Characterization of the primary photochemistry of proteorhodopsin with femtosecond spectroscopy

A. Rupenyan; I.H.M. van Stokkum; R. van Grondelle; J.C. Arents; K.J. Hellingwerf; M.L. Groot

doi:10.1529/biophysj.107.121376

Characterization of the primary photochemistry of proteorhodopsin with femtosecond spectroscopy

A. Rupenyan, I.H.M. van Stokkum, R. van Grondelle, J.C. Arents, K.J. Hellingwerf, M.L. Groot

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Abstract

Proteorhodopsin is an ion-translocating member of the microbial rhodopsin family. Light absorption by its retinal chromophore initiates a photocycle, driven by trans/cis isomerization, leading to transmembrane translocation of a proton toward the extracellular side of the cytoplasmic membrane. Here we report a study on the photoisomerization dynamics of the retinal chromophore of proteorhodopsin, using femtosecond time-resolved spectroscopy, by probing in the visible- and in the midinfrared spectral regions. Experiments were performed both at pH 9.5 (a physiologically relevant pH value in which the primary proton acceptor of the protonated Schiff base, Asp

Original language	English
Pages (from-to)	4020-4030
Journal	Biophysical Journal
Volume	94
Issue number	10
DOIs	https://doi.org/10.1529/biophysj.107.121376
Publication status	Published - 2008

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Characterization of the primary photochemistry of proteorhodopsin with femtosecond spectroscopy

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10.1529/biophysj.107.121376

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AU - Arents, J.C.

AU - Hellingwerf, K.J.

AU - Groot, M.L.

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Characterization of the primary photochemistry of proteorhodopsin with femtosecond spectroscopy

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