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Mastigocladopsis repens Rhodopsin (MastR), the newest member of a family of retinal-binding anionic transmembrane pumps, can trap light energy to allow inward chloride transport across a cellular membrane. The pumping action is driven by retinal isomerization, which is thermodynamically unfavorable in the ground state but occurs at a higher rate under photo-excitation in the host protein environment. Particularly interesting is MastR’s conversion to an outward proton pump (MastR-T74D) due to single-point mutation of an amino acid located close to the retinal chromophore. Although flash photolysis studies have characterized the MastR/MastR-T74D photocycle on a microsecond timescale, its ultrafast dynamics involving retinal isomerization have not yet been investigated. We performed ultrafast transient absorption studies on MastR and MastR-T74D to look at the femtosecond to picosecond dynamics that lead to retinal isomerization and compared them to the well-studied ultrafast dynamics of bacteriorhodopsin.
(2024) Published by SPIE. Downloading of the abstract is permitted for personal use only.
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Harmanjot S. Grewal, Jessica Besaw, Soumyajit Mitra, Manoel L. da Silva-Neto, R. J. D. Miller, "Ultrafast studies on a cyanobacterial chloride pump and its proton pumping mutant," Proc. SPIE 12875, Frontiers in Ultrafast Optics: Biomedical, Scientific, and Industrial Applications XXIV, 128750I (12 March 2024); https://doi.org/10.1117/12.3001901