open access

https://hdl.handle.net/2115/33763

Interaction of the Halobacterial Transducer to a Halorhodopsin Mutant Engineered so as to Bind the Transducer : Cl- Circulation within the Extracellular Channel

英語

2007-03

Blackwell Publishing

Photochemistry and Photobiology

83(2)

293-302

An alkali-halophilic archaeum, Natronomonas pharaonis, contains two rhodopsins that are halorhodopsin (phR), a light-driven inward Cl- pump and phoborhodopsin (ppR), the receptor of negative phototaxis functioning by forming a signaling complexes with a transducer, pHtrII. Previously, we reported that the phR double mutant, P240T/F250YphR, can bind with pHtrII [Y. Sudo et al. (2006) J. Mol. Biol. 357, 1274-1282]. This mutant itself can transport Cl-, while the net transport was stopped upon formation of the complex. The flash photolysis data were analyzed by a scheme in which phR ⇒ P1 → P2 → P3 → P4 → phR. The P3 of the wild-type and the double mutant contained two components, X- and O-intermediates. After the complex formation, however, the P3 of the double mutant lacked the X-intermediate. These observations imply that the X-intermediate (probably the N-intermediate) is the state having Cl- in the cytoplasmic binding site and that the complex undergoes an extracellular Cl- circulation due to the inhibition of formation of the X-intermediate.

学術雑誌論文

Accepted Manuscript

Author Posting. © The Authors 2007 This is the author's version of the work. It is posted here for personal use, not for redistribution. The definitive version was published in Photochemistry and Photobiology, Volume 83, Issue 2, Page 293-302. http://dx.doi.org/10.1562/2006-06-09-RA-916

0031-8655

AA00773103