Biotechnology Letters

, Volume 34, Issue 2, pp 239–245

Photosystem I from plants as a bacterial cytochrome P450 surrogate electron donor: terminal hydroxylation of branched hydrocarbon chains

  • Kenneth Jensen
  • Jonathan B. Johnston
  • Paul R. Ortiz de Montellano
  • Birger Lindberg Møller
Original Research Paper

DOI: 10.1007/s10529-011-0768-4

Cite this article as:
Jensen, K., Johnston, J.B., de Montellano, P.R.O. et al. Biotechnol Lett (2012) 34: 239. doi:10.1007/s10529-011-0768-4

Abstract

The ability of cytochrome P450 enzymes to catalyze highly regio- and stereospecific hydroxylations makes them attractive alternatives to approaches based on chemical synthesis but they require expensive cofactors, e.g. NAD(P)H, which limits their commercial potential. Ferredoxin (Fdx) is a multifunctional electron carrier that in plants accepts electrons from photosystem I (PSI) and facilitates photoreduction of NADP+ to NADPH mediated by ferredoxin-NAD(P)H oxidoreductase (FdR). In bacteria, the electron flow is reversed and Fdx accepts electrons from NADPH via FdR and serves as the direct electron donor to bacterial P450s. By combining the two systems, we demonstrate that irradiation of PSI can drive the activity of a bacterial P450, CYP124 from Mycobacterium tuberculosis. The substitution of the costly cofactor NADPH with sunlight illustrates the potential of the light-driven hydroxylation system for biotechnology applications.

Keywords

Cytochrome P450ω-hydroxylationLight-driven biosynthesisLipid hydroxyllasePhotosystem I

Copyright information

© Springer Science+Business Media B.V. 2011

Authors and Affiliations

  • Kenneth Jensen
    • 1
  • Jonathan B. Johnston
    • 2
  • Paul R. Ortiz de Montellano
    • 2
  • Birger Lindberg Møller
    • 1
  1. 1.Plant Biochemistry Laboratory, Department of Plant Biology and BiotechnologyUniversity of CopenhagenCopenhagen, Frederiksberg CDenmark
  2. 2.Department of Pharmaceutical ChemistryUniversity of California San FranciscoSan FranciscoUSA