PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
8286338-0	1994	Fluorescence investigation of yeast cytochrome c peroxidase oxidation by H2O2 and enzyme activities of the oxidized enzyme.	Hydrogen Peroxide	73-77	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	36-59	
8286338-1	1994	The role of tryptophan residues as endogenous electron donors in cytochrome c peroxidase (CCP) was examined by protein steady-state fluorescence.	Tryptophan	12-22	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	65-88	
8286338-1	1994	The role of tryptophan residues as endogenous electron donors in cytochrome c peroxidase (CCP) was examined by protein steady-state fluorescence.	Tryptophan	12-22	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	90-93	
8286338-2	1994	Compound I and more highly oxidized forms of CCP were formed by adding 1, 3, and 10 equiv of H2O2 to 5 microM protein at pH 7.0 in the absence of exogenous reducing substrates.	Hydrogen Peroxide	93-97	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	45-48	
8286338-3	1994	Addition of native CCP to 8 M urea at pH 1.5 relieved heme quenching, and compound I exhibited 90 +/- 4% fluorescence relative to unoxidized CCP, consistent with the loss of 0.7 +/- 0.2 tryptophan and the assignment of the primary radical site to Trp191.	Urea	30-34	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	19-22	
8286338-3	1994	Addition of native CCP to 8 M urea at pH 1.5 relieved heme quenching, and compound I exhibited 90 +/- 4% fluorescence relative to unoxidized CCP, consistent with the loss of 0.7 +/- 0.2 tryptophan and the assignment of the primary radical site to Trp191.	Heme	54-58	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	19-22	
8286338-3	1994	Addition of native CCP to 8 M urea at pH 1.5 relieved heme quenching, and compound I exhibited 90 +/- 4% fluorescence relative to unoxidized CCP, consistent with the loss of 0.7 +/- 0.2 tryptophan and the assignment of the primary radical site to Trp191.	Tryptophan	186-196	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	19-22	
8286338-4	1994	CCP oxidized with 10-fold excess H2O2 exhibited 65 +/- 1% relative fluorescence, indicating loss of 2.4 +/- 0.1 tryptophans.	Hydrogen Peroxide	33-37	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	0-3	
8286338-4	1994	CCP oxidized with 10-fold excess H2O2 exhibited 65 +/- 1% relative fluorescence, indicating loss of 2.4 +/- 0.1 tryptophans.	Tryptophan	112-123	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	0-3	
8286338-5	1994	Compound I and the higher oxidized forms of CCP spontaneously decayed to ferric CCP species over approximately 24 h with the loss of approximately 0.5 additional tryptophan in each case.	Tryptophan	162-172	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	44-47	
8286338-9	1994	The fluorescence decrease with time paralleled the decrease in activity of H2O2-oxidized CCP using both ferrocytochrome c and ferrocyanide as substrates, indicating that tryptophan and activity loss occurred on similar time scales.	Hydrogen Peroxide	75-79	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	89-92	
8286338-9	1994	The fluorescence decrease with time paralleled the decrease in activity of H2O2-oxidized CCP using both ferrocytochrome c and ferrocyanide as substrates, indicating that tryptophan and activity loss occurred on similar time scales.	hexacyanoferrate II	126-138	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	89-92	
8286338-9	1994	The fluorescence decrease with time paralleled the decrease in activity of H2O2-oxidized CCP using both ferrocytochrome c and ferrocyanide as substrates, indicating that tryptophan and activity loss occurred on similar time scales.	Tryptophan	170-180	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	89-92