open access

https://hdl.handle.net/2115/60922

Characterization of a Cyanobacterial Chloride-pumping Rhodopsin and Its Conversion into a Proton Pump

英語

retinal proteins

2016-01-01

American Society for Biochemistry and Molecular Biology (ASBMB)

Journal of biological chemistry

291(1)

355-362

Light-driven ion-pumping rhodopsins are widely distributed in microorganisms and are now classified into the categories of outward H+ and Na+ pumps and an inward Cl- pump. These different types share a common protein architecture and utilize the photoisomerization of the same chromophore, retinal, to evoke photoreactions. Despite these similarities, successful pump-to-pump conversion had been confined to only the H+ pump bacteriorhodopsin, which was converted to a Cl- pump in 1995 by a single amino acid replacement. In this study we report the first success of the reverse conversion from a Cl- pump to a H+ pump. A novel microbial rhodopsin (MrHR) from the cyanobacterium Mastigocladopsis repens functions as a Cl- pump and belongs to a cluster that is far distant from the known Cl- pumps. With a single amino acid replacement, MrHR is converted to a H+ pump in which dissociable residues function almost completely in the H+ relay reactions. MrHR most likely evolved from a H+ pump, but it has not yet been highly optimized into a mature Cl- pump.

学術雑誌論文

Accepted Manuscript

This research was originally published in Journal of Biological Chemistry. Takatoshi Hasemi, Takashi Kikukawa1, Naoki Kamo and Makoto Demura. Characterization of a Cyanobacterial Chloride-pumping Rhodopsin and Its Conversion into a Proton Pump. 2016; 291(1):355-362. © the American Society for Biochemistry and Molecular Biology.

0021-9258

1083-351X