Article
The effect of the Asn82-->Asp mutation in yeast cytochrome c peroxidase studied by proton NMR spectroscopy.
European journal of biochemistry - 15 Aug 1994
Satterlee J D, Alam S L, Mauro J M, Erman J E, Poulos T L
Abstract excerpt
Proton NMR studies of the mutant of baker's yeast cytochrome c peroxidase-cyanide with the Asn 82-->Asp mutation ([N82D]cytochrome c peroxidase-CN) are presented and compared to the wild-type enzyme. This mutation alters an amino acid that forms a hydrogen bond to His52, the distal histidine residue that interacts in the heme pocket with heme-bound ligands. His52 is an important participant in the initial...
Topics
- Asparagine
- Aspartic Acid
- Cytochrome-c Peroxidase
- Histidine
- Hydrogen Bonding
- Magnetic Resonance Spectroscopy
- Mutagenesis, Site-Directed
- Mutation
- Saccharomyces cerevisiae