Issue 24, 1994
From the journal:

Journal of the Chemical Society, Chemical Communications

Cytochrome P-450cam monooxygenase can be redesigned to catalyse the regioselective aromatic hydroxylation of diphenylmethane

Stephen M. Fowler,   Paul A. England,   Andrew C. G. Westlake,   Duncan R. Rouch,   Darren P. Nickerson,   Caroline Blunt,   David Braybrook,   Susan West,   Luet-Lok Wong  and  Sabine L. Flitsch  

Abstract

A single-site mutant (Y96A) of the monooxygenase cytochrome P-450cam was found to bind diphenylmethane 5 and to catalyse its regioselective aromatic hydroxylation to p-hydroxydiphenylmethane 6.

About
Cited by
Related
Download options Please wait...

Article information

DOI
https://doi.org/10.1039/C39940002761
Article type
Paper

J. Chem. Soc., Chem. Commun., 1994, 2761-2762

Permissions

Request permissions

Cytochrome P-450cam monooxygenase can be redesigned to catalyse the regioselective aromatic hydroxylation of diphenylmethane

S. M. Fowler, P. A. England, A. C. G. Westlake, D. R. Rouch, D. P. Nickerson, C. Blunt, D. Braybrook, S. West, L. Wong and S. L. Flitsch, J. Chem. Soc., Chem. Commun., 1994, 2761 DOI: 10.1039/C39940002761

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Spotlight

Advertisements