PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
8380332-0	1993	Fourier-transform infrared study of azide binding to the Fea3-CuB binuclear site of bovine heart cytochrome c oxidase: new evidence for a redox-linked conformational change at the binuclear site.	Azides	36-41	cytochrome c oxidase subunit 6A1, mitochondrial	Bos taurus	97-117	
8380332-1	1993	Azide binding to the Fea3-CuB site of cytochrome c oxidase purified from bovine heart mitochondria was investigated in various redox levels by Fourier-transform infrared spectroscopy.	Azides	0-5	cytochrome c oxidase subunit 6A1, mitochondrial	Bos taurus	38-58	
8380332-4	1993	Upon addition of cyanide to the preformed fully oxidized cytochrome c oxidase-azide complex, a new azide species exhibiting a sharp antisymmetric stretching band at 2032.5 cm-1 was formed.	Azides	78-83	cytochrome c oxidase subunit 6A1, mitochondrial	Bos taurus	57-77	
8380332-4	1993	Upon addition of cyanide to the preformed fully oxidized cytochrome c oxidase-azide complex, a new azide species exhibiting a sharp antisymmetric stretching band at 2032.5 cm-1 was formed.	Azides	99-104	cytochrome c oxidase subunit 6A1, mitochondrial	Bos taurus	57-77	
8380332-6	1993	This cytochrome c oxidase-azide-cyanide ternary complex is relatively stable, and cyanide ion replaces the 2032.5-cm-1 azide species very slowly, resulting in the formation of the Fea3(3+)-C-N-CuB2+ bridging structure characterized by the 2152-cm-1 band.	Azides	26-31	cytochrome c oxidase subunit 6A1, mitochondrial	Bos taurus	5-25	
8380332-7	1993	Upon the introduction of 1 electron equivalent to the fully oxidized cytochrome c oxidase-azide complex, an azide band at 2003.5 cm-1 developed.	Azides	90-95	cytochrome c oxidase subunit 6A1, mitochondrial	Bos taurus	69-89	
8380332-7	1993	Upon the introduction of 1 electron equivalent to the fully oxidized cytochrome c oxidase-azide complex, an azide band at 2003.5 cm-1 developed.	Azides	108-113	cytochrome c oxidase subunit 6A1, mitochondrial	Bos taurus	69-89	
1315769-0	1992	Infrared evidence of azide binding to iron, copper, and non-metal sites in heart cytochrome c oxidase.	Azides	21-26	cytochrome c oxidase subunit 6A1, mitochondrial	Bos taurus	81-101	
1315769-1	1992	Interactions of azide ion with bovine heart cytochrome c oxidase (CcO) at five redox levels (IV) to (0), obtained by zero to four electron reduction of fully oxidized enzyme CcO(IV), were monitored by infrared and visible/Soret spectra.	Azides	16-21	cytochrome c oxidase subunit 6A1, mitochondrial	Bos taurus	44-64	
1315769-1	1992	Interactions of azide ion with bovine heart cytochrome c oxidase (CcO) at five redox levels (IV) to (0), obtained by zero to four electron reduction of fully oxidized enzyme CcO(IV), were monitored by infrared and visible/Soret spectra.	Azides	16-21	cytochrome c oxidase subunit 6A1, mitochondrial	Bos taurus	66-69	
1315769-1	1992	Interactions of azide ion with bovine heart cytochrome c oxidase (CcO) at five redox levels (IV) to (0), obtained by zero to four electron reduction of fully oxidized enzyme CcO(IV), were monitored by infrared and visible/Soret spectra.	Azides	16-21	cytochrome c oxidase subunit 6A1, mitochondrial	Bos taurus	174-177	
1315769-2	1992	Partially reduced CcO gave three azide asymmetric stretch band at 2040, 2016, and 2004 cm-1 for CcO(III)N3 and two at 2040 and 2016 cm-1 for CcO(II)N3 and CcO(I)N3.	Azides	33-38	cytochrome c oxidase subunit 6A1, mitochondrial	Bos taurus	18-21	
1315769-2	1992	Partially reduced CcO gave three azide asymmetric stretch band at 2040, 2016, and 2004 cm-1 for CcO(III)N3 and two at 2040 and 2016 cm-1 for CcO(II)N3 and CcO(I)N3.	Azides	33-38	cytochrome c oxidase subunit 6A1, mitochondrial	Bos taurus	96-99	
1315769-2	1992	Partially reduced CcO gave three azide asymmetric stretch band at 2040, 2016, and 2004 cm-1 for CcO(III)N3 and two at 2040 and 2016 cm-1 for CcO(II)N3 and CcO(I)N3.	Azides	33-38	cytochrome c oxidase subunit 6A1, mitochondrial	Bos taurus	96-99	
1315769-2	1992	Partially reduced CcO gave three azide asymmetric stretch band at 2040, 2016, and 2004 cm-1 for CcO(III)N3 and two at 2040 and 2016 cm-1 for CcO(II)N3 and CcO(I)N3.	Azides	33-38	cytochrome c oxidase subunit 6A1, mitochondrial	Bos taurus	96-99	
30077971-5	2018	To experimentally test this, we examined X-ray structures of the azide-bound, oxidized bovine CcO and found that an azide derivative (N3--Fe a33+, CuB2+-N3-) induces a translational movement of the heme a3 plane.	Azides	65-70	cytochrome c oxidase subunit 6A1, mitochondrial	Bos taurus	94-97	
30077971-5	2018	To experimentally test this, we examined X-ray structures of the azide-bound, oxidized bovine CcO and found that an azide derivative (N3--Fe a33+, CuB2+-N3-) induces a translational movement of the heme a3 plane.	Azides	116-121	cytochrome c oxidase subunit 6A1, mitochondrial	Bos taurus	94-97