Yeast cytochrome c peroxidase: mechanistic studies via protein engineering.
Cytochrome c peroxidase (CcP) is a yeast mitochondrial enzyme that catalyzes the reduction of hydrogen peroxide to water by ferrocytochrome c. It was the first heme enzyme to have its crystallographic structure determined and, as a consequence, has played a pivotal role in developing ideas about structural control of heme protein reactivity. Genetic engineering of the active site of CcP, along with structural, spectroscopic, and kinetic characterization of the mutant proteins has provided considerable insight into the mechanism of hydrogen peroxide activation, oxygen-oxygen bond cleavage, and formation of the higher-oxidation state intermediates in heme enzymes. The catalytic mechanism involves complex formation between cytochrome c and CcP. The cytochrome c/CcP system has been very useful in elucidating the complexities of long-range electron transfer in biological systems, including protein-protein recognition, complex formation, and intracomplex electron transfer processes.
Erman
James E
JE
Department of Chemistry and Biochemistry, Northern Illinois University, Normal Rd., DeKalb, IL 60115-2862, USA. jerman@niu.edu
Vitello
Lidia B
LB
D020134:Catalytic Domain / Q000235:genetics; D003574:Cytochrome c Group / Q000378:metabolism; D003578:Cytochrome-c Peroxidase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D004579:Electron Transport; D004789:Enzyme Activation / Q000187:drug effects; D006861:Hydrogen Peroxide / Q000494:pharmacology; D007700:Kinetics; D008956:Models, Chemical; D008958:Models, Molecular; D015394:Molecular Structure; D016297:Mutagenesis, Site-Directed; D011487:Protein Conformation; D015202:Protein Engineering; D012428:Ruthenium / Q000737:chemistry; D012441:Saccharomyces cerevisiae / Q000201:enzymology* / Q000235:genetics; D015032:Zinc / Q000737:chemistry
D003574:Cytochrome c Group; D012428:Ruthenium; D006861:Hydrogen Peroxide; D003578:Cytochrome-c Peroxidase; D015032:Zinc