The Impact of Retinal Configuration on the Protein–Chromophore Interactions in Bistable Jumping Spider Rhodopsin-1
1
Fritz Haber Center for Molecular Dynamics Research, Institute of Chemistry, The Hebrew University of Jerusalem, Jerusalem 9190401, Israel
2
DTU Chemistry, Technical University of Denmark, DK-2800 Kongens Lyngby, Denmark
*
Author to whom correspondence should be addressed.
Academic Editors: Juan J. Nogueira, Lara Martínez and Javier Segarra
Molecules 2022, 27(1), 71; https://doi.org/10.3390/molecules27010071
Received: 14 November 2021
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Revised: 15 December 2021
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Accepted: 17 December 2021
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Published: 23 December 2021
(This article belongs to the Special Issue Photophysics and Photochemistry in Complex Molecular Systems)
Bistable rhodopsins have two stable forms that can be interconverted by light. Due to their ability to act as photoswitches, these proteins are considered as ideal candidates for applications such as optogenetics. In this work, we analyze a recently crystalized bistable rhodopsin, namely the jumping spider rhodopsin-1 (JSR1). This rhodopsin exhibits identical absorption maxima for the parent and the photoproduct form, which impedes its broad application. We performed hybrid QM/MM simulations to study three isomers of the retinal chromophore: the 9-cis, 11-cis and all-trans configurations. The main aim was to gain insight into the specific interactions of each isomer and their impact on the absorption maximum in JSR1. The absorption spectra were computed using sampled snapshots from QM/MM molecular dynamics trajectories and compared to their experimental counterparts. The chromophore–protein interactions were analyzed by visualizing the electrostatic potential of the protein and projecting it onto the chromophore. It was found that the distance between a nearby tyrosine (Y126) residue plays a larger role in the predicted absorption maximum than the primary counterion (E194). Geometric differences between the isomers were also noted, including a structural change in the polyene chain of the chromophore, as well as changes in the nearby hydrogen bonding network.
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Keywords:
rhodopsins; bistable; jumping spider; QM/MM; spectral tuning
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MDPI and ACS Style
Church, J.R.; Olsen, J.M.H.; Schapiro, I. The Impact of Retinal Configuration on the Protein–Chromophore Interactions in Bistable Jumping Spider Rhodopsin-1. Molecules 2022, 27, 71. https://doi.org/10.3390/molecules27010071
AMA Style
Church JR, Olsen JMH, Schapiro I. The Impact of Retinal Configuration on the Protein–Chromophore Interactions in Bistable Jumping Spider Rhodopsin-1. Molecules. 2022; 27(1):71. https://doi.org/10.3390/molecules27010071
Chicago/Turabian StyleChurch, Jonathan R., Jógvan M.H. Olsen, and Igor Schapiro. 2022. "The Impact of Retinal Configuration on the Protein–Chromophore Interactions in Bistable Jumping Spider Rhodopsin-1" Molecules 27, no. 1: 71. https://doi.org/10.3390/molecules27010071
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