Structure and function of CYP108D1 fromNovosphingobium aromaticivoransDSM12444: an aromatic hydrocarbon-binding P450 enzyme-Reference-Cited by-同舟云学术

Structure and function of CYP108D1 fromNovosphingobium aromaticivoransDSM12444: an aromatic hydrocarbon-binding P450 enzyme

Published:2012-02-14 Issue:3 Volume:68 Page:277-291
ISSN:0907-4449
Container-title:Acta Crystallographica Section D Biological Crystallography
language:
Short-container-title:Acta Crystallogr D Biol Cryst

Author:

Bell Stephen G.,Yang Wen,Yorke Jake A.,Zhou Weihong,Wang Hui,Harmer Jeffrey,Copley Rachel,Zhang Aili,Zhou Ruimin,Bartlam Mark,Rao Zihe,Wong Luet-Lok

Publisher

International Union of Crystallography (IUCr)

Subject

General Medicine,Structural Biology

Link

http://journals.iucr.org/d/issues/2012/03/00/kw5040/kw5040.pdf

Reference83 articles.

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2. Engineering substrate recognition in catalysis by cytochrome P450cam

3. A cytochrome P450 class I electron transfer system from Novosphingobium aromaticivorans

4. Engineering the CYP101 system for in vivo oxidation of unnatural substrates

5. Bell, S. G., Hoskins, N., Whitehouse, C. J. C. & Wong, L.-L. (2007). The Ubiquitous Roles of Cytochrome P450 Proteins, edited by A. Sigel, H. Sigel & R. K. O. Sigel, pp. 437-476. New York: Wiley.

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