Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/75494
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Type: Journal article
Title: Structural analysis of CYP101C1 from Novosphingobium aromaticivorans DSM12444
Author: Ma, M.
Bell, S.
Yang, W.
Hao, Y.
Rees, N.
Bartlam, M.
Zhou, W.
Wong, L.
Rao, Z.
Citation: ChemBioChem, 2011; 12(1):88-99
Publisher: Wiley-VCH Verlag GMBH
Issue Date: 2011
ISSN: 1439-4227
1439-7633
Statement of
Responsibility: 
Ming Ma, Stephen G. Bell, Wen Yang, Yiming Hao, Nicholas H. Rees, Mark Bartlam, Weihong Zhou, Luet-Lok Wong, and Zihe Rao
Abstract: CYP101C1 from Novosphingobium aromaticivorans DSM12444 is a homologue of CYP101D1 and CYP101D2 enzymes from the same bacterium and CYP101A1 from Pseudomonas putida. CYP101C1 does not bind camphor but is capable of binding and hydroxylating ionone derivatives including α- and β-ionone and β-damascone. The activity of CYP101C1 was highest with β-damascone (kcat=86 s⁻¹) but α-ionone oxidation was the most regioselective (98 % at C3). The crystal structures of hexane-2,5-diol- and β-ionone-bound CYP101C1 have been solved; both have open conformations and the hexanediol-bound form has a clear access channel from the heme to the bulk solvent. The entrance of this channel is blocked when β-ionone binds to the enzyme. The heme moiety of CYP101C1 is in a significantly different environment compared to the other structurally characterised CYP101 enzymes. The likely ferredoxin binding site on the proximal face of CYP101C1 has a different topology but a similar overall positive charge compared to CYP101D1 and CYP101D2, all of which accept electrons from the ArR/Arx class I electron transfer system.
Keywords: biocatalysis; C[BOND]H activation; crystal structure; cytochrome P450; heme proteins
Rights: © 2011 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim
RMID: 0020121235
DOI: 10.1002/cbic.201000537
Appears in Collections:Chemistry and Physics publications

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