http://purl.uniprot.org/citations/10586875 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/10586875 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/10586875 | http://www.w3.org/2000/01/rdf-schema#comment | "Fumarate reductase couples the reduction of fumarate to succinate to the oxidation of quinol to quinone, in a reaction opposite to that catalysed by the related complex II of the respiratory chain (succinate dehydrogenase). Here we describe the crystal structure at 2.2 A resolution of the three protein subunits containing fumarate reductase from the anaerobic bacterium Wolinella succinogenes. Subunit A contains the site of fumarate reduction and a covalently bound flavin adenine dinucleotide prosthetic group. Subunit B contains three iron-sulphur centres. The menaquinol-oxidizing subunit C consists of five membrane-spanning, primarily helical segments and binds two haem b molecules. On the basis of the structure, we propose a pathway of electron transfer from the dihaem cytochrome b to the site of fumarate reduction and a mechanism of fumarate reduction. The relative orientations of the soluble and membrane-embedded subunits of succinate:quinone oxidoreductases appear to be unique."xsd:string |
http://purl.uniprot.org/citations/10586875 | http://purl.org/dc/terms/identifier | "doi:10.1038/46483"xsd:string |
http://purl.uniprot.org/citations/10586875 | http://purl.org/dc/terms/identifier | "doi:10.1038/46483"xsd:string |
http://purl.uniprot.org/citations/10586875 | http://purl.uniprot.org/core/author | "Michel H."xsd:string |
http://purl.uniprot.org/citations/10586875 | http://purl.uniprot.org/core/author | "Michel H."xsd:string |
http://purl.uniprot.org/citations/10586875 | http://purl.uniprot.org/core/author | "Kroeger A."xsd:string |
http://purl.uniprot.org/citations/10586875 | http://purl.uniprot.org/core/author | "Kroeger A."xsd:string |
http://purl.uniprot.org/citations/10586875 | http://purl.uniprot.org/core/author | "Auer M."xsd:string |
http://purl.uniprot.org/citations/10586875 | http://purl.uniprot.org/core/author | "Auer M."xsd:string |
http://purl.uniprot.org/citations/10586875 | http://purl.uniprot.org/core/author | "Lancaster C.R.D."xsd:string |
http://purl.uniprot.org/citations/10586875 | http://purl.uniprot.org/core/author | "Lancaster C.R.D."xsd:string |
http://purl.uniprot.org/citations/10586875 | http://purl.uniprot.org/core/date | "1999"xsd:gYear |
http://purl.uniprot.org/citations/10586875 | http://purl.uniprot.org/core/date | "1999"xsd:gYear |
http://purl.uniprot.org/citations/10586875 | http://purl.uniprot.org/core/name | "Nature"xsd:string |
http://purl.uniprot.org/citations/10586875 | http://purl.uniprot.org/core/name | "Nature"xsd:string |
http://purl.uniprot.org/citations/10586875 | http://purl.uniprot.org/core/pages | "377-385"xsd:string |
http://purl.uniprot.org/citations/10586875 | http://purl.uniprot.org/core/pages | "377-385"xsd:string |
http://purl.uniprot.org/citations/10586875 | http://purl.uniprot.org/core/title | "Structure of fumarate reductase from Wolinella succinogenes at 2.2 A resolution."xsd:string |
http://purl.uniprot.org/citations/10586875 | http://purl.uniprot.org/core/title | "Structure of fumarate reductase from Wolinella succinogenes at 2.2 A resolution."xsd:string |
http://purl.uniprot.org/citations/10586875 | http://purl.uniprot.org/core/volume | "402"xsd:string |
http://purl.uniprot.org/citations/10586875 | http://purl.uniprot.org/core/volume | "402"xsd:string |
http://purl.uniprot.org/citations/10586875 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/10586875 |
http://purl.uniprot.org/citations/10586875 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/10586875 |