BibTex format
@article{Polli:2014:10.1002/anie.201309867,
author = {Polli, D and Weingart, O and Brida, D and Poli, E and Maiuri, M and Spillane, KM and Bottoni, A and Kukura, P and Mathies, RA and Cerullo, G and Garavelli, M},
doi = {10.1002/anie.201309867},
journal = {Angew Chem Int Ed Engl},
pages = {2504--2507},
title = {Wavepacket splitting and two-pathway deactivation in the photoexcited visual pigment isorhodopsin.},
url = {http://dx.doi.org/10.1002/anie.201309867},
volume = {53},
year = {2014}
}
RIS format (EndNote, RefMan)
TY - JOUR
AB - Isorhodopsin is the visual pigment analogue of rhodopsin. It shares the same opsin environment but it embeds 9-cis retinal instead of 11-cis. Its photoisomerization is three times slower and less effective. The mechanistic rationale behind this observation is revealed by combining high-level quantum-mechanical/molecular-mechanical simulations with ultrafast optical spectroscopy with sub-20fs time resolution and spectral coverage extended to the near-infrared. Whereas in rhodopsin the photoexcited wavepacket has ballistic motion through a single conical intersection seam region between the ground and excited states, in isorhodopsin it branches into two competitive deactivation pathways involving distinct conical intersection funnels. One is rapidly accessed but unreactive. The other is slower, as it features extended steric interactions with the environment, but it is productive as it follows forward bicycle pedal motion.
AU - Polli,D
AU - Weingart,O
AU - Brida,D
AU - Poli,E
AU - Maiuri,M
AU - Spillane,KM
AU - Bottoni,A
AU - Kukura,P
AU - Mathies,RA
AU - Cerullo,G
AU - Garavelli,M
DO - 10.1002/anie.201309867
EP - 2507
PY - 2014///
SP - 2504
TI - Wavepacket splitting and two-pathway deactivation in the photoexcited visual pigment isorhodopsin.
T2 - Angew Chem Int Ed Engl
UR - http://dx.doi.org/10.1002/anie.201309867
UR - https://www.ncbi.nlm.nih.gov/pubmed/24481600
VL - 53
ER -