Pub. Date : 1994 Jul 26
PMID : 8038158
10 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Interaction domain for the reaction of cytochrome c with the radical and the oxyferryl heme in cytochrome c peroxidase compound I. Site-directed mutants of cytochrome c peroxidase (CcP) were created to modify the interaction domain between CcP and yeast iso-1-cytochrome c (yCC) seen in the crystal structure of the CcP-yCC complex [Pelletier & Kraut (1992) Science 258, 1748-1755]. | Adenosine Monophosphate | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 2 | Interaction domain for the reaction of cytochrome c with the radical and the oxyferryl heme in cytochrome c peroxidase compound I. Site-directed mutants of cytochrome c peroxidase (CcP) were created to modify the interaction domain between CcP and yeast iso-1-cytochrome c (yCC) seen in the crystal structure of the CcP-yCC complex [Pelletier & Kraut (1992) Science 258, 1748-1755]. | Adenosine Monophosphate | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 3 | Interaction domain for the reaction of cytochrome c with the radical and the oxyferryl heme in cytochrome c peroxidase compound I. Site-directed mutants of cytochrome c peroxidase (CcP) were created to modify the interaction domain between CcP and yeast iso-1-cytochrome c (yCC) seen in the crystal structure of the CcP-yCC complex [Pelletier & Kraut (1992) Science 258, 1748-1755]. | Adenosine Monophosphate | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 4 | In the crystalline CcP-yCC complex, two acidic regions of CcP contact lysine residues on yCC. | Lysine | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 5 | In the crystalline CcP-yCC complex, two acidic regions of CcP contact lysine residues on yCC. | Lysine | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 6 | Stopped-flow experiments carried out in 310 mM ionic strength buffer at pH 7 revealed that yCC initially reduced the indole radical on Trp-191 of the parent CcP compound I with a bimolecular rate constant ka = 2.5 x 10(8) M-1 s-1. | indole radical | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 7 | Stopped-flow experiments carried out in 310 mM ionic strength buffer at pH 7 revealed that yCC initially reduced the indole radical on Trp-191 of the parent CcP compound I with a bimolecular rate constant ka = 2.5 x 10(8) M-1 s-1. | Tryptophan | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 8 | CcP mutants D34N and E290N that are closest to a complementary yCC lysine residue in the crystalline CcP-yCC complex gave the lowest values for ka and kb, which were 25-50% of the values of the CcP parent. | Lysine | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 9 | CcP mutants D34N and E290N that are closest to a complementary yCC lysine residue in the crystalline CcP-yCC complex gave the lowest values for ka and kb, which were 25-50% of the values of the CcP parent. | Lysine | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 10 | CcP mutants D34N and E290N that are closest to a complementary yCC lysine residue in the crystalline CcP-yCC complex gave the lowest values for ka and kb, which were 25-50% of the values of the CcP parent. | Lysine | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |