Pub. Date : 2003 Sep
PMID : 14505074
4 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Cytochrome c peroxidase (C cP) variants with an engineered Mn(II) binding site, including MnC cP [C cP(MI, G41E, V45E, H181D)], MnC cP(W191F), and MnC cP(W191F, W51F), that mimic manganese peroxidase (MnP), have been characterized by resonance Raman (RR) spectroscopy. | Manganese(2+) | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 2 | At neutral pH the frequencies of the nu(3) mode indicate that a pure five-coordinate heme iron exists in C cP(MI) whereas a six-coordinate low-spin iron is the dominant species in the C cP variants with the engineered Mn(II) binding site. | Iron | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 3 | At neutral pH the frequencies of the nu(3) mode indicate that a pure five-coordinate heme iron exists in C cP(MI) whereas a six-coordinate low-spin iron is the dominant species in the C cP variants with the engineered Mn(II) binding site. | Iron | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |
| 4 | At neutral pH the frequencies of the nu(3) mode indicate that a pure five-coordinate heme iron exists in C cP(MI) whereas a six-coordinate low-spin iron is the dominant species in the C cP variants with the engineered Mn(II) binding site. | Manganese(2+) | cytochrome-c peroxidase | Saccharomyces cerevisiae S288C |