| Autor: |
Segall, M. D., Payne, M. C., Ellis, S. W., Tucker, G. T., Boyes, R. N. |
| Předmět: |
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| Zdroj: |
Xenobiotica; Jan1998, Vol. 28 Issue 1, p15-19, 5p |
| Abstrakt: |
1. We describe the application of novel ab initio quantum mechanical methods to the study of ligand interactions with cytochrome P450 (CYP101). cam 2. We find that our techniques accurately describe the transition from a low-spin state to a high-spin state of the haem Fe on binding of a substrate. Furthermore,our methods correctly predict that a large fraction of low-spin character is retained on binding of an inhibitor. 3. We demonstrate the use of ' computationalexperiments' to elucidate key features of the mechanism of interaction. This leads us to identify a new mechanism for the suppression of the low- to high-spin transition on binding of an inhibitor, namely the shortening of the bond between the Fe atom and the coordinated S atom of the cysteine axial ligand. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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