Retinal photoisomerization versus counterion protonation in light and dark-adapted bacteriorhodopsin and its primary photoproduct

Partha Malakar, Samira Gholami, Mohammad Aarabi, Ivan Rivalta, Mordechai Sheves (), Marco Garavelli () and Sanford Ruhman ()
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Partha Malakar: The Hebrew University of Jerusalem
Samira Gholami: Università di Bologna
Mohammad Aarabi: Università di Bologna
Ivan Rivalta: Università di Bologna
Mordechai Sheves: The Weizmann Institute of Science
Marco Garavelli: Università di Bologna
Sanford Ruhman: The Hebrew University of Jerusalem

Nature Communications, 2024, vol. 15, issue 1, 1-14

Abstract: Abstract Discovered over 50 years ago, bacteriorhodopsin is the first recognized and most widely studied microbial retinal protein. Serving as a light-activated proton pump, it represents the archetypal ion-pumping system. Here we compare the photochemical dynamics of bacteriorhodopsin light and dark-adapted forms with that of the first metastable photocycle intermediate known as “K”. We observe that following thermal double isomerization of retinal in the dark from bio-active all-trans 15-anti to 13-cis, 15-syn, photochemistry proceeds even faster than the ~0.5 ps decay of the former, exhibiting ballistic wave packet curve crossing to the ground state. In contrast, photoexcitation of K containing a 13-cis, 15-anti chromophore leads to markedly multi-exponential excited state decay including much slower stages. QM/MM calculations, aimed to interpret these results, highlight the crucial role of protonation, showing that the classic quadrupole counterion model poorly reproduces spectral data and dynamics. Single protonation of ASP212 rectifies discrepancies and predicts triple ground state structural heterogeneity aligning with experimental observations. These findings prompt a reevaluation of counter ion protonation in bacteriorhodopsin and contribute to the broader understanding of its photochemical dynamics.

Date: 2024
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DOI: 10.1038/s41467-024-46061-w

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