http://purl.uniprot.org/citations/11148026 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/11148026 | http://www.w3.org/2000/01/rdf-schema#comment | "Mutating three conserved alanine residues in the tether region of the iron-sulfur protein of the yeast cytochrome bc(1) complex resulted in 22-56% decreases in enzymatic activity [Obungu et al. (2000) Biochim. Biophys. Acta 1457, 36-44]. The activity of the cytochrome bc(1) complex isolated from A86L was decreased 60% compared to the wild-type without loss of heme or protein and without changes in the 2Fe2S cluster or proton-pumping ability. The activity of the bc(1) complex from mutant A92R was identical to the wild-type, while loss of both heme and activity was observed in the bc(1) complex isolated from mutant A90I. Computer simulations indicated that neither mutation A86L nor mutation A92R affects the alpha-helical backbone in the tether region; however, the side chain of the leucine substituted for Ala-86 interacts with the side chain of Leu-89. The Arrhenius plot for mutant A86L was apparently biphasic with a transition observed at 17-19 degrees C and an activation energy of 279.9 kJ/mol below 17 degrees C and 125.1 kJ/mol above 17 degrees C. The initial rate of cytochrome c(1) reduction was lowered 33% in mutant A86L; however, the initial rate of cytochrome b reduction was unaffected, suggesting that movement of the tether region of the iron-sulfur protein is necessary for maximum rates of enzymatic activity. Substituting a leucine for Ala-86 impedes the unwinding of the alpha-helix and hence movement of the tether."xsd:string |
http://purl.uniprot.org/citations/11148026 | http://purl.org/dc/terms/identifier | "doi:10.1021/bi001708t"xsd:string |
http://purl.uniprot.org/citations/11148026 | http://purl.uniprot.org/core/author | "Wang Y."xsd:string |
http://purl.uniprot.org/citations/11148026 | http://purl.uniprot.org/core/author | "Ghosh M."xsd:string |
http://purl.uniprot.org/citations/11148026 | http://purl.uniprot.org/core/author | "Beattie D.S."xsd:string |
http://purl.uniprot.org/citations/11148026 | http://purl.uniprot.org/core/author | "Ebert C.E."xsd:string |
http://purl.uniprot.org/citations/11148026 | http://purl.uniprot.org/core/author | "Vadlamuri S."xsd:string |
http://purl.uniprot.org/citations/11148026 | http://purl.uniprot.org/core/date | "2001"xsd:gYear |
http://purl.uniprot.org/citations/11148026 | http://purl.uniprot.org/core/name | "Biochemistry"xsd:string |
http://purl.uniprot.org/citations/11148026 | http://purl.uniprot.org/core/pages | "327-335"xsd:string |
http://purl.uniprot.org/citations/11148026 | http://purl.uniprot.org/core/title | "Substituting leucine for alanine-86 in the tether region of the iron-sulfur protein of the cytochrome bc1 complex affects the mobility of the [2Fe2S] domain."xsd:string |
http://purl.uniprot.org/citations/11148026 | http://purl.uniprot.org/core/volume | "40"xsd:string |
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