PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
11562206-0	2001	A distal histidine mutant (H52Q) of yeast cytochrome c peroxidase catalyzes the oxidation of H(2)O(2) instead of its reduction.	Histidine	9-18	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	42-65	
11562206-0	2001	A distal histidine mutant (H52Q) of yeast cytochrome c peroxidase catalyzes the oxidation of H(2)O(2) instead of its reduction.	Hydrogen Peroxide	93-101	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	42-65	
11562206-1	2001	A H52Q variant of yeast cytochrome c peroxidase (CcP), in which the distal histidine is replaced by glutamine, catalyzes oxidation of H(2)O(2) instead of reduction.	Histidine	75-84	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	24-47	
11562206-1	2001	A H52Q variant of yeast cytochrome c peroxidase (CcP), in which the distal histidine is replaced by glutamine, catalyzes oxidation of H(2)O(2) instead of reduction.	Histidine	75-84	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	49-52	
11562206-1	2001	A H52Q variant of yeast cytochrome c peroxidase (CcP), in which the distal histidine is replaced by glutamine, catalyzes oxidation of H(2)O(2) instead of reduction.	Glutamine	100-109	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	24-47	
11562206-1	2001	A H52Q variant of yeast cytochrome c peroxidase (CcP), in which the distal histidine is replaced by glutamine, catalyzes oxidation of H(2)O(2) instead of reduction.	Glutamine	100-109	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	49-52	
11562206-3	2001	In the presence of H(2)O(2), wild-type CcP, adsorbed on a graphite electrode, shows a strong catalytic reduction wave commencing at about 0.8V (pH 5.4); by contrast, H52Q does not exhibit this activity but instead shows a catalytic oxidation current at potentials in the region of 0.9 V. The oxidation current is partly suppressed in the presence of tetranitromethane (a superoxide scavenger) and is not observed for other mutants studied, including H52A.	Hydrogen Peroxide	19-27	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	39-42	
11562206-3	2001	In the presence of H(2)O(2), wild-type CcP, adsorbed on a graphite electrode, shows a strong catalytic reduction wave commencing at about 0.8V (pH 5.4); by contrast, H52Q does not exhibit this activity but instead shows a catalytic oxidation current at potentials in the region of 0.9 V. The oxidation current is partly suppressed in the presence of tetranitromethane (a superoxide scavenger) and is not observed for other mutants studied, including H52A.	Graphite	58-66	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	39-42	
11562206-3	2001	In the presence of H(2)O(2), wild-type CcP, adsorbed on a graphite electrode, shows a strong catalytic reduction wave commencing at about 0.8V (pH 5.4); by contrast, H52Q does not exhibit this activity but instead shows a catalytic oxidation current at potentials in the region of 0.9 V. The oxidation current is partly suppressed in the presence of tetranitromethane (a superoxide scavenger) and is not observed for other mutants studied, including H52A.	Tetranitromethane	350-367	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	39-42	
11562206-3	2001	In the presence of H(2)O(2), wild-type CcP, adsorbed on a graphite electrode, shows a strong catalytic reduction wave commencing at about 0.8V (pH 5.4); by contrast, H52Q does not exhibit this activity but instead shows a catalytic oxidation current at potentials in the region of 0.9 V. The oxidation current is partly suppressed in the presence of tetranitromethane (a superoxide scavenger) and is not observed for other mutants studied, including H52A.	Superoxides	371-381	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	39-42