Ab initio excited-state dynamics of the photoactive yellow protein chromophore.
The photoisomerization mechanism of the neutral form of the photoactive yellow protein (PYP) chromophore is investigated using ab initio quantum chemistry and first-principles nonadiabatic molecular dynamics (ab initio multiple spawning or AIMS). We identify the nature of the two lowest-lying excited states, characterize the short-time behavior of molecules excited directly to S2, and explain the origin of the experimentally observed wavelength-dependent photoisomerization quantum yield.
Ko
Chaehyuk
C
Department of Chemistry and The Beckman Institute, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, USA.
Levine
Benjamin
B
Toniolo
A
A
Manohar
Leslie
L
Olsen
Seth
S
Werner
Hans-Joachim
HJ
Martínez
Todd J
TJ
D001426:Bacterial Proteins / Q000737:chemistry*; D003373:Coumaric Acids / Q000737:chemistry*; D007536:Isomerism; D010777:Photochemistry; D020283:Photoreceptors, Microbial / Q000737:chemistry*; D011422:Propionates; D011789:Quantum Theory; D013050:Spectrometry, Fluorescence
D001426:Bacterial Proteins; D003373:Coumaric Acids; D020283:Photoreceptors, Microbial; D011422:Propionates; C050162:photoactive yellow protein, Bacteria; C495469:p-coumaric acid