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Hydrogen-Bonding Interaction Regulates Photoisomerization of a Single-Bond-Rotation Locked Photoactive Yellow Protein Chromophore in Protein
journal contribution
posted on 2020-03-13, 18:44 authored by Teng-Shuo Zhang, Ye-Guang Fang, Xiu-Fang Song, Wei-Hai Fang, Ganglong CuiWe
have employed the QM(CASPT2//CASSCF)/MM method to explore the
excited-state isomerization and decay mechanism of a single-bond-rotation
locked photoactive yellow protein (PYP) chromophore in wild-type and
mutant proteins. The S1 state is a spectroscopically bright
state in the Franck–Condon region. In this state, there exist
two excited-state isomerization pathways separately related to the
clockwise and anticlockwise rotations of the C=C bond. The clockwise
path is favorable because of a small barrier of 2 kcal/mol and uses
a novel bicycle-pedal unidirectional photoisomerization mechanism
in which the involved two dihedral angles rotate asynchronously because
of the reinforced hydrogen-bonding interaction between the chromophore
and Cys69. Near the twisted S1 minimum, the chromophore
hops to the S0 state via the S1/S0 conical intersection. Finally, the R52A mutation has small effects
on the excited-state properties and photoisomerization of the locked
PYP chromophore. The present work provides new insights for understanding
the photochemistry of PYP chromophores in protein surroundings.
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S 1 statePhotoactive Yellow Protein ChromophorePYP chromophoresR 52A mutationanticlockwise rotationsphotoisomerization mechanismHydrogen-Bonding Interaction Regulates Photoisomerizationdecay mechanismexcited-state isomerizationhydrogen-bonding interactionprotein surroundingsdihedral anglesexcited-state propertiesexcited-state isomerization pathwaysCys 69.novel bicycle-pedalS 1PYP chromophoreS 0 stateQM
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