Download MendeleyStructural Analysis of CYP101C1 from Novosphingobium aromaticivorans DSM12444.
Ma, M., Bell, S.G., Yang, W., Hao, Y., Rees, N.H., Bartlam, M., Zhou, W., Wong, L.L., Rao, Z.(2011) Chembiochem 12: 88-99
- PubMed: 21154803
- DOI: https://doi.org/10.1002/cbic.201000537
- Primary Citation of Related Structures:
3OFT, 3OFU - PubMed 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.
Organizational Affiliation:
National Laboratory of Macromolecules, Institute of Biophysics, Chinese Academy of Science, Beijing 100101, China.
