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http://purl.uniprot.org/citations/17223530http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17223530http://www.w3.org/2000/01/rdf-schema#comment"The Rieske [2Fe-2S] iron-sulfur protein of cytochrome bc(1) functions as the initial electron acceptor in the rate-limiting step of the catalytic reaction. Prior studies have established roles for a number of conserved residues that hydrogen bond to ligands of the [2Fe-2S] cluster. We have constructed site-specific variants at two of these residues, measured their thermodynamic and functional properties, and determined atomic resolution X-ray crystal structures for the native protein at 1.2 A resolution and for five variants (Ser-154-->Ala, Ser-154-->Thr, Ser-154-->Cys, Tyr-156-->Phe, and Tyr-156-->Trp) to resolutions between 1.5 A and 1.1 A. These structures and complementary biophysical data provide a molecular framework for understanding the role hydrogen bonds to the cluster play in tuning thermodynamic properties, and hence the rate of this bioenergetic reaction. These studies provide a detailed structure-function dissection of the role of hydrogen bonds in tuning the redox potentials of [2Fe-2S] clusters."xsd:string
http://purl.uniprot.org/citations/17223530http://purl.org/dc/terms/identifier"doi:10.1016/j.str.2006.11.012"xsd:string
http://purl.uniprot.org/citations/17223530http://purl.uniprot.org/core/author"Nair S.K."xsd:string
http://purl.uniprot.org/citations/17223530http://purl.uniprot.org/core/author"Brunzelle J.S."xsd:string
http://purl.uniprot.org/citations/17223530http://purl.uniprot.org/core/author"Crofts A.R."xsd:string
http://purl.uniprot.org/citations/17223530http://purl.uniprot.org/core/author"Lhee S."xsd:string
http://purl.uniprot.org/citations/17223530http://purl.uniprot.org/core/author"Kolling D.J."xsd:string
http://purl.uniprot.org/citations/17223530http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17223530http://purl.uniprot.org/core/name"Structure"xsd:string
http://purl.uniprot.org/citations/17223530http://purl.uniprot.org/core/pages"29-38"xsd:string
http://purl.uniprot.org/citations/17223530http://purl.uniprot.org/core/title"Atomic resolution structures of rieske iron-sulfur protein: role of hydrogen bonds in tuning the redox potential of iron-sulfur clusters."xsd:string
http://purl.uniprot.org/citations/17223530http://purl.uniprot.org/core/volume"15"xsd:string
http://purl.uniprot.org/citations/17223530http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17223530
http://purl.uniprot.org/citations/17223530http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/17223530
http://purl.uniprot.org/uniprot/#_Q02762-mappedCitation-17223530http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17223530
http://purl.uniprot.org/uniprot/Q02762http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/17223530