RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/30628436http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/30628436http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/30628436http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/30628436http://www.w3.org/2000/01/rdf-schema#comment"Mycofactocin is a putative redox cofactor and is classified as a ribosomally synthesized and post-translationally modified peptide (RiPP). Some RiPP natural products, including mycofactocin, rely on a radical S-adenosylmethionine (RS, SAM) protein to modify the precursor peptide. Mycofactocin maturase, MftC, is a unique RS protein that catalyzes the oxidative decarboxylation and C-C bond formation on the precursor peptide MftA. However, the number, chemical nature, and catalytic roles for the MftC [Fe-S] clusters remain unknown. Here, we report that MftC binds a RS [4Fe-4S] cluster and two auxiliary [4Fe-4S] clusters that are required for MftA modification. Furthermore, electron paramagnetic resonance spectra of MftC suggest that SAM and MftA affect the environments of the RS and Aux I cluster, whereas the Aux II cluster is unaffected by the substrates. Lastly, reduction potential assignments of individual [4Fe-4S] clusters by protein film voltammetry show that their potentials are within 100 mV of each other."xsd:string
http://purl.uniprot.org/citations/30628436http://purl.org/dc/terms/identifier"doi:10.1021/acs.biochem.8b01082"xsd:string
http://purl.uniprot.org/citations/30628436http://purl.org/dc/terms/identifier"doi:10.1021/acs.biochem.8b01082"xsd:string
http://purl.uniprot.org/citations/30628436http://purl.uniprot.org/core/author"Pandelia M.E."xsd:string
http://purl.uniprot.org/citations/30628436http://purl.uniprot.org/core/author"Pandelia M.E."xsd:string
http://purl.uniprot.org/citations/30628436http://purl.uniprot.org/core/author"Elliott S.J."xsd:string
http://purl.uniprot.org/citations/30628436http://purl.uniprot.org/core/author"Elliott S.J."xsd:string
http://purl.uniprot.org/citations/30628436http://purl.uniprot.org/core/author"Walker L.M."xsd:string
http://purl.uniprot.org/citations/30628436http://purl.uniprot.org/core/author"Walker L.M."xsd:string
http://purl.uniprot.org/citations/30628436http://purl.uniprot.org/core/author"Latham J.A."xsd:string
http://purl.uniprot.org/citations/30628436http://purl.uniprot.org/core/author"Latham J.A."xsd:string
http://purl.uniprot.org/citations/30628436http://purl.uniprot.org/core/author"Ayikpoe R."xsd:string
http://purl.uniprot.org/citations/30628436http://purl.uniprot.org/core/author"Ayikpoe R."xsd:string
http://purl.uniprot.org/citations/30628436http://purl.uniprot.org/core/author"Bonitatibus S."xsd:string
http://purl.uniprot.org/citations/30628436http://purl.uniprot.org/core/author"Bonitatibus S."xsd:string
http://purl.uniprot.org/citations/30628436http://purl.uniprot.org/core/author"Eaton G.R."xsd:string
http://purl.uniprot.org/citations/30628436http://purl.uniprot.org/core/author"Eaton G.R."xsd:string
http://purl.uniprot.org/citations/30628436http://purl.uniprot.org/core/author"Eaton S.S."xsd:string
http://purl.uniprot.org/citations/30628436http://purl.uniprot.org/core/author"Eaton S.S."xsd:string
http://purl.uniprot.org/citations/30628436http://purl.uniprot.org/core/author"Langton M."xsd:string
http://purl.uniprot.org/citations/30628436http://purl.uniprot.org/core/author"Langton M."xsd:string
http://purl.uniprot.org/citations/30628436http://purl.uniprot.org/core/author"Ngendahimana T."xsd:string