Substrate binding in the active site of cytochrome P450cam

Marcel Swart; Andre R. Groenhof; Andreas W. Ehlers; Koop Lammertsma

doi:10.1016/j.cplett.2004.12.092

Substrate binding in the active site of cytochrome P450cam

Marcel Swart, Andre R. Groenhof, Andreas W. Ehlers, Koop Lammertsma

Vrije Universiteit Amsterdam

Research output: Contribution to journal › Article › peer-review

6 Citations (Scopus)

Abstract

We have studied the binding of camphor in the active site of cytochrome P450cam with density functional theory (DFT) calculations. A strong hydrogen bond (>6 kcal/mol) to a tyrosine residue (Tyr96) is observed, that may account for the high specificity of the reaction taking place. The DFT interaction energy is well reproduced by QM/MM calculations, which allows for application of QM/MM to the catalytic cycle of cytochrome P450s. The substrate is distorted considerably due to the presence of the protein environment, which however does not have a large impact on the strong hydrogen bonding interactions.

Original language	English
Pages (from-to)	35-41
Number of pages	7
Journal	Chemical Physics Letters
Volume	403
Issue number	1-3
DOIs	https://doi.org/10.1016/j.cplett.2004.12.092
Publication status	Published - 14 Feb 2005
Externally published	Yes

ASJC Scopus subject areas

General Physics and Astronomy
Physical and Theoretical Chemistry

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10.1016/j.cplett.2004.12.092

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abstract = "We have studied the binding of camphor in the active site of cytochrome P450cam with density functional theory (DFT) calculations. A strong hydrogen bond (>6 kcal/mol) to a tyrosine residue (Tyr96) is observed, that may account for the high specificity of the reaction taking place. The DFT interaction energy is well reproduced by QM/MM calculations, which allows for application of QM/MM to the catalytic cycle of cytochrome P450s. The substrate is distorted considerably due to the presence of the protein environment, which however does not have a large impact on the strong hydrogen bonding interactions.",

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AU - Swart, Marcel

AU - Groenhof, Andre R.

AU - Ehlers, Andreas W.

AU - Lammertsma, Koop

PY - 2005/2/14

Y1 - 2005/2/14

N2 - We have studied the binding of camphor in the active site of cytochrome P450cam with density functional theory (DFT) calculations. A strong hydrogen bond (>6 kcal/mol) to a tyrosine residue (Tyr96) is observed, that may account for the high specificity of the reaction taking place. The DFT interaction energy is well reproduced by QM/MM calculations, which allows for application of QM/MM to the catalytic cycle of cytochrome P450s. The substrate is distorted considerably due to the presence of the protein environment, which however does not have a large impact on the strong hydrogen bonding interactions.

AB - We have studied the binding of camphor in the active site of cytochrome P450cam with density functional theory (DFT) calculations. A strong hydrogen bond (>6 kcal/mol) to a tyrosine residue (Tyr96) is observed, that may account for the high specificity of the reaction taking place. The DFT interaction energy is well reproduced by QM/MM calculations, which allows for application of QM/MM to the catalytic cycle of cytochrome P450s. The substrate is distorted considerably due to the presence of the protein environment, which however does not have a large impact on the strong hydrogen bonding interactions.

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JO - Chemical Physics Letters

JF - Chemical Physics Letters

IS - 1-3

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Substrate binding in the active site of cytochrome P450cam

Abstract

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