Article
Apolar distal pocket mutants of yeast cytochrome c peroxidase: hydrogen peroxide reactivity and cyanide binding of the TriAla, TriVal, and TriLeu variants.
Biochimica et biophysica acta - 1 Jan 2013
Bidwai Anil K, Meyen Cassandra, Kilheeney Heather, Wroblewski Damian, Vitello Lidia B, Erman James E
Abstract excerpt
Three yeast cytochrome c peroxidase (CcP) variants with apolar distal heme pockets have been constructed. The CcP variants have Arg48, Trp51, and His52 mutated to either all alanines, CcP(triAla), all valines, CcP(triVal), or all leucines, CcP(triLeu). The triple mutants have detectable enzymatic activity at pH 6 but the activity is less than 0.02% that of wild-type CcP. The activity loss is primarily due to the...
Topics
- Binding Sites
- Cyanides
- Cytochrome-c Peroxidase
- Hydrogen Peroxide
- Hydrogen-Ion Concentration
- Mutation
- Saccharomyces cerevisiae
- Saccharomyces cerevisiae Proteins
- Spectrometry, Fluorescence