Structural Analysis of CYP101C1 from Novosphingobium aromaticivorans DSM12444.

Journal article

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.

Authors: Ma, M; Bell, S; Yang, W; Hao, Y; Rees, N

• Publication status: Published
• Journal: Chembiochem : a European journal of chemical biology
• Volume: 12
• Issue: 1
• Pages: 88-99
• Publication date: 2011-01-01
• DOI: 10.1002/cbic.201000537
• EISSN: 1439-7633
• ISSN: 1439-4227
• Language: English
• Keywords: Camphor 5-Monooxygenase; Kinetics; Sphingomonadaceae; Heme; Substrate Specificity; Norisoprenoids; Models, Molecular; Catalytic Domain