FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W1563472611> ?p ?o ?g. }

• W1563472611 endingPage "8429" @default.
• W1563472611 startingPage "8420" @default.
• W1563472611 abstract "The resolution of new features in the 1H electron nuclear double resonance (ENDOR) spectrum of the oxidized CuA site in beef heart cytochrome c oxidase is presented. In a previous study, we assigned resonances in the CuA ENDOR spectrum to hyperfine interactions of methylene protons on one or two cysteine ligands to CuA (Stevens, T.H., Martin, C.T., Wang, H., Brudvig, G.W., Scholes, C.P., and Chan, S.I. (1982) J. Biol. Chem. 257, 12106-12113). In this work, a new 1H ENDOR resonance in the beef heart CuA ENDOR spectrum is reported and can be assigned to either anisotropy in a previously resolved cysteine methylene proton hyperfine interaction (Aiso = 12 MHz, Aaniso = 2.5 MHz) or to a third isotropic hyperfine coupling (A = 13.6 MHz) to a cysteine methylene proton of a second cysteine ligand to copper. In either case, the 1H ENDOR results require the delocalization of approximately 50% of the unpaired spin from copper onto either one or two cysteine ligands to CuA. To characterize further the CuA site, we have prepared yeast cytochrome c oxidase incorporating isotopically substituted [beta-13C]cysteine. The CuA ENDOR spectrum of this species shows only one clearly resolved 13C hyperfine interaction (A = 3.6 MHz). This result confirms the assignment of at least one strongly interacting cysteine ligand to CuA and suggests that if the assignment of two cysteine ligands to CuA is correct, the two cysteines interact with copper in a highly symmetric manner. A recent extended x-ray absorption fine structure study of native and modified forms of cytochrome c oxidase indicates the coordination of two sulfur ligands to CuA (Li, P.M., Gelles, J., Chan, S.I., Sullivan R.J., and Scott, R.A. (1987) Biochemistry 26, 2091-2095). In light of the new possibility of two symmetrically coordinated cysteine ligands to CuA, we propose a molecular orbital description of the oxidized CuA site which is characterized by a high degree of delocalization of unpaired spin away from copper and onto a pair of symmetrically coordinated cysteine sulfur ligands. We also present a protein model for the CuA site in which two cysteine ligands derived from subunit II lie on the face of an alpha-helix. This structure would allow the unprecedented stable coordination of two cysteine thiolate sulfurs to copper and may provide a mechanism for the redox-linked proton pumping by cytochrome c oxidase." @default.
• W1563472611 created "2016-06-24" @default.
• W1563472611 creator A5012942751 @default.
• W1563472611 creator A5017230178 @default.
• W1563472611 creator A5085256219 @default.
• W1563472611 date "1988-06-01" @default.
• W1563472611 modified "2023-09-28" @default.
• W1563472611 title "On the nature of cysteine coordination to CuA in cytochrome c oxidase." @default.
• W1563472611 cites W1550650979 @default.
• W1563472611 cites W1558725106 @default.
• W1563472611 cites W1975098194 @default.
• W1563472611 cites W1980233437 @default.
• W1563472611 cites W2006751673 @default.
• W1563472611 cites W2015643247 @default.
• W1563472611 cites W2015730581 @default.
• W1563472611 cites W2019789717 @default.
• W1563472611 cites W2027460541 @default.
• W1563472611 cites W2033486561 @default.
• W1563472611 cites W2044573513 @default.
• W1563472611 cites W2046242531 @default.
• W1563472611 cites W2054167141 @default.
• W1563472611 cites W2063289130 @default.
• W1563472611 cites W2080048275 @default.
• W1563472611 cites W2084360842 @default.
• W1563472611 cites W2087589818 @default.
• W1563472611 cites W2091802531 @default.
• W1563472611 cites W2093887563 @default.
• W1563472611 cites W2108586287 @default.
• W1563472611 cites W2119121006 @default.
• W1563472611 cites W2324505685 @default.
• W1563472611 cites W268331719 @default.
• W1563472611 cites W2949146084 @default.
• W1563472611 cites W4319308131 @default.
• W1563472611 cites W53396245 @default.
• W1563472611 doi "https://doi.org/10.1016/s0021-9258(18)68494-7" @default.
• W1563472611 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/2836423" @default.
• W1563472611 hasPublicationYear "1988" @default.
• W1563472611 type Work @default.
• W1563472611 sameAs 1563472611 @default.
• W1563472611 citedByCount "48" @default.
• W1563472611 countsByYear W15634726112016 @default.
• W1563472611 crossrefType "journal-article" @default.
• W1563472611 hasAuthorship W1563472611A5012942751 @default.
• W1563472611 hasAuthorship W1563472611A5017230178 @default.
• W1563472611 hasAuthorship W1563472611A5085256219 @default.
• W1563472611 hasBestOaLocation W15634726111 @default.
• W1563472611 hasConcept C123249941 @default.
• W1563472611 hasConcept C181199279 @default.
• W1563472611 hasConcept C185592680 @default.
• W1563472611 hasConcept C2779201268 @default.
• W1563472611 hasConcept C28859421 @default.
• W1563472611 hasConcept C2909484822 @default.
• W1563472611 hasConcept C38485361 @default.
• W1563472611 hasConcept C55493867 @default.
• W1563472611 hasConceptScore W1563472611C123249941 @default.
• W1563472611 hasConceptScore W1563472611C181199279 @default.
• W1563472611 hasConceptScore W1563472611C185592680 @default.
• W1563472611 hasConceptScore W1563472611C2779201268 @default.
• W1563472611 hasConceptScore W1563472611C28859421 @default.
• W1563472611 hasConceptScore W1563472611C2909484822 @default.
• W1563472611 hasConceptScore W1563472611C38485361 @default.
• W1563472611 hasConceptScore W1563472611C55493867 @default.
• W1563472611 hasIssue "17" @default.
• W1563472611 hasLocation W15634726111 @default.
• W1563472611 hasOpenAccess W1563472611 @default.
• W1563472611 hasPrimaryLocation W15634726111 @default.
• W1563472611 hasRelatedWork W1969682508 @default.
• W1563472611 hasRelatedWork W1994078300 @default.
• W1563472611 hasRelatedWork W2029130887 @default.
• W1563472611 hasRelatedWork W2037546361 @default.
• W1563472611 hasRelatedWork W2058962213 @default.
• W1563472611 hasRelatedWork W2105992474 @default.
• W1563472611 hasRelatedWork W2109512882 @default.
• W1563472611 hasRelatedWork W2167245403 @default.
• W1563472611 hasRelatedWork W2204518340 @default.
• W1563472611 hasRelatedWork W263815323 @default.
• W1563472611 hasVolume "263" @default.
• W1563472611 isParatext "false" @default.
• W1563472611 isRetracted "false" @default.
• W1563472611 magId "1563472611" @default.
• W1563472611 workType "article" @default.