The catalytic pathway of cytochrome P450cam at atomic resolution

Ilme Schlichting, Joel Berendzen, Kelvin Chu, Ann M. Stock, Shelley A. Maves, David E. Benson, Robert M. Sweet, Dagmar Ringe, Gregory A. Petsko, Stephen G. Sligar

Research output: Contribution to journalArticle

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.

Original languageEnglish (US)
Pages (from-to)1615-1622
Number of pages8
JournalScience
Volume287
Issue number5458
DOIs
StatePublished - Mar 3 2000

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    Schlichting, I., Berendzen, J., Chu, K., Stock, A. M., Maves, S. A., Benson, D. E., Sweet, R. M., Ringe, D., Petsko, G. A., & Sligar, S. G. (2000). The catalytic pathway of cytochrome P450cam at atomic resolution. Science, 287(5458), 1615-1622. https://doi.org/10.1126/science.287.5458.1615