Issue 12, 2003
From the journal:

Chemical Communications

The origin of the low-spin character of the resting state of cytochrome P450cam investigated by means of active site analogues

Martin Lochner,a   Markus Meuwlya  and  Wolf-D. Woggon*a  

* Corresponding authors

a Department of Chemistry, University of Basel, St. Johanns-Ring 19, 4056 Basel, Switzerland
E-mail: wolf-d.woggon@unibas.ch
Fax: +41 61 267 11 02
Tel: +41 61 267 11 02

Abstract

Crown-capped iron(S−) porphyrins 1·H2O and 2·H2O and their corresponding Ba2+ complexes have been prepared as active site analogues of the resting state of cytochrome P450cam. cw-EPR studies and electronic structure calculations at the density functional theory (DFT) level of model systems suggest a functional role of the water cluster of P450cam.

Graphical abstract: The origin of the low-spin character of the resting state of cytochrome P450cam investigated by means of active site analogues

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Article information

DOI
https://doi.org/10.1039/B302274A
Article type
Communication
Submitted
27 Feb 2003
Accepted
23 Apr 2003
First published
14 May 2003

Chem. Commun., 2003, 1330-1332

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The origin of the low-spin character of the resting state of cytochrome P450cam investigated by means of active site analogues

M. Lochner, M. Meuwly and Wolf-D. Woggon, Chem. Commun., 2003, 1330 DOI: 10.1039/B302274A

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