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


Autoria(s): Lochner, Martin; Meuwly, Markus; Woggon, Wolf-D.
Data(s)

2003

Resumo

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.

Formato

application/pdf

Identificador

http://boris.unibe.ch/60961/1/ChemComm2003.pdf

Lochner, Martin; Meuwly, Markus; Woggon, Wolf-D. (2003). The origin of the low-spin character of the resting state of cytochrome P450cam investigated by means of active site analogues. Chemical communications, 2003(12), pp. 1330-1332. Royal Society of Chemistry 10.1039/b302274a <http://dx.doi.org/10.1039/b302274a>

doi:10.7892/boris.60961

info:doi:10.1039/b302274a

urn:issn:1359-7345

Idioma(s)

eng

Publicador

Royal Society of Chemistry

Relação

http://boris.unibe.ch/60961/

Direitos

info:eu-repo/semantics/restrictedAccess

Fonte

Lochner, Martin; Meuwly, Markus; Woggon, Wolf-D. (2003). The origin of the low-spin character of the resting state of cytochrome P450cam investigated by means of active site analogues. Chemical communications, 2003(12), pp. 1330-1332. Royal Society of Chemistry 10.1039/b302274a <http://dx.doi.org/10.1039/b302274a>

Palavras-Chave #570 Life sciences; biology #540 Chemistry
Tipo

info:eu-repo/semantics/article

info:eu-repo/semantics/publishedVersion

PeerReviewed