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dc.contributor.authorMa, M.en
dc.contributor.authorBell, S.en
dc.contributor.authorYang, W.en
dc.contributor.authorHao, Y.en
dc.contributor.authorRees, N.en
dc.contributor.authorBartlam, M.en
dc.contributor.authorZhou, W.en
dc.contributor.authorWong, L.en
dc.contributor.authorRao, Z.en
dc.identifier.citationChemBioChem, 2011; 12(1):88-99en
dc.description.abstractCYP101C1 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.en
dc.description.statementofresponsibilityMing Ma, Stephen G. Bell, Wen Yang, Yiming Hao, Nicholas H. Rees, Mark Bartlam, Weihong Zhou, Luet-Lok Wong, and Zihe Raoen
dc.publisherWiley-VCH Verlag GMBHen
dc.rights© 2011 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheimen
dc.subjectbiocatalysis; C[BOND]H activation; crystal structure; cytochrome P450; heme proteinsen
dc.titleStructural analysis of CYP101C1 from Novosphingobium aromaticivorans DSM12444en
dc.typeJournal articleen
pubs.library.collectionChemistry and Physics publicationsen
dc.identifier.orcidBell, S. [0000-0002-7457-9727]en
Appears in Collections:Chemistry and Physics publications

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