The catalytic pathway of cytochrome p450cam at atomic resolution.

TitleThe catalytic pathway of cytochrome p450cam at atomic resolution.
Publication TypeJournal Article
Year of Publication2000
AuthorsSchlichting I, Berendzen J, Chu K, Stock AM, Maves SA, Benson DE, Sweet RM, Ringe D, Petsko GA, Sligar SG
Date Published2000 Mar 3
KeywordsCamphor, Camphor 5-Monooxygenase, Catalysis, Crystallization, Crystallography, X-Ray, Electrons, Ferric Compounds, Ferrous Compounds, Hydrogen Bonding, Hydroxylation, Ligands, Models, Molecular, Molecular Conformation, Oxygen, Protein Conformation, Protein Structure, Secondary, Protons, Pseudomonas putida, Water

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.

Alternate JournalScience
PubMed ID10698731
Grant ListGM31756 / GM / NIGMS NIH HHS / United States
GM33775 / GM / NIGMS NIH HHS / United States