PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
10788423-9	2000	Such a movement seems necessary to shuttle electrons from the membrane-soluble quinol to the extramembrane heme of cytochrome c(1).	Hydroquinones	79-85	cytochrome c, somatic	Homo sapiens	115-127	
29705394-1	2018	Transfer of electron from quinol to cytochrome c is an integral part of catalytic cycle of cytochrome bc1.	Hydroquinones	26-32	cytochrome c, somatic	Homo sapiens	36-48	
29705394-2	2018	It is a multi-step reaction involving: i) electron transfer from quinol bound at the catalytic Qo site to the Rieske iron-sulfur ([2Fe-2S]) cluster, ii) large-scale movement of a domain containing [2Fe-2S] cluster (ISP-HD) towards cytochrome c1, iii) reduction of cytochrome c1 by reduced [2Fe-2S] cluster, iv) reduction of cytochrome c by cytochrome c1.	Hydroquinones	65-71	cytochrome c, somatic	Homo sapiens	231-243	
18272433-0	2008	Quinol type compound in cytochrome c preparations leads to non-enzymatic reduction of cytochrome c during the measurement of complex III activity.	Hydroquinones	0-6	cytochrome c, somatic	Homo sapiens	24-36	
18272433-0	2008	Quinol type compound in cytochrome c preparations leads to non-enzymatic reduction of cytochrome c during the measurement of complex III activity.	Hydroquinones	0-6	cytochrome c, somatic	Homo sapiens	86-98	
18272433-4	2008	Analysis of cytochrome c (producing a high-background) by fast protein liquid chromatography yielded a contaminant peak containing a lipid extractable component with redox spectra and mass spectroscopy fragmentation suggestive of a quinol.	Hydroquinones	232-238	cytochrome c, somatic	Homo sapiens	12-24	
16600173-1	2006	The Q-cycle mechanism of the bc1 complex explains how the electron transfer from ubihydroquinone (quinol, QH2) to cytochrome (cyt) c (or c2 in bacteria) is coupled to the pumping of protons across the membrane.	Hydroquinones	98-104	cytochrome c, somatic	Homo sapiens	114-132	
7832587-2	1994	The substrate specificity (quinol vs. cytochrome c) is reflected in the presence of a unique copper centre (CuA) in cytochrome c oxidases.	Hydroquinones	27-33	cytochrome c, somatic	Homo sapiens	116-128	
10932727-7	1997	The main difference between quinol- and the aa3-type cytochrome c-oxidases is the CuA center, which is absent in the quinol oxidases.	Hydroquinones	28-34	cytochrome c, somatic	Homo sapiens	53-65	
10932727-7	1997	The main difference between quinol- and the aa3-type cytochrome c-oxidases is the CuA center, which is absent in the quinol oxidases.	Hydroquinones	117-123	cytochrome c, somatic	Homo sapiens	53-65	
6319123-3	1983	Measurements of the H+/e- stoichiometry, with three different methods, show that four protons are released from the vesicles per 2e- flowing from quinols to cytochrome c, two of these protons formally deriving from scalar oxidation of quinols by cytochrome c.	Hydroquinones	146-153	cytochrome c, somatic	Homo sapiens	157-169	
6319123-3	1983	Measurements of the H+/e- stoichiometry, with three different methods, show that four protons are released from the vesicles per 2e- flowing from quinols to cytochrome c, two of these protons formally deriving from scalar oxidation of quinols by cytochrome c.	Hydroquinones	146-153	cytochrome c, somatic	Homo sapiens	246-258	
6319123-3	1983	Measurements of the H+/e- stoichiometry, with three different methods, show that four protons are released from the vesicles per 2e- flowing from quinols to cytochrome c, two of these protons formally deriving from scalar oxidation of quinols by cytochrome c.	Hydroquinones	235-242	cytochrome c, somatic	Homo sapiens	157-169	
14285230-0	1965	PHOTOREACTIONS OF CHLOROPLASTS AND CHLOROPHYLL A WITH HYDROQUINONES AND QUINONES: COUPLED PHOTOREDUCTION OF CYTOCHROME C.	Hydroquinones	54-67	cytochrome c, somatic	Homo sapiens	108-120	
6284121-2	1982	The kinetics of reduction of cytochrome c by catechol(s), quinol(s) and related compounds were investigated by stopped-flow spectrophotometry.	Hydroquinones	58-64	cytochrome c, somatic	Homo sapiens	29-41