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http://purl.uniprot.org/citations/12824504http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12824504http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12824504http://www.w3.org/2000/01/rdf-schema#comment"The diverse reactions catalyzed by the radical-SAM superfamily of enzymes are thought to proceed via a set of common mechanistic steps, key among which is the reductive cleavage of S-adenosyl-L-methionine (SAM) by a reduced [4Fe-4S] cluster to generate an intermediate deoxyadenosyl radical. A number of spectroscopic studies have provided evidence that SAM interacts directly with the [4Fe-4S] clusters in several of the radical-SAM enzymes; however, the molecular mechanism for the reductive cleavage has yet to be elucidated. Selenium X-ray absorption spectroscopy (Se-XAS) was used previously to provide evidence for a close interaction between the Se atom of selenomethionine (a cleavage product of Se-SAM) and an Fe atom of the [4Fe-4S] cluster of lysine-2,3-aminomutase (KAM). Here, we utilize the same approach to investigate the possibility of a similar interaction in pyruvate formate-lyase activating enzyme (PFL-AE) and biotin synthase (BioB), two additional members of the radical-SAM superfamily. The results show that the latter two enzymes do not exhibit the same Fe-Se interaction as was observed in KAM, indicating that the methionine product of reductive cleavage of SAM does not occupy a well-defined site close to the cluster in PFL-AE and BioB. These results are interpreted in terms of the differences among these enzymes in their use of SAM as either a cofactor or a substrate."xsd:string
http://purl.uniprot.org/citations/12824504http://purl.org/dc/terms/identifier"doi:10.1110/ps.0302203"xsd:string
http://purl.uniprot.org/citations/12824504http://purl.org/dc/terms/identifier"doi:10.1110/ps.0302203"xsd:string
http://purl.uniprot.org/citations/12824504http://purl.uniprot.org/core/author"Broderick J.B."xsd:string
http://purl.uniprot.org/citations/12824504http://purl.uniprot.org/core/author"Broderick J.B."xsd:string
http://purl.uniprot.org/citations/12824504http://purl.uniprot.org/core/author"Cosper N.J."xsd:string
http://purl.uniprot.org/citations/12824504http://purl.uniprot.org/core/author"Cosper N.J."xsd:string
http://purl.uniprot.org/citations/12824504http://purl.uniprot.org/core/author"Johnson M.K."xsd:string
http://purl.uniprot.org/citations/12824504http://purl.uniprot.org/core/author"Johnson M.K."xsd:string
http://purl.uniprot.org/citations/12824504http://purl.uniprot.org/core/author"Scott R.A."xsd:string
http://purl.uniprot.org/citations/12824504http://purl.uniprot.org/core/author"Scott R.A."xsd:string
http://purl.uniprot.org/citations/12824504http://purl.uniprot.org/core/author"Hong W."xsd:string
http://purl.uniprot.org/citations/12824504http://purl.uniprot.org/core/author"Hong W."xsd:string
http://purl.uniprot.org/citations/12824504http://purl.uniprot.org/core/author"Broderick W.E."xsd:string
http://purl.uniprot.org/citations/12824504http://purl.uniprot.org/core/author"Broderick W.E."xsd:string
http://purl.uniprot.org/citations/12824504http://purl.uniprot.org/core/author"Cosper M.M."xsd:string
http://purl.uniprot.org/citations/12824504http://purl.uniprot.org/core/author"Cosper M.M."xsd:string
http://purl.uniprot.org/citations/12824504http://purl.uniprot.org/core/author"Shokes J.E."xsd:string
http://purl.uniprot.org/citations/12824504http://purl.uniprot.org/core/author"Shokes J.E."xsd:string
http://purl.uniprot.org/citations/12824504http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12824504http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12824504http://purl.uniprot.org/core/name"Protein Sci."xsd:string
http://purl.uniprot.org/citations/12824504http://purl.uniprot.org/core/name"Protein Sci."xsd:string