PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
2471518-1	1989	Valinomycin binds to soluble and reconstituted cytochrome c oxidase (COX) in a stoichiometric manner, as shown by a spectral shift of the oxidized gamma-band.	Valinomycin	0-11	cytochrome c oxidase subunit 8A	Homo sapiens	69-72	
2471518-3	1989	Titration of the proton pumping activity of reconstituted COX with valinomycin reached a maximum of H+/e- - 0.73 after addition of 1 mole of valinomycin per mole of reconstituted COX.	Valinomycin	67-78	cytochrome c oxidase subunit 8A	Homo sapiens	58-61	
2471518-3	1989	Titration of the proton pumping activity of reconstituted COX with valinomycin reached a maximum of H+/e- - 0.73 after addition of 1 mole of valinomycin per mole of reconstituted COX.	Valinomycin	67-78	cytochrome c oxidase subunit 8A	Homo sapiens	179-182	
2471518-3	1989	Titration of the proton pumping activity of reconstituted COX with valinomycin reached a maximum of H+/e- - 0.73 after addition of 1 mole of valinomycin per mole of reconstituted COX.	Valinomycin	141-152	cytochrome c oxidase subunit 8A	Homo sapiens	58-61	
2471518-3	1989	Titration of the proton pumping activity of reconstituted COX with valinomycin reached a maximum of H+/e- - 0.73 after addition of 1 mole of valinomycin per mole of reconstituted COX.	Valinomycin	141-152	cytochrome c oxidase subunit 8A	Homo sapiens	179-182	
2471518-4	1989	It is concluded that K+-translocation in proton-pumping COX vesicles occurs via enzyme-bound valinomycin.	Valinomycin	93-104	cytochrome c oxidase subunit 8A	Homo sapiens	56-59