PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
25881547-5	2015	We find here that the response of ccp1Delta and ccp1(W191F) cells to SIN-1 mirrors that to H2O2, identifying Ccp1 as a sensor of both peroxides.	Peroxides	134-143	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	34-38	
25881547-9	2015	Overall, our results reveal that yeast cells mount a common antioxidant response to ONOO(H) and H2O2, with Ccp1 playing a pivotal role as an inorganic peroxide sensor.	Peroxides	151-159	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	107-111	
25881547-5	2015	We find here that the response of ccp1Delta and ccp1(W191F) cells to SIN-1 mirrors that to H2O2, identifying Ccp1 as a sensor of both peroxides.	Peroxides	134-143	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	109-113	
7547943-1	1995	Cytochrome c peroxidase (CcP) reacts with peroxide to form compound I, an intermediate that has an oxy-ferryl iron center and a stable indolyl radical at Trp 191.	Peroxides	42-50	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	0-23	
7547943-1	1995	Cytochrome c peroxidase (CcP) reacts with peroxide to form compound I, an intermediate that has an oxy-ferryl iron center and a stable indolyl radical at Trp 191.	Peroxides	42-50	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	25-28	
7547943-4	1995	The Trp 191-->Phe enzyme [CcP(MI,F191)] reacts with peroxide to form an oxy-ferryl iron center and a transient porphyrin radical.	Peroxides	55-63	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	29-32	
7547943-5	1995	The reaction of Cc from horse and yeast with peroxide-oxidized CcP(MI,F191) was characterized under transient and steady-state conditions.	Peroxides	45-53	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	63-66	
7547943-13	1995	Transient changes in the absorption spectrum further indicate that steady-state oxidation of Cc2+ by CcP(MI,F191) occurs via reaction of peroxide with the oxy-ferryl enzyme.	Peroxides	137-145	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	101-104	
2156573-4	1990	The initial peroxide-oxidation product of CcP(MI, F191) is an oxyferryl porphyrin pi-cation radical intermediate in contrast to the oxyferryl amino-acid radical intermediate formed upon oxidation of CcP or CcP(MI) with hydrogen peroxide.	Peroxides	12-20	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	42-45	
1847080-1	1991	The reaction of ferric cytochrome c peroxidase (CcP) from Saccharomyces cerevisiae with peroxide produces compound I, characterized by both an oxyferryl iron center and a protein-based free radical.	Peroxides	88-96	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	23-46	
1847080-1	1991	The reaction of ferric cytochrome c peroxidase (CcP) from Saccharomyces cerevisiae with peroxide produces compound I, characterized by both an oxyferryl iron center and a protein-based free radical.	Peroxides	88-96	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	48-51	
5116561-8	1971	The peroxide compound of yeast cytochrome c peroxidase was found to have two oxidizing equivalents accessible to cytochrome c but only one readily accessible to ferrocyanide.	Peroxides	4-12	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	31-54	
2557891-2	1989	Peroxide oxidation of a mutant cytochrome c peroxidase, in which Trp-191 has been replaced by Phe through site-directed mutagenesis, produces an oxidized intermediate whose stable UV/visible absorption spectrum is very similar to that of compound I of the native yeast enzyme.	Peroxides	0-8	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	31-54	
2853973-6	1988	The rate of peroxide-dependent oxidation of ferrocytochrome c by the mutant CCP is reduced only 2-fold relative to that of the parental CCP, under steady-state conditions.	Peroxides	12-20	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	136-139	
2853973-0	1988	Site-directed mutagenesis of yeast cytochrome c peroxidase shows histidine 181 is not required for oxidation of ferrocytochrome c. The long-distance electron transfer observed in the complex formed between ferrocytochrome c and compound I, the peroxide-oxidized form of cytochrome c peroxidase (CCP), has been proposed to occur through the participation of His 181 of CCP and Phe 87 of yeast iso-1 cytochrome c [Poulos, T. L., & Kraut, J.	Peroxides	244-252	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	35-58	
2853973-6	1988	The rate of peroxide-dependent oxidation of ferrocytochrome c by the mutant CCP is reduced only 2-fold relative to that of the parental CCP, under steady-state conditions.	Peroxides	12-20	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	76-79