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Publication Detail
Electronic structure and dynamics of torsion-locked photoactive yellow protein chromophores
  • Publication Type:
    Journal article
  • Publication Sub Type:
  • Authors:
    Henley A, Diveky ME, Patel AM, Parkes MA, Anderson JC, Fielding HH
  • Publisher:
    Royal Society of Chemistry
  • Publication date:
  • Journal:
    Physical Chemistry Chemical Physics
  • Medium:
  • Status:
  • Print ISSN:
  • Language:
  • Addresses:
    Department of Chemistry, University College London, 20 Gordon Street, London WC1H 0AJ, UK. h.h.fielding@ucl.ac.uk.
The photocycle of photoactive yellow protein (PYP) begins with small-scale torsional motions of the chromophore leading to large-scale movements of the protein scaffold triggering a biological response. The role of single-bond torsional molecular motions of the chromophore in the initial steps of the PYP photocycle are not fully understood. Here, we employ anion photoelectron spectroscopy measurements and quantum chemistry calculations to investigate the electronic relaxation dynamics following photoexcitation of four model chromophores, para-coumaric acid, its methyl ester, and two analogues with aliphatic bridges hindering torsional motions around the single bonds adjacent to the alkene group. Following direct photoexcitation of S1 at 400 nm, we find that both single bond rotations play a role in steering the PYP chromophore through the S1/S0 conical intersection but that rotation around the single bond between the alkene moiety and the phenoxide group is particularly important. Following photoexcitation of higher lying electronic states in the range 346-310 nm, we find that rotation around the single bond between the alkene and phenoxide groups also plays a key role in the electronic relaxation from higher lying states to the S1 state. These results have potential applications in tuning the photoresponse of photoactive proteins and materials with chromophores based on PYP.
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