PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
19415898-1	2009	During the operation of cytochrome bc(1), a key enzyme of biological energy conversion, the iron-sulfur head domain of one of the subunits of the catalytic core undergoes a large-scale movement from the catalytic quinone oxidation Q(o) site to cytochrome c(1).	quinone	213-220	cytochrome c, somatic	Homo sapiens	244-256	
26062463-14	2016	These data provide evidence that the covalent binding of PCB quinone metabolites to cytochrome c may be included among the toxic effects of PCBs.	quinone	61-68	cytochrome c, somatic	Homo sapiens	84-96	
25540143-0	2015	Electronic connection between the quinone and cytochrome C redox pools and its role in regulation of mitochondrial electron transport and redox signaling.	quinone	34-41	cytochrome c, somatic	Homo sapiens	46-58	
25540143-2	2015	One of the mitochondrial complexes, complex III (cytochrome bc1 or ubiquinol:cytochrome c oxidoreductase), provides an electronic connection between these two diffusible redox pools linking in a fully reversible manner two-electron quinone oxidation/reduction with one-electron cytochrome c reduction/oxidation.	quinone	232-239	cytochrome c, somatic	Homo sapiens	77-89	
25540143-2	2015	One of the mitochondrial complexes, complex III (cytochrome bc1 or ubiquinol:cytochrome c oxidoreductase), provides an electronic connection between these two diffusible redox pools linking in a fully reversible manner two-electron quinone oxidation/reduction with one-electron cytochrome c reduction/oxidation.	quinone	232-239	cytochrome c, somatic	Homo sapiens	278-290	
21527774-0	2011	The frequency of 1,4-benzoquinone-lysine adducts in cytochrome c correlate with defects in apoptosome activation.	quinone	17-33	cytochrome c, somatic	Homo sapiens	52-64	
21527774-4	2011	Site-specific BQ-lysine adducts are found on residues in cytochrome c that are necessary for protein-protein interactions, and these adducts contribute to interferences in its ability to facilitate apoptosome formation.	quinone	14-16	cytochrome c, somatic	Homo sapiens	57-69	
20513347-1	2010	The two spatially distant quinone-binding sites of the ubihydroquinone: cytochrome c oxidoreductase (cyt bc(1)) complex have been shown to influence one another in some fashion.	quinone	26-33	cytochrome c, somatic	Homo sapiens	72-84	
16343695-7	2006	Pretreatment with the sulfhydryl antioxidant N-acetylcysteine or the quinone reductase inducer dimethyl fumarate prevents the ETC inhibition and cytochrome c release following BH4 exposure, suggesting the involvement of quinone products.	quinone	69-76	cytochrome c, somatic	Homo sapiens	145-157	
14961113-2	2004	This includes the intensely studied cytochrome bc1, which catalyses electron transfer between quinone and cytochrome c.	quinone	94-101	cytochrome c, somatic	Homo sapiens	106-118	
11405891-5	2001	In contrast to the quinone complex, the thermoinduced transition of the macromolecular RC complex to the state providing effective electron transport from the multiheme cytochrome c to the photoactive bacteriochlorophyll dimer within the temperature range 220-280 K accounts for tens of seconds.	quinone	19-26	cytochrome c, somatic	Homo sapiens	169-181	
9251814-4	1997	The kinetic limitation of the photocycle was attributed to the turnover of the cytochrome c binding site (pH < 6), light intensity and quinone/quinol exchange (6 < pH < 8), and proton-coupled second electron transfer in the quinone acceptor complex (pH > 8).	quinone	233-240	cytochrome c, somatic	Homo sapiens	79-91	
2546562-2	1989	Moreover, our data strongly suggest that two catalytic sites are present, one for cytochrome c and one for quinone type compounds.	quinone	107-114	cytochrome c, somatic	Homo sapiens	82-94	
2556468-5	1989	N-Acetylcysteine inhibited quinone-stimulated cytochrome C reduction at high concentrations.	quinone	27-34	cytochrome c, somatic	Homo sapiens	46-58	
2831977-7	1988	During illumination of reaction center membranes supplemented with cytochrome c and a ubiquinone pool, there is a small but significant steady-state current which is considered to be caused by the re-oxidation of photoreduced quinone by molecular oxygen.	quinone	89-96	cytochrome c, somatic	Homo sapiens	67-79