ArticleJournal of the American Chemical Society2012
9-Mercaptodethiobiotin is generated as a ligand to the [2Fe-2S]+ cluster during the reaction catalyzed by biotin synthase from Escherichia coli.
Article in Journal of the American Chemical Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 34 citations in OpenAlex.
- Iron-sulfur protein odyssey: exploring their cluster functional versatility and challenging identification.Metallomics : integrated biometal science · 2024Review
- Radical SAM Enzymes and Metallocofactor Assembly: A Structural Point of View.ACS bio & med chem Au · 2022Review
- 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
- The Biotin Biosynthetic Pathway in Mycobacterium tuberculosis is a Validated Target for the Development of Antibacterial Agents.Current medicinal chemistry · 2020Review
- Metabolic functions of the human gut microbiota: the role of metalloenzymes.Natural product reports · 2019Review
- Investigation of ( S)-(-)-Acidomycin: A Selective Antimycobacterial Natural Product That Inhibits Biotin Synthase.ACS infectious diseases · 2019Article
- EPR-Derived Structure of a Paramagnetic Intermediate Generated by Biotin Synthase BioB.Journal of the American Chemical Society · 2018Article
- Carbon-sulfur bond-forming reaction catalysed by the radical SAM enzyme HydE.Nature chemistry · 2016Article
- Density functional theory calculations on the active site of biotin synthase: mechanism of S transfer from the Fe(2)S(2) cluster and the role of 1st and 2nd sphere residues.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2015Article
- N-Substituted Derivatives of the Azadithiolate Cofactor from the [FeFe] Hydrogenases: Stability and Complexation.Inorganic chemistry · 2015Article
- Advanced paramagnetic resonance spectroscopies of iron-sulfur proteins: Electron nuclear double resonance (ENDOR) and electron spin echo envelope modulation (ESEEM).Biochimica et biophysica acta · 2015Review
- [FeFe]-hydrogenase maturation: insights into the role HydE plays in dithiomethylamine biosynthesis.Biochemistry · 2015Article
- Spore photoproduct lyase: the known, the controversial, and the unknown.The Journal of biological chemistry · 2015Review
- The biosynthesis of thiol- and thioether-containing cofactors and secondary metabolites catalyzed by radical S-adenosylmethionine enzymes.The Journal of biological chemistry · 2015Review
- SPASM and twitch domains in S-adenosylmethionine (SAM) radical enzymes.The Journal of biological chemistry · 2015Review
- Choosing the right metal: case studies of class I ribonucleotide reductases.The Journal of biological chemistry · 2014Review
- Paramagnetic intermediates generated by radical S-adenosylmethionine (SAM) enzymes.Accounts of chemical research · 2014Article
- Radical S-adenosylmethionine enzymes.Chemical reviews · 2014Review
- Identification of an intermediate methyl carrier in the radical S-adenosylmethionine methylthiotransferases RimO and MiaB.Journal of the American Chemical Society · 2013Article
- Emerging themes in radical SAM chemistry.Current opinion in structural biology · 2012Review
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6 authors at 2 institutions in 1 country.
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Abstract
Biotin synthase catalyzes formation of the thiophane ring through stepwise substitution of a sulfur atom for hydrogen atoms at the C9 and C6 positions of dethiobiotin. Biotin synthase is a radical S-adenosylmethionine (SAM) enzyme that reductively cleaves S-adenosylmethionine, generating 5'-deoxyadenosyl radicals that initially abstract a hydrogen atom from the C9 position of dethiobiotin. We have proposed that the resulting dethiobiotinyl radical is quenched by the μ-sulfide of the nearby [2Fe-2S](2+) cluster, resulting in coupled formation of 9-mercaptodethiobiotin and a reduced [2Fe-2S](+) cluster. This reduced FeS cluster is observed by electron paramagnetic resonance spectroscopy as a mixture of two orthorhombic spin systems. In the present work, we use isotopically labeled 9-mercaptodethiobiotin and enzyme to probe the ligand environment of the [2Fe-2S](+) cluster in this reaction intermediate. Hyperfine sublevel correlation spectroscopy (HYSCORE) spectra exhibit strong cross-peaks demonstrating strong isotropic coupling of the nuclear spin with the paramagnetic center. The hyperfine coupling constants are consistent with a structural model for the reaction intermediate in which 9-mercaptodethiobiotin is covalently coordinated to the remnant [2Fe-2S](+) cluster.
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