PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
7547943-0	1995	Regulation of interprotein electron transfer by Trp 191 of cytochrome c peroxidase.	Tryptophan	48-51	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	59-82	
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	
7547943-1	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.	Iron	110-114	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.	Iron	110-114	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	25-28	
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.	indolyl radical	135-150	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.	indolyl radical	135-150	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	25-28	
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.	Tryptophan	154-157	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.	Tryptophan	154-157	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	25-28	
7547943-2	1995	During the normal catalytic cycle, the oxy-ferryl heme and the Trp 191 radical are reduced by sequential electron transfers from ferrous cytochrome c (Cc).	oxy-ferryl heme	39-54	cytochrome c, somatic	Equus caballus	137-149	
7547943-2	1995	During the normal catalytic cycle, the oxy-ferryl heme and the Trp 191 radical are reduced by sequential electron transfers from ferrous cytochrome c (Cc).	Tryptophan	63-66	cytochrome c, somatic	Equus caballus	137-149	
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.	Tryptophan	4-7	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	29-32	
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.	Phenylalanine	17-20	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	29-32	
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	
7547943-4	1995	The Trp 191-->Phe enzyme [CcP(MI,F191)] reacts with peroxide to form an oxy-ferryl iron center and a transient porphyrin radical.	Iron	86-90	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	29-32	
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.	porphyrin radical	114-131	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, somatic	Equus caballus	16-18	
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	
7547943-6	1995	The rate of ET from Cc to the oxy-ferryl heme of CcP(MI,F191) was decreased by at least 10,000-fold relative to the CcP(MI) parent.	oxy-ferryl heme	30-45	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	49-52	
7547943-11	1995	The steady-state activity of the mutant enzyme was 300-600-fold lower than the CcP(MI) parent, but kcat is 7-20 times greater than the rate constant for reduction of the oxy-ferryl heme under all conditions examined.	ferryl heme	174-185	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	79-82	
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.	cc2+	93-97	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	101-104	
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