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Structural Analysis of CYP101C1 from Novosphingobium aromaticivorans DSM12444
Author(s) -
Ma Ming,
Bell Stephen G.,
Yang Wen,
Hao Yiming,
Rees Nicholas H.,
Bartlam Mark,
Zhou Weihong,
Wong LuetLok,
Rao Zihe
Publication year - 2011
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201000537
Subject(s) - ferredoxin , chemistry , stereochemistry , moiety , heme , pseudomonas putida , enzyme , biochemistry
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.