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  The catalytic pathway of cytochrome P450cam at atomic resolution

Schlichting, I., Berendzen, J., Chu, K., Stock, A. M., Maves, S. A., Benson, D. E., et al. (2000). The catalytic pathway of cytochrome P450cam at atomic resolution. Science, 287, 1615-1622. doi:10.1126/science.287.5458.1615.

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Science_287_2000_1615.pdf (Any fulltext), 668KB
 
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Schlichting, Ilme1, Author              
Berendzen, Joel, Author
Chu, Kelvin, Author
Stock, Ann M., Author
Maves, Shelley A., Author
Benson, David E., Author
Sweet, Robert M., Author
Ringe, Dagmar1, Author              
Petsko, Gregory A., Author
Sligar, Stephen G., Author
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1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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 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.

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Language(s): eng - English
 Dates: 1999-10-222000-02-012000-05-03
 Publication Status: Published in print
 Pages: 8
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 Table of Contents: -
 Rev. Type: Peer
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Title: Science
Source Genre: Journal
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Publ. Info: Washington, D.C. : American Association for the Advancement of Science
Pages: - Volume / Issue: 287 Sequence Number: - Start / End Page: 1615 - 1622 Identifier: ISSN: 0036-8075
CoNE: https://pure.mpg.de/cone/journals/resource/991042748276600_1