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Structural Analysis of CYP101C1 from Novosphingobium aromaticivorans DSM12444.

Chembiochem : a European journal of chemical biology (2010-12-15)
Ming Ma, Stephen G Bell, Wen Yang, Yiming Hao, Nicholas H Rees, Mark Bartlam, Weihong Zhou, Luet-Lok Wong, 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 (k(cat)=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.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
β-Ionone, 96%
Sigma-Aldrich
β-Ionone, predominantly trans, ≥97%, FCC, FG
Sigma-Aldrich
β-Ionone, natural, ≥95%, FG

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