Evidence from Mössbauer spectroscopy for distinct [2Fe-2S](2+) and [4Fe-4S](2+) cluster binding sites in biotin synthase from Escherichia coli

scientific article published on August 2002

Evidence from Mössbauer spectroscopy for distinct [2Fe-2S](2+) and [4Fe-4S](2+) cluster binding sites in biotin synthase from Escherichia coli is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1021/JA027004J
P932PMC publication ID1400546
P698PubMed publication ID12148999
P5875ResearchGate publication ID244440992

P2093author name stringJoseph T Jarrett
Kristene K Surerus
Natalia B Ugulava
P2860cites workRadical SAM, a novel protein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: functional characterization using new analysis and information visualization methodsQ24616026
Biotin synthase contains two distinct iron-sulfur cluster binding sites: chemical and spectroelectrochemical analysis of iron-sulfur cluster interconversionsQ24680072
Spectroscopic changes during a single turnover of biotin synthase: destruction of a [2Fe-2S] cluster accompanies sulfur insertionQ28343711
The enzymology of sulfur activation during thiamin and biotin biosynthesisQ33745004
Adenosylmethionine-dependent iron-sulfur enzymes: versatile clusters in a radical new roleQ34227395
Adenosylmethionine as a source of 5'-deoxyadenosyl radicalsQ34386228
Enzymology of carbon-sulfur bond formationQ34386259
Radical mechanisms of S-adenosylmethionine-dependent enzymesQ34414518
Mutagenesis of the proposed iron-sulfur cluster binding ligands in Escherichia coli biotin synthaseQ38315251
Iron-sulfur cluster interconversions in biotin synthase: dissociation and reassociation of iron during conversion of [2Fe-2S] to [4Fe-4S] clustersQ42229914
Biotin synthase from Escherichia coli: isolation of an enzyme-generated intermediate and stoichiometry of S-adenosylmethionine use.Q42989826
Coordination of adenosylmethionine to a unique iron site of the [4Fe-4S] of pyruvate formate-lyase activating enzyme: a Mössbauer spectroscopic studyQ43877988
The iron-sulfur center of biotin synthase: site-directed mutantsQ43894040
Electron-nuclear double resonance spectroscopic evidence that S-adenosylmethionine binds in contact with the catalytically active [4Fe-4S](+) cluster of pyruvate formate-lyase activating enzymeQ43922832
Biotin Synthase from Escherichiacoli, an Investigation of the Low Molecular Weight and Protein Components Required for Activity inVitroQ47348909
Biotin synthase, a new member of the family of enzymes which uses S-adenosylmethionine as a source of deoxyadenosyl radical.Q54561995
Flavodoxin is required for conversion of dethiobiotin to biotin in Escherichia coli.Q54628754
Biotin synthase: purification, characterization as a [2Fe-2S]cluster protein, and in vitro activity of the Escherichia coli bioB gene product.Q54637383
Escherichia coli biotin synthase: an investigation into the factors required for its activity and its sulfur donorQ70945686
On the mechanism of biotin synthase of Bacillus sphaericusQ72874869
Mössbauer studies of Escherichia coli biotin synthase: evidence for reversible interconversion between [2Fe-2S](2+) and [4Fe-4S](2+) clustersQ73094154
Direct FeS cluster involvement in generation of a radical in lysine 2,3-aminomutaseQ73313370
Iron-sulfur center of biotin synthase and lipoate synthaseQ73626058
[2Fe-2S] to [4Fe-4S] cluster conversion in Escherichia coli biotin synthaseQ73718081
Biotin synthase mechanism: on the origin of sulphurQ77715329
Transfer of sulfur to biotin from biotin synthase (BioB protein)Q77911750
Effect of serinate ligation at each of the iron sites of the [Fe4S4] cluster of Pyrococcus furiosus ferredoxin on the redox, spectroscopic, and biological propertiesQ78108876
P433issue31
P407language of work or nameEnglishQ1860
P921main subjectEscherichia coliQ25419
Mössbauer spectroscopyQ899927
P304page(s)9050-9051
P577publication date2002-08-01
P1433published inJournal of the American Chemical SocietyQ898902
P1476titleEvidence from Mössbauer spectroscopy for distinct [2Fe-2S](2+) and [4Fe-4S](2+) cluster binding sites in biotin synthase from Escherichia coli
P478volume124

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cites work (P2860)
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Q33990654Function, attachment and synthesis of lipoic acid in Escherichia coli
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Q43013624Loss of iron-sulfur clusters from biotin synthase as a result of catalysis promotes unfolding and degradation
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