Pub. Date : 2001 Sep 26
PMID : 11562206
10 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | A distal histidine mutant (H52Q) of yeast cytochrome c peroxidase catalyzes the oxidation of H(2)O(2) instead of its reduction. | Histidine | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 2 | A distal histidine mutant (H52Q) of yeast cytochrome c peroxidase catalyzes the oxidation of H(2)O(2) instead of its reduction. | Hydrogen Peroxide | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 3 | 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 | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 4 | 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 | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 5 | 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 | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 6 | 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 | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 7 | 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 | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 8 | 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 | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 9 | 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 | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 10 | 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 | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |