Spectral tuning of the photoactive yellow protein chromophore by H-bonding.
Spectral tuning in the photoactive yellow protein (PYP) is investigated by performing gas-phase absorption measurements on a PYP-model chromophore with two water molecules hydrogen-bonded to it. The photoabsorption maximum shows an unusually large blue shift of 0.71 eV in going from the bare to the hydrogen-bonded chromophore. It is concluded that several interactions within the PYP protein are mutually cancelling each other, yielding an absorption maximum that is close to the absorption maximum of the bare chromophore. The system breaks apart upon photoexcitation in the gas phase by releasing the two water molecules, leaving the chromophore itself intact. The hydrogen-bonding interactions thus play an important role in stabilizing the gas phase chromophore against photofragmentation. The relaxation dynamics for the breakup process was also studied, and the timescale of relaxation via fragmentation was found to be < 25 ns.
Department of Physics and Astronomy, Aarhus University, Aarhus, Denmark.
J
J
Rajput
D B
DB
Rahbek
G
G
Aravind
L H
LH
Andersen
D000042:Absorption; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D003373:Coumaric Acids / Q000737:chemistry; D004797:Enzyme-Linked Immunosorbent Assay / Q000295:instrumentation / Q000379:methods; D005740:Gases / Q000737:chemistry*; D006860:Hydrogen Bonding; D007700:Kinetics; D008027:Light; D008958:Models, Molecular; D020283:Photoreceptors, Microbial / Q000737:chemistry* / Q000235:genetics; D011422:Propionates; D013057:Spectrum Analysis / Q000295:instrumentation / Q000379:methods; D014867:Water / Q000737:chemistry
D001426:Bacterial Proteins; D003373:Coumaric Acids; D005740:Gases; D020283:Photoreceptors, Microbial; D011422:Propionates; C050162:photoactive yellow protein, Bacteria; D014867:Water; C495469:p-coumaric acid