Pub. Date : 1995 Jan 24
PMID : 7827055
23 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Photooxidation of Trp-191 in cytochrome c peroxidase by ruthenium-cytochrome c derivatives. | Tryptophan | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 2 | A novel photoinduced electron-transfer reaction is reported in complexes between resting ferric state cytochrome c peroxidase (CcP) and several horse cytochrome c derivatives labeled at single lysine amino groups with [bis(bipyridine)](dicarboxybipyridine)ruthenium(II) (Ru-CC). | Lysine | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 3 | A novel photoinduced electron-transfer reaction is reported in complexes between resting ferric state cytochrome c peroxidase (CcP) and several horse cytochrome c derivatives labeled at single lysine amino groups with [bis(bipyridine)](dicarboxybipyridine)ruthenium(II) (Ru-CC). | Lysine | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 4 | A novel photoinduced electron-transfer reaction is reported in complexes between resting ferric state cytochrome c peroxidase (CcP) and several horse cytochrome c derivatives labeled at single lysine amino groups with [bis(bipyridine)](dicarboxybipyridine)ruthenium(II) (Ru-CC). | [bis(bipyridine)](dicarboxybipyridine)ruthenium(ii) | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 5 | A novel photoinduced electron-transfer reaction is reported in complexes between resting ferric state cytochrome c peroxidase (CcP) and several horse cytochrome c derivatives labeled at single lysine amino groups with [bis(bipyridine)](dicarboxybipyridine)ruthenium(II) (Ru-CC). | [bis(bipyridine)](dicarboxybipyridine)ruthenium(ii) | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 6 | A novel photoinduced electron-transfer reaction is reported in complexes between resting ferric state cytochrome c peroxidase (CcP) and several horse cytochrome c derivatives labeled at single lysine amino groups with [bis(bipyridine)](dicarboxybipyridine)ruthenium(II) (Ru-CC). | ru-cc | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 7 | A novel photoinduced electron-transfer reaction is reported in complexes between resting ferric state cytochrome c peroxidase (CcP) and several horse cytochrome c derivatives labeled at single lysine amino groups with [bis(bipyridine)](dicarboxybipyridine)ruthenium(II) (Ru-CC). | ru-cc | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 8 | Photoexcitation of Ru(II) in the 1:1 Ru-27-CC:CcP complex results in formation of a metal-to-ligand charge-transfer state, Ru(II*), which is a strong reducing agent and rapidly transfers an electron to the CC heme Fe(III) with rate constant k1 = 2.3 x 10(7) s-1. | ru(ii) | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 9 | Photoexcitation of Ru(II) in the 1:1 Ru-27-CC:CcP complex results in formation of a metal-to-ligand charge-transfer state, Ru(II*), which is a strong reducing agent and rapidly transfers an electron to the CC heme Fe(III) with rate constant k1 = 2.3 x 10(7) s-1. | ru-27-cc | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 10 | Photoexcitation of Ru(II) in the 1:1 Ru-27-CC:CcP complex results in formation of a metal-to-ligand charge-transfer state, Ru(II*), which is a strong reducing agent and rapidly transfers an electron to the CC heme Fe(III) with rate constant k1 = 2.3 x 10(7) s-1. | Metals | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 11 | Photoexcitation of Ru(II) in the 1:1 Ru-27-CC:CcP complex results in formation of a metal-to-ligand charge-transfer state, Ru(II*), which is a strong reducing agent and rapidly transfers an electron to the CC heme Fe(III) with rate constant k1 = 2.3 x 10(7) s-1. | Heme | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 12 | Photoexcitation of Ru(II) in the 1:1 Ru-27-CC:CcP complex results in formation of a metal-to-ligand charge-transfer state, Ru(II*), which is a strong reducing agent and rapidly transfers an electron to the CC heme Fe(III) with rate constant k1 = 2.3 x 10(7) s-1. | Iron | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 13 | The cycle is completed by electron transfer from Fe(II) in CC to the Trp-191 radical in CcP with rate constant k4 = 6.1 x 10(4) s-1. | ammonium ferrous sulfate | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 14 | The cycle is completed by electron transfer from Fe(II) in CC to the Trp-191 radical in CcP with rate constant k4 = 6.1 x 10(4) s-1. | Tryptophan | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 15 | The cycle is completed by electron transfer from Fe(II) in CC to the Trp-191 radical in CcP with rate constant k4 = 6.1 x 10(4) s-1. | antibiotic K 4 | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 16 | The Ru group is located close to the interaction domain in the Ru-27-CC:CcP complex, allowing rapid electron transfer with both the heme in CC and Trp-191 in CcP. | Ruthenium | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 17 | The Ru group is located close to the interaction domain in the Ru-27-CC:CcP complex, allowing rapid electron transfer with both the heme in CC and Trp-191 in CcP. | Ruthenium | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 18 | The Ru group is located close to the interaction domain in the Ru-27-CC:CcP complex, allowing rapid electron transfer with both the heme in CC and Trp-191 in CcP. | Heme | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 19 | The Ru group is located close to the interaction domain in the Ru-27-CC:CcP complex, allowing rapid electron transfer with both the heme in CC and Trp-191 in CcP. | Heme | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 20 | The Ru group is located close to the interaction domain in the Ru-27-CC:CcP complex, allowing rapid electron transfer with both the heme in CC and Trp-191 in CcP. | Tryptophan | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 21 | The Ru group is located close to the interaction domain in the Ru-27-CC:CcP complex, allowing rapid electron transfer with both the heme in CC and Trp-191 in CcP. | Tryptophan | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 22 | The electron-transfer reaction was observed in CcP mutants modified at residues in the heme crevice, R48K, R48L, H52L, M230I, and M231I, but not in D235N which destabilizes the radical on Trp-191. | Heme | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 23 | The electron-transfer reaction was observed in CcP mutants modified at residues in the heme crevice, R48K, R48L, H52L, M230I, and M231I, but not in D235N which destabilizes the radical on Trp-191. | Tryptophan | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |