Redox regulation of cytochrome P450cam mixed function oxidation by putidaredoxin and camphor ligation.
A methylene group of camphor is hydroxylated by a P450 monoxygenase system containing in addition to the cytochrome and flavoprotein dehydrogenase a two-iron, two-sulfur redox protein termed putidaredoxin. The regulatory control of electron transport equilibrium occurs via ligation of substrate and redoxin to the cytochrome. The component interactions and electron flow are represented clearly and concisely by a free energy state diagram of the coupled binding and redox transfer reactions.
D002164:Camphor / Q000378:metabolism*; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism*; D003580:Cytochromes / Q000378:metabolism; D004579:Electron Transport; D004734:Energy Metabolism; D005288:Ferredoxins / Q000378:metabolism*; D010084:Oxidation-Reduction; D011549:Pseudomonas / Q000378:metabolism*
D003580:Cytochromes; D005288:Ferredoxins; D002164:Camphor; D003577:Cytochrome P-450 Enzyme System