Pub. Date : 1994 Jan 11
PMID : 8286338
13 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Fluorescence investigation of yeast cytochrome c peroxidase oxidation by H2O2 and enzyme activities of the oxidized enzyme. | Hydrogen Peroxide | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 2 | The role of tryptophan residues as endogenous electron donors in cytochrome c peroxidase (CCP) was examined by protein steady-state fluorescence. | Tryptophan | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 3 | The role of tryptophan residues as endogenous electron donors in cytochrome c peroxidase (CCP) was examined by protein steady-state fluorescence. | Tryptophan | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 4 | 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 | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 5 | 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 | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 6 | 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 | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 7 | 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 | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 8 | CCP oxidized with 10-fold excess H2O2 exhibited 65 +/- 1% relative fluorescence, indicating loss of 2.4 +/- 0.1 tryptophans. | Hydrogen Peroxide | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 9 | CCP oxidized with 10-fold excess H2O2 exhibited 65 +/- 1% relative fluorescence, indicating loss of 2.4 +/- 0.1 tryptophans. | Tryptophan | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 10 | 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 | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 11 | 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 | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 12 | 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 | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 13 | 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 | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |