title: Controlling radical formation in the photoactive yellow protein chromophore.
abstract: To understand how photoactive proteins function, it is necessary to understand the photoresponse of the chromophore. Photoactive yellow protein (PYP) is a prototypical signaling protein. Blue light triggers trans-cis isomerization of the chromophore covalently bound within PYP as the first step in a photocycle that results in the host bacterium moving away from potentially harmful light. At higher energies, photoabsorption has the potential to create radicals and free electrons; however, this process is largely unexplored. Here, we use photoelectron spectroscopy and quantum chemistry calculations to show that the molecular structure and conformation of the isolated PYP chromophore can be exploited to control the competition between trans-cis isomerization and radical formation. We also find evidence to suggest that one of the roles of the protein is to impede radical formation in PYP by preventing torsional motion in the electronic ground state of the chromophore.
authors.affiliation: Department of Chemistry, University College London, 20 Gordon Street, London WC1H 0AJ (UK).
authors.forename: Ciarán R S
authors.initials: CR
authors.lastname: Mooney
authors.forename: Michael A
authors.initials: MA
authors.lastname: Parkes
authors.forename: Andreas
authors.initials: A
authors.lastname: Iskra
authors.forename: Helen H
authors.initials: HH
authors.lastname: Fielding
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry*; D003373:Coumaric Acids / Q000138:chemical synthesis* / Q000737:chemistry; D005609:Free Radicals / Q000138:chemical synthesis / Q000737:chemistry; D020607:Halorhodospira halophila / Q000737:chemistry; D055668:Photochemical Processes; D011789:Quantum Theory; D013237:Stereoisomerism
chemical_list: D001426:Bacterial Proteins; D003373:Coumaric Acids; D005609:Free Radicals
keywords: biophysics; chromophores; photochemistry; proteins; radical formation