PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
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	
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