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

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

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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.

Item Type:

Journal Article (Original Article)

Division/Institute:

08 Faculty of Science > Departement of Chemistry and Biochemistry

UniBE Contributor:

Lochner, Martin

Subjects:

500 Science > 570 Life sciences; biology
500 Science > 540 Chemistry

ISSN:

1359-7345

Publisher:

Royal Society of Chemistry

Language:

English

Submitter:

Martin Lochner

Date Deposited:

19 Dec 2014 10:48

Last Modified:

19 Dec 2014 10:48

Publisher DOI:

10.1039/b302274a

BORIS DOI:

10.7892/boris.60961

URI:

https://boris.unibe.ch/id/eprint/60961

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