Abstract
Halorhodopsin is a light-driven inward Cl− pump found in the membrane of a halophilic archaeon called Halobacterium salinarum. While the physiological role of halorhodopsin has not been fully resolved, its functional mechanism has been studied as a model system for anion transport. Halorhodopsin has become widely used in optogenetics due to its light-induced neural-silencing ability. Here, we summarize the functional analyses of halorhodopsin since its discovery. Like other microbial rhodopsins, halorhodopsin contains all-trans retinal bound to a specific lysine residue through a protonated Schiff base. Proton-pumping rhodopsins utilize Asp residues as the counter-ions for the protonated Schiff bases. In halorhodopsin, this Asp residue is replaced by Thr, and Cl− becomes the counter-ion. Photoexcited halorhodopsin undergoes a photocycle including several intermediates where sequential Cl− movements occur. During the formation of the N-intermediate, Cl− moves from its original position to the cytoplasmic channel. During the subsequent N decay, the Cl− is released to the cytoplasmic medium. During the Cl− release, the dissociation constant of Cl− increases significantly compared with that at the dark state. Next, another Cl− is captured from the extracellular medium to complete the net Cl− translocation. This recapture process is not well defined.
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Kikukawa, T., Kamo, N., Demura, M. (2015). Photochemistry of Halorhodopsin. In: Yawo, H., Kandori, H., Koizumi, A. (eds) Optogenetics. Springer, Tokyo. https://doi.org/10.1007/978-4-431-55516-2_4
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DOI: https://doi.org/10.1007/978-4-431-55516-2_4
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