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http://purl.uniprot.org/citations/15122898http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15122898http://www.w3.org/2000/01/rdf-schema#comment"We have used EPR spectroscopy, redox potentiometry, and protein crystallography to characterize the [4Fe-4S] cluster (FS0) of the Escherichia coli nitrate reductase A (NarGHI) catalytic subunit (NarG). FS0 is clearly visible in the crystal structure of NarGHI [Bertero, M. G., et al. (2003) Nat. Struct. Biol. 10, 681-687] but has novel coordination comprising one His residue and three Cys residues. At low temperatures (<15 K), reduced NarGHI exhibits a previously unobserved EPR signal comprising peaks at g = 5.023 and g = 5.556. We have assigned these features to a [4Fe-4S](+) cluster with an S = (3)/(2) ground state, with the g = 5.023 and g = 5.556 peaks corresponding to subpopulations exhibiting DeltaS = (1)/(2) and DeltaS = (3)/(2) transitions, respectively. Both peaks exhibit midpoint potentials of approximately -55 mV at pH 8.0 and are eliminated in the EPR spectrum of apomolybdo-NarGHI. The structure of apomolybdo-NarGHI reveals that FS0 is still present but that there is significant conformational disorder in a segment of residues that includes one of the Cys ligands. On the basis of these observations, we have assigned the high-spin EPR features of reduced NarGHI to FS0."xsd:string
http://purl.uniprot.org/citations/15122898http://purl.org/dc/terms/identifier"doi:10.1021/bi049938l"xsd:string
http://purl.uniprot.org/citations/15122898http://purl.uniprot.org/core/author"Bertero M.G."xsd:string
http://purl.uniprot.org/citations/15122898http://purl.uniprot.org/core/author"Strynadka N.C."xsd:string
http://purl.uniprot.org/citations/15122898http://purl.uniprot.org/core/author"Weiner J.H."xsd:string
http://purl.uniprot.org/citations/15122898http://purl.uniprot.org/core/author"Cammack R."xsd:string
http://purl.uniprot.org/citations/15122898http://purl.uniprot.org/core/author"Rothery R.A."xsd:string
http://purl.uniprot.org/citations/15122898http://purl.uniprot.org/core/author"Blasco F."xsd:string
http://purl.uniprot.org/citations/15122898http://purl.uniprot.org/core/author"Palak M."xsd:string
http://purl.uniprot.org/citations/15122898http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15122898http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/15122898http://purl.uniprot.org/core/pages"5324-5333"xsd:string
http://purl.uniprot.org/citations/15122898http://purl.uniprot.org/core/title"The catalytic subunit of Escherichia coli nitrate reductase A contains a novel [4Fe-4S] cluster with a high-spin ground state."xsd:string
http://purl.uniprot.org/citations/15122898http://purl.uniprot.org/core/volume"43"xsd:string
http://purl.uniprot.org/citations/15122898http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15122898
http://purl.uniprot.org/citations/15122898http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/15122898
http://purl.uniprot.org/uniprot/P09152#attribution-543603F4C847588EDD4901111BCD61BBhttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/15122898
http://purl.uniprot.org/uniprot/#_P09152-mappedCitation-15122898http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/15122898
http://purl.uniprot.org/uniprot/#_P11349-mappedCitation-15122898http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/15122898
http://purl.uniprot.org/uniprot/#_P11350-mappedCitation-15122898http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/15122898
http://purl.uniprot.org/uniprot/P11349http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/15122898
http://purl.uniprot.org/uniprot/P09152http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/15122898
http://purl.uniprot.org/uniprot/P11350http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/15122898