Please use this identifier to cite or link to this item:
|Scopus||Web of Science®||Altmetric|
|Title:||Structural analysis of CYP101C1 from Novosphingobium aromaticivorans DSM12444|
|Citation:||ChemBioChem, 2011; 12(1):88-99|
|Publisher:||Wiley-VCH Verlag GMBH|
|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|
|Appears in Collections:||Chemistry and Physics publications|
Files in This Item:
There are no files associated with this item.
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.