| http://purl.uniprot.org/citations/2174874 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/2174874 | http://www.w3.org/2000/01/rdf-schema#comment | "The properties of the ubiquinol-cytochrome c reductase complex (bc1 complex) have been studied in respiratory defective mutants of Saccharomyces cerevisiae bearing lesions in the core 1 subunit. All the cor1 mutants examined have greatly reduced concentrations of mitochondrial cytochrome b and display succinate-cytochrome c reductase activities near the limits of detection. Two mutants (E576 and C7), however, had 5% of wild type activity when the cells were grown at 23 degrees C, but not at 37 degrees C. The temperature-sensitive phenotype was determined to result from substitution of either Arg or Glu for Gly68 of the core 1 subunit. The respiratory competent revertants E576/R8 and C7/R4 derived from E576 and C7 retain the temperature sensitivity of the original mutants. Both revertants are temperature sensitive in vivo, but only mitochondria isolated from E576/R8 are temperature sensitive in vitro. The bc1 complex of mitochondria isolated from this revertant displays a normal value of the ratio Kcat/Km for cytochrome c and four times higher than the wild type for duroquinol. The succinate-cytochrome c reductase activity of E576/R8 is almost completely abolished after incubation at 37 degrees C for 90 min. It is inferred that the quaternary structure of ubiquinol-cytochrome c reductase complex is more labile at the nonpermissive temperature in the mutant and undergoes an alteration such that cytochrome b is no longer able to receive electrons through either the "o" or the "i" site pathway. The temperature lability and kinetic properties of the mutant enzyme point to a requirement of the core 1 not only for assembly but also for the catalytic activity of the complex."xsd:string |
| http://purl.uniprot.org/citations/2174874 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0021-9258(18)45761-4"xsd:string |
| http://purl.uniprot.org/citations/2174874 | http://purl.uniprot.org/core/author | "Gatti D.L."xsd:string |
| http://purl.uniprot.org/citations/2174874 | http://purl.uniprot.org/core/author | "Tzagoloff A."xsd:string |
| http://purl.uniprot.org/citations/2174874 | http://purl.uniprot.org/core/date | "1990"xsd:gYear |
| http://purl.uniprot.org/citations/2174874 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/2174874 | http://purl.uniprot.org/core/pages | "21468-21475"xsd:string |
| http://purl.uniprot.org/citations/2174874 | http://purl.uniprot.org/core/title | "Structure and function of the mitochondrial bc1 complex. Properties of the complex in temperature-sensitive cor1 mutants."xsd:string |
| http://purl.uniprot.org/citations/2174874 | http://purl.uniprot.org/core/volume | "265"xsd:string |
| http://purl.uniprot.org/citations/2174874 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/2174874 |
| http://purl.uniprot.org/citations/2174874 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/2174874 |
| http://purl.uniprot.org/uniprot/P07256#attribution-858BEE5E1DE4C859B3FB80CAA447F814 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/2174874 |
| http://purl.uniprot.org/uniprot/#_P07256-mappedCitation-2174874 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/2174874 |
| http://purl.uniprot.org/uniprot/P07256 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/2174874 |