Abstract
Members of the cytochrome P450 superfamily catalyze the addition of molecular oxygen to nonactivated hydrocarbons at physiological temperature-a reaction that requires high temperature to proceed in the absence of a catalyst. Structures were obtained for three intermediates in the hydroxylation reaction of camphor by P450cam with trapping techniques and cryocrystallography. The structure of the ferrous dioxygen adduct of P450cam was determined with 0.91 angstrom wavelength x-rays; irradiation with 1.5 angstrom x-rays results in breakdown of the dioxygen molecule to an intermediate that would be consistent with an oxyferryl species. The structures show conformational changes in several important residues and reveal a network of bound water molecules that may provide the protons needed for the reaction.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Camphor / chemistry*
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Camphor / metabolism*
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Camphor 5-Monooxygenase / chemistry*
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Camphor 5-Monooxygenase / metabolism*
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Catalysis
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Crystallization
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Crystallography, X-Ray
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Electrons
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Ferric Compounds / chemistry
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Ferric Compounds / metabolism
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Ferrous Compounds / chemistry
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Ferrous Compounds / metabolism
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Hydrogen Bonding
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Hydroxylation
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Ligands
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Models, Molecular
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Molecular Conformation
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Oxygen / chemistry
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Oxygen / metabolism
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Protein Conformation
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Protein Structure, Secondary
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Protons
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Pseudomonas putida / enzymology
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Water / chemistry
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Water / metabolism
Substances
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Ferric Compounds
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Ferrous Compounds
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Ligands
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Protons
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Water
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Camphor
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Camphor 5-Monooxygenase
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Oxygen
Associated data
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PDB/1D24
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PDB/1D26
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PDB/1D28
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PDB/1D29