Theory and Simulation of the Ultrafast Double-Bond Isomerization of Biological Chromophores

Samer Gozem, Hoi Ling Luk, Igor Schapiro, Massimo Olivucci*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

191 Scopus citations


Ultrafast processes in light-absorbing proteins have been implicated in the primary step in the light-to-energy conversion and the initialization of photoresponsive biological functions. Theory and computations have played an instrumental role in understanding the molecular mechanism of such processes, as they provide a molecular-level insight of structural and electronic changes at ultrafast time scales that often are very difficult or impossible to obtain from experiments alone. Among theoretical strategies, the application of hybrid quantum mechanics and molecular mechanics (QM/MM) models is an important approach that has reached an evident degree of maturity, resulting in several important contributions to the field. This review presents an overview of state-of-the-art computational studies on subnanosecond events in rhodopsins, photoactive yellow proteins, phytochromes, and some other photoresponsive proteins where photoinduced double-bond isomerization occurs. The review also discusses current limitations that need to be solved in future developments.

Original languageAmerican English
Pages (from-to)13502-13565
Number of pages64
JournalChemical Reviews
Issue number22
StatePublished - 22 Nov 2017

Bibliographical note

Publisher Copyright:
© 2017 American Chemical Society.


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