PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 2851591-0 1988 Influence of 8-azido-ATP and other anions on the activity of cytochrome c oxidase. 8-azidoadenosine 5'-triphosphate 13-24 cytochrome c oxidase subunit 6A1, mitochondrial Bos taurus 61-81 7873550-0 1995 8-Azido-ATP modification of cytochrome c: retardation of its electron-transfer activity to cytochrome c oxidase. 8-azidoadenosine 5'-triphosphate 0-11 cytochrome c oxidase subunit 6A1, mitochondrial Bos taurus 91-111 7873550-1 1995 Horse heart cytochrome c has been modified by 8-azido-ATP and the electron-transfer activity of the modified cytochrome c"s to bovine heart cytochrome c oxidase (CcO) under physiological ionic strengths has been studied by the laser flash photolysis technique with 5-deazariboflavin and EDTA as the electron donor. 8-azidoadenosine 5'-triphosphate 46-57 cytochrome c oxidase subunit 6A1, mitochondrial Bos taurus 162-165 7873550-3 1995 The 8-azido-ATP-modified system exhibited less than 5% of the intracomplex electron-transfer rate observed between native cytochrome c and CcO under otherwise identical conditions. 8-azidoadenosine 5'-triphosphate 4-15 cytochrome c oxidase subunit 6A1, mitochondrial Bos taurus 139-142 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. 8-azidoadenosine 5'-triphosphate 236-247 cytochrome c oxidase subunit 6A1, mitochondrial Bos taurus 176-179