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http://purl.uniprot.org/citations/1310545http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1310545http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1310545http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/1310545http://www.w3.org/2000/01/rdf-schema#comment"Pyruvate formate-lyase (acetyl-CoA:formate C-acetyltransferase, EC 2.3.1.54) from anaerobic Escherichia coli cells converts pyruvate to acetyl-CoA and formate by a unique homolytic mechanism that involves a free radical harbored in the protein structure. By EPR spectroscopy of selectively 13C-labeled enzyme, the radical (g = 2.0037) has been assigned to carbon-2 of a glycine residue. Estimated hyperfine coupling constants to the central 13C nucleus (A parallel = 4.9 mT and A perpendicular = 0.1 mT) and to 13C nuclei in alpha and beta positions agree with literature data for glycine radical models. N-coupling was verified through uniform 15N-labeling. The large 1H hyperfine splitting (1.5 mT) dominating the EPR spectrum was assigned to the alpha proton, which in the enzyme radical is readily solvent-exchangeable. Oxygen destruction of the radical produced two unique fragments (82 and 3 kDa) of the constituent polypeptide chain. The N-terminal block on the small fragment was identified by mass spectrometry as an oxalyl residue that derives from Gly-734, thus assigning the primary structural glycyl radical position. The carbon-centered radical is probably resonance-stabilized through the adjacent carboxamide groups in the polypeptide main chain and could be comparable energetically with other known protein radicals carrying the unpaired electron in tyrosine or tryptophan residues."xsd:string
http://purl.uniprot.org/citations/1310545http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/1310545http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/1310545http://purl.org/dc/terms/identifier"doi:10.1073/pnas.89.3.996"xsd:string
http://purl.uniprot.org/citations/1310545http://purl.org/dc/terms/identifier"doi:10.1073/pnas.89.3.996"xsd:string
http://purl.uniprot.org/citations/1310545http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/1310545
http://purl.uniprot.org/citations/1310545http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/1310545
http://purl.uniprot.org/citations/1310545http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/1310545
http://purl.uniprot.org/citations/1310545http://purl.uniprot.org/core/author"Frey M."xsd:string
http://purl.uniprot.org/citations/1310545http://purl.uniprot.org/core/author"Frey M."xsd:string
http://purl.uniprot.org/citations/1310545http://purl.uniprot.org/core/author"Schaefer W."xsd:string
http://purl.uniprot.org/citations/1310545http://purl.uniprot.org/core/author"Schaefer W."xsd:string
http://purl.uniprot.org/citations/1310545http://purl.uniprot.org/core/author"Knappe J."xsd:string
http://purl.uniprot.org/citations/1310545http://purl.uniprot.org/core/author"Knappe J."xsd:string
http://purl.uniprot.org/citations/1310545http://purl.uniprot.org/core/author"Wagner A.F.V."xsd:string
http://purl.uniprot.org/citations/1310545http://purl.uniprot.org/core/author"Wagner A.F.V."xsd:string
http://purl.uniprot.org/citations/1310545http://purl.uniprot.org/core/author"Neugebauer F.A."xsd:string
http://purl.uniprot.org/citations/1310545http://purl.uniprot.org/core/author"Neugebauer F.A."xsd:string
http://purl.uniprot.org/citations/1310545http://purl.uniprot.org/core/date"1992"xsd:gYear
http://purl.uniprot.org/citations/1310545http://purl.uniprot.org/core/date"1992"xsd:gYear
http://purl.uniprot.org/citations/1310545http://purl.uniprot.org/core/pages"996-1000"xsd:string
http://purl.uniprot.org/citations/1310545http://purl.uniprot.org/core/pages"996-1000"xsd:string