Cytochrome P450cin (CYP176A1)

  • Jeanette E. Stok
  • Kate E. Slessor
  • Anthony J. Farlow
  • David B. Hawkes
  • James J. De VossEmail author
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 851)


Cytochrome P450cin (P450cin) (CYP176A1) is a bacterial P450 enzyme that catalyses the enantiospecific hydroxylation of 1,8-cineole to (1R)-6β-hydroxycineole when reconstituted with its natural reduction-oxidation (redox) partner cindoxin, E. coli flavodoxin reductase, and NADPH as a source of electrons. This catalytic system has become a useful tool in the study of P450s as not only can large quantities of P450cin be prepared and rates of oxidation up to 1,500 min−1 achieved, but it also displays a number of unusual characteristics. These include an asparagine residue in P450cin that has been found in place of the usual conserved threonine residue observed in most P450s. In general, this conserved threonine controls oxygen activation to create the potent ferryl (Fe(IV=O) porphyrin cation radical required for substrate oxidation. Another atypical characteristic of P450cin is that it utilises an FMN-containing redoxin (cindoxin) rather than a ferridoxin as is usually observed with other bacterial P450s (e.g. P450cam). This chapter will review what is currently known about P450cin and how this enzyme has provided a greater understanding of P450s in general.


Cytochrome P450cin CYP176A1 Cindoxin Cindoxin reductase Ferric hydroperoxy species Ferryl porphyrin radical species 



The authors would like to acknowledge that this work was supported in part by ARC Grants DP110104455 and DP140103229.


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Copyright information

© Springer International Publishing Switzerland 2015

Authors and Affiliations

  • Jeanette E. Stok
    • 1
  • Kate E. Slessor
    • 1
  • Anthony J. Farlow
    • 1
  • David B. Hawkes
    • 1
  • James J. De Voss
    • 1
    Email author
  1. 1.School of Chemistry and Molecular BiosciencesUniversity of QueenslandBrisbaneAustralia

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