyl Synthase from Mycobacterium Tuberculosis.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Characterization of Fe-S Clusters in Proteins by Mӧssbauer Spectroscopy.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Assembly of the [4Fe-4S] cluster of NFU1 requires the coordinated donation of two [2Fe-2S] clusters from the scaffold proteins, ISCU2 and ISCA1.Human molecular genetics · 2020Article
- The A-type domain inThe Journal of biological chemistry · 2019Article
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2 authors at 1 institution in 1 country.
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Abstract
Lipoyl synthase (LipA in bacteria) is a radical S-adenosylmethionine (SAM) enzyme that catalyzes the second step of the de novo biosynthesis of the lipoyl cofactor: the insertion of sulfur at C6 and C8 of a pendant octanoyl chain. In addition to the [4Fe4S] cluster that is characteristic of the radical SAM (RS) enzymes, LipA contains a second [4Fe4S] cluster that, though controversial, has been proposed to be degraded during turnover to supply the inserted sulfur atoms. A consequence of this proposed role is that the destruction of its iron-sulfur cluster renders the enzyme in an inactive state. Recently, it was shown that Escherichia coli proteins NfuA or IscU can confer catalytic properties to E. coli LipA in vitro. In this chapter, we present methods for characterizing LipA and analyzing its activity in vitro, and provide strategies to monitor the pathway for the regeneration of LipA's auxiliary cluster by E. coli iron-sulfur carrier protein NfuA.
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