PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 24811894-5 2014 This may be a feature of a charge relay mechanism involved in some part of the CcO electron transfer system from bound cytochrome c via CuA and heme a to the a3CuB binuclear center. Dinuclear Copper Ion 136-139 cytochrome c, somatic Homo sapiens 119-131 24502917-1 2014 In this overview we present recent combined electrochemical, spectroelectrochemical, spectroscopic and computational studies from our group on the electron transfer reactions of cytochrome c and of the primary electron acceptor of cytochrome c oxidase, the CuA site, in biomimetic complexes. Dinuclear Copper Ion 257-260 cytochrome c, somatic Homo sapiens 178-190 24502917-1 2014 In this overview we present recent combined electrochemical, spectroelectrochemical, spectroscopic and computational studies from our group on the electron transfer reactions of cytochrome c and of the primary electron acceptor of cytochrome c oxidase, the CuA site, in biomimetic complexes. Dinuclear Copper Ion 257-260 cytochrome c, somatic Homo sapiens 231-243 9922138-1 1998 The metals of the cytochrome c oxidase structures of the bovine heart mitochondrion (PDB code 1occ) and of the soil bacterium Paracoccus denitrificans (1arl) include a dicopper center (CuA), magnesium, two proximal hemes, a copper (CuB) atom, and a calcium. Dinuclear Copper Ion 185-188 cytochrome c, somatic Homo sapiens 18-30 15326290-7 2004 The corresponding histidine in cytochrome c oxidases is along a major electron transfer pathway from CuA center to heme a. Dinuclear Copper Ion 101-104 cytochrome c, somatic Homo sapiens 31-43 9922138-6 1998 Our analysis uncovers several statistically significant residue clusters, including a cysteine-histidine-tyrosine cluster overlapping the CuA-Mg complex; a histidine-acidic cluster enveloping the environment of Mg, the two hemes, and CuB; and on the protein surface a mixed charge cluster, which may help stabilize the quaternary structure and/or mediate docking to cytochrome c. Dinuclear Copper Ion 138-141 cytochrome c, somatic Homo sapiens 366-378 8643669-4 1996 The multiphasic kinetics in cytochrome c oxidase can largely be attributed to the presence Of CuA as the donor of a fourth electron, which rereduces the originally oxidized low-spin heme and completes the reduction of O2 to water. Dinuclear Copper Ion 94-97 cytochrome c, somatic Homo sapiens 28-40 8257706-0 1993 ENDOR and ESEEM studies of cytochrome c oxidase: evidence for exchangeable protons at the CuA site. Dinuclear Copper Ion 90-93 cytochrome c, somatic Homo sapiens 27-39 7873550-6 1995 Since the redox potential of the modified cytochrome c is close to the value of its native form, we conclude that there has been a change in the docking of the cytochrome c to CcO and the electronic coupling between heme c and CuA upon 8-azido-ATP modification. Dinuclear Copper Ion 227-230 cytochrome c, somatic Homo sapiens 42-54 7873550-6 1995 Since the redox potential of the modified cytochrome c is close to the value of its native form, we conclude that there has been a change in the docking of the cytochrome c to CcO and the electronic coupling between heme c and CuA upon 8-azido-ATP modification. Dinuclear Copper Ion 227-230 cytochrome c, somatic Homo sapiens 160-172 8257706-8 1993 This relatively short surface separation distance is consistent with the role of CuA as the immediate oxidant of cytochrome c in the cytochrome oxidase (Hill, B. C. (1991) J. Biol. Dinuclear Copper Ion 81-84 cytochrome c, somatic Homo sapiens 113-125 8407882-4 1993 The EPR, optical, and resonance Raman spectra of the oxidized enzyme demonstrated the presence of CuA whose coordination environment bore close resemblance to that of the aa3-type cytochrome c oxidase. Dinuclear Copper Ion 98-101 cytochrome c, somatic Homo sapiens 180-192 30315812-2 2019 Here we extend the model beyond reversible binding of Cytc and its irreversible oxidation to include CuA, heme a and the oxidation cycle of the binuclear center. Dinuclear Copper Ion 101-104 cytochrome c, somatic Homo sapiens 54-58 2543448-6 1989 These results suggest a dual mechanism for respiratory control in cytochrome oxidase vesicles under steady-state conditions, in which the electrical gradient predominantly affects electron transfer from cytochrome c to heme a, possibly by altering the reduction potential of heme a, while the pH gradient affects electron transfer from heme a (CuA) to heme a3 (CuB), possibly by a conformationally mediated change in the reduction potential of heme a3 or in the kinetics of the electron-transfer process. Dinuclear Copper Ion 344-347 cytochrome c, somatic Homo sapiens 203-215 2454843-0 1988 The location of CuA in mammalian cytochrome c oxidase. Dinuclear Copper Ion 16-19 cytochrome c, somatic Homo sapiens 33-45 3000820-3 1986 When all cytochrome c has been oxidized, CuA is also completely oxidized, whereas cytochrome a is still partially reduced. Dinuclear Copper Ion 41-44 cytochrome c, somatic Homo sapiens 9-21 1965780-1 1990 The kinetics of electron entry in beef heart cytochrome c oxidase have been studied by stopped-flow spectroscopy following chemical modification of the CuA site with mercurials. Dinuclear Copper Ion 152-155 cytochrome c, somatic Homo sapiens 45-57 1965780-2 1990 In this derivative CuA is no longer reducible by cytochrome c while cytochrome alpha may accept electrons from the latter with rates comparable to the native enzyme. Dinuclear Copper Ion 19-22 cytochrome c, somatic Homo sapiens 49-61 2854415-10 1988 It is proposed that the fast phase of cytochrome c oxidation is the result of electron transfer to O2, either via CuA or direct to the oxygen binding site. Dinuclear Copper Ion 114-117 cytochrome c, somatic Homo sapiens 38-50 30315812-4 2019 It predicts that the off rate constants for reduced and oxidized Cytc can be unequal and that the non-Nernst response of CuA and heme a is due to disequilibrium between free Cytc and CuA rather than redox anticooperativity. Dinuclear Copper Ion 121-124 cytochrome c, somatic Homo sapiens 174-178