1.14.15.1 (+)-camphor + reduced putidaredoxin + O2 = (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O active binding of substrate camphor, analysis by density functional theory calculations, residue Tyr96 is important forming a strong hydrogen bond, catalytic cycle of cytochrome P450, the strong hydrogen bonding is not affected by the enzyme's environment, reaction mechanism, overview 673054 1.14.15.1 (+)-camphor + reduced putidaredoxin + O2 = (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O binding of putidaredoxin forces selection of the active conformation of enzyme 658988 1.14.15.1 (+)-camphor + reduced putidaredoxin + O2 = (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O K+ plays an important role in substrate binding and structural and conformational stability of the enzyme 672100 1.14.15.1 (+)-camphor + reduced putidaredoxin + O2 = (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O mechanism of O2 activation: binding of O2 to ferrous P450cam to yield the ferric-superoxo form, oxyP450cam, followed by an irreversible, long-range electron transfer from putidaredoxin to reduce the oxyP450cam, camphor is bound to all enzyme forms, overview 672115 1.14.15.1 (+)-camphor + reduced putidaredoxin + O2 = (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O model for putidaredoxin activity, primary role of putidaredoxin is to prevent uncoupling by enforcing conformations of enzyme that prevent loss of substrate and to enforce conformations that permit efficient proton transfer 657999 1.14.15.1 (+)-camphor + reduced putidaredoxin + O2 = (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O multi-component mixed function oxidase, consisting of putidaredoxin reductase, putidaredoxin and cytochrome P450cam, heme-thiolate protein 347691 1.14.15.1 (+)-camphor + reduced putidaredoxin + O2 = (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O oxygen-transfer reaction via a monooxygenation mechanism 659825 1.14.15.1 (+)-camphor + reduced putidaredoxin + O2 = (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O proposed catalytic cycle for cytochrome P450, a ferryl-oxo Pi-cation porphyrin radical, is the putative oxidant that reacts directly with substrate, overview. The axial ligand to the heme iron, a cysteine thiolate, is generally believed to control P450 reactivity -, 746282 1.14.15.1 (+)-camphor + reduced putidaredoxin + O2 = (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O proposed catalytic cycle for cytochrome P450, overview -, 744343 1.14.15.1 (+)-camphor + reduced putidaredoxin + O2 = (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O putidaredoxin acts as a shuttle for transport of electrons from putidaredoxin reductase to enzyme 658056