PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
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	
8214607-0	1993	Electrocatalytic reduction of hydrogen peroxide at a stationary pyrolytic graphite electrode surface in the presence of cytochrome c peroxidase: a description based on a microelectrode array model for adsorbed enzyme molecules.	Graphite	74-82	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	120-143	
8214607-1	1993	Electrochemical reduction of H2O2 at pyrolytic graphite disc electrodes of radius 2.5 mm occurs at readily accessible potentials (600 mV versus the standard hydrogen electrode) in the presence of yeast cytochrome c peroxidase.	Graphite	47-55	cytochrome-c peroxidase	Saccharomyces cerevisiae S288C	202-225