Pseudomonas cytochrome c peroxidase XI. Kinetics of the peroxidatic oxidation of Pseudomonas respiratory chain components.
The steady state kinetics of cytochrome c peroxidase from Pseudomonas aeruginosa (PaCCP) has been studied by initial velocity techniques using several cytochromes c (550 and 555 P. aeruginosa; 551 P. fluorescens) and Pseudomonas azurin as electron donors and hydrogen peroxide as electron acceptor. From the initial velocity patterns a sequential mechanism with compulsory substrate-binding order is proposed for PaCCP. A comparative kinetic study of the peroxidatic oxidation of cytochrome c-551 (P. aeruginosa) by yeast cytochrome c peroxidase was made to evaluate the significance of electrostatic interactions in complex formation between the enzyme and substrates.
D000818:Animals; D003574:Cytochrome c Group / Q000378:metabolism; D003578:Cytochrome-c Peroxidase / Q000378:metabolism*; D004589:Electrophoresis, Disc; D006736:Horses; D006861:Hydrogen Peroxide; D007525:Isoelectric Focusing; D007700:Kinetics; D009206:Myocardium / Q000201:enzymology; D010084:Oxidation-Reduction; D010544:Peroxidases / Q000378:metabolism*; D011550:Pseudomonas aeruginosa / Q000201:enzymology*; D015003:Yeasts / Q000201:enzymology
D003574:Cytochrome c Group; D006861:Hydrogen Peroxide; D010544:Peroxidases; D003578:Cytochrome-c Peroxidase