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(+)-camphor + reduced putidaredoxin + O2 = (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
(+)-camphor + reduced putidaredoxin + O2 = (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
reaction mechanism
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(+)-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
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(+)-camphor + reduced putidaredoxin + O2 = (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
binding of putidaredoxin forces selection of the active conformation of enzyme
(+)-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
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(+)-camphor + reduced putidaredoxin + O2 = (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
oxygen-transfer reaction via a monooxygenation mechanism
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(+)-camphor + reduced putidaredoxin + O2 = (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
putidaredoxin acts as a shuttle for transport of electrons from putidaredoxin reductase to enzyme
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(+)-camphor + reduced putidaredoxin + O2 = (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
the acvtive conformation of enzyme is stabilized by binding of the substrate at the active site
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(+)-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
(+)-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
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(+)-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
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(+)-camphor + reduced putidaredoxin + O2 = (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
reaction mechanism and cycle of the enzyme including postulated intermediates, detailed overview
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(+)-camphor + reduced putidaredoxin + O2 = (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
reaction mechanism involving a heme ring and residue Asp297, modelling of the hydroxylation of camphor and the hydrogen abstraction from heme using combined quantum mechanical/molecular mechanical method
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(+)-camphor + reduced putidaredoxin + O2 = (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
reaction mechanism, and second reductive step of the mechanism of interaction and electron transfer, overview
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(+)-camphor + reduced putidaredoxin + O2 = (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
rebound mechanism of C-H hydroxylation by P450, molecular dynamics
(+)-camphor + reduced putidaredoxin + O2 = (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
the active site structure changes due to putidaredoxin-enzyme interaction involving salt bridge and hydrogen bonding network between Arg112, His355, Leu356, and the heme ligand Cys357
(+)-camphor + reduced putidaredoxin + O2 = (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
via H2O2 and a nucleophilic intermediate, the substrate can modulate the properties of both the monoxygenase active-oxygen intermediates and the proton-delivery network that encompasses them, the catalytic cycle, overview
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(+)-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
(+)-camphor + reduced putidaredoxin + O2 = (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
proposed catalytic cycle for cytochrome P450, overview
(+)-camphor + reduced putidaredoxin + O2 = (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
proposed catalytic cycle for cytochrome P450, overview
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(+)-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
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(+)-camphor + reduced putidaredoxin + O2 = (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + H2O
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