Insight into the isomerization mechanism of retinal proteins from hybrid quantum mechanics/molecular mechanics simulations

Saumik Sen, Rajiv K. Kar, Veniamin A. Borin, Igor Schapiro*

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

9 Scopus citations


The photoisomerization of retinal is a unifying primary event in the rhodopsin protein family. In vertebrate rhodopsins it is the first step in the vision process, while in the microbial rhodopsins it activates the transport of ions across the cell-membrane. This reaction is highly optimized in the protein, which is ultrafast, selective, and efficient. A great effort was directed to elucidate the mechanism due to the overall complexity of the process inside the protein. The classical one-bond-flip is too demanding in space for the confined protein cavity. Therefore, various space saving mechanisms based on the rotation of multiple double bonds have been proposed. The hybrid quantum mechanics/molecular mechanics (QM/MM) method played an important role in the elucidation of the mechanism inside the tight protein environment. It allows to take the entire protein into account while describing the ground and excited states of retinal. The predicted mechanisms include full isomerization of two or three double bonds, a simultaneous isomerization of a single and a double bond as well as the partial rotation of bonds adjacent to the central isomerization. This review summarizes mechanistic studies in the literature and compares them. This article is categorized under: Structure and Mechanism > Computational Biochemistry and Biophysics Electronic Structure Theory > Combined QM/MM Methods Software > Molecular Modeling.

Original languageAmerican English
Article numbere1562
JournalWiley Interdisciplinary Reviews: Computational Molecular Science
Issue number1
StatePublished - 1 Jan 2022

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