PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
8395206-7	1993	The rate constant for electron transfer from the cytochrome c heme to CuA is greater than 10(5) s-1, and the rate constant for electron transfer from CuA to cytochrome a is 2 x 10(4) s-1.	Dinuclear Copper Ion	70-73	LOC104968582	Bos taurus	49-61	
8395206-7	1993	The rate constant for electron transfer from the cytochrome c heme to CuA is greater than 10(5) s-1, and the rate constant for electron transfer from CuA to cytochrome a is 2 x 10(4) s-1.	Dinuclear Copper Ion	150-153	LOC104968582	Bos taurus	49-61	
27605664-7	2016	The redox-coupled x-ray structural changes in Glu198, which bridges the Mg2+ and CuA (the initial electron acceptor from cytochrome c) sites, suggest that the CuA-Glu198-Mg2+ system drives redox-coupled transfer of protons pooled in the water cluster to the H-pathway.	Dinuclear Copper Ion	81-84	LOC104968582	Bos taurus	121-133	
27605664-7	2016	The redox-coupled x-ray structural changes in Glu198, which bridges the Mg2+ and CuA (the initial electron acceptor from cytochrome c) sites, suggest that the CuA-Glu198-Mg2+ system drives redox-coupled transfer of protons pooled in the water cluster to the H-pathway.	Dinuclear Copper Ion	159-162	LOC104968582	Bos taurus	121-133