title: A kinetic study of the alkaline transitions in cytochrome c peroxidase.
abstract: Cytochrome c peroxidase undergoes a complex series of transitions between pH 8 and 14. Seven distinct spectral transitions occur between 4 ms and 24 h after exposure to alkaline pH. The fastest transition occurs within the mixing time of a stopped-flow instrument and converts the native high-spin ferric form of the enzyme to a low-spin form which may be the hydroxy complex of the enzyme. An apparent pKa of 9.7 +/- 0.2 relates the native and initial alkaline form of the enzyme. Three other low-spin enzyme forms are evident from the experimental data prior to denaturation of the enzyme and complete exposure of the heme to the solvent. The final denaturation process occurs with an apparent pKa of 10.3 +/- 0.3.
authors.forename: B K
authors.initials: BK
authors.lastname: Dhaliwal
authors.forename: J E
authors.initials: JE
authors.lastname: Erman
mesh_terms: D003578:Cytochrome-c Peroxidase / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D010544:Peroxidases / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D013057:Spectrum Analysis
chemical_list: D010544:Peroxidases; D003578:Cytochrome-c Peroxidase