Pub. Date : 1995 Sep 19
PMID : 7547943
19 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Regulation of interprotein electron transfer by Trp 191 of cytochrome c peroxidase. | Tryptophan | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 2 | 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 | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 3 | 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 | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 4 | 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 | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 5 | 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 | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 6 | 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 | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 7 | 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 | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 8 | 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 | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 9 | 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 | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 10 | The Trp 191-->Phe enzyme [CcP(MI,F191)] reacts with peroxide to form an oxy-ferryl iron center and a transient porphyrin radical. | Tryptophan | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 11 | The Trp 191-->Phe enzyme [CcP(MI,F191)] reacts with peroxide to form an oxy-ferryl iron center and a transient porphyrin radical. | Phenylalanine | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 12 | The Trp 191-->Phe enzyme [CcP(MI,F191)] reacts with peroxide to form an oxy-ferryl iron center and a transient porphyrin radical. | Peroxides | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 13 | The Trp 191-->Phe enzyme [CcP(MI,F191)] reacts with peroxide to form an oxy-ferryl iron center and a transient porphyrin radical. | Iron | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 14 | 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 | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 15 | The reaction of Cc from horse and yeast with peroxide-oxidized CcP(MI,F191) was characterized under transient and steady-state conditions. | Peroxides | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 16 | 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 | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 17 | 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 | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 18 | 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+ | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 19 | 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 | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |