Photochemistry of pharaonis phoborhodopsin and its interaction with the transducer

Kamo, Naoki; Shimono, Kazumi; Iwamoto, Masayuki; Sudo, Yuki; Yoshida, Hideaki

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자료유형: 학술저널

저자정보: Kamo, Naoki (Laboratory of Biophysical Chemistry, Graduate School of Pharmaceutical Sciences, Hokkaido University) Shimono, Kazumi (Laboratory of Biophysical Chemistry, Graduate School of Pharmaceutical Sciences, Hokkaido University) Iwamoto, Masayuki (Laboratory of Biophysical Chemistry, Graduate School of Pharmaceutical Sciences, Hokkaido University) Sudo, Yuki (Laboratory of Biophysical Chemistry, Graduate School of Pharmaceutical Sciences, Hokkaido University) Yoshida, Hideaki (Laboratory of Biophysical Chemistry, Graduate School of Pharmaceutical Sciences, Hokkaido University)

저널정보: 한국광과학회 Journal of photoscience : an international journal officail organ of the korean society of photoscience Journal of photoscience : an international journal officail organ of the korean society of photoscience 제9권 제2호

발행연도: 2002.1

수록면: 102 - 105 (4page)

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Phoborhodopsin (pR or sensory rhodopsin II, sRII; the absorption maximum of ∼ 500 nm) is a retinoid protein and works as a photoreceptor of the negative phototaxis of Halobacterium salinarum. pharaonis phoborhodopsin (ppR or pharaonis sensory rhodopsin II, psRII) is a corresponding protein of Natronobacterium pharaonis. These sensory proteins form a complex with a cognate transducer protein in the membrane, and this complex transmits the light-signal to the cytoplasm to evoke avoidance reaction from blue-green light. Recently, the functional expression in Escherichia coli membrane of ppR was achieved, which can afford a large amount of the protein and enables mutant studies to clarify the role of various amino acid residues. A truncated transducer which can bind to ppR is also expressed in Escherichia. coli membrane. In this article, we will review properties of ppR mainly using observations of our laboratory; which contains photochemistry (photocycle), light-driven proton uptake, release and transport, F -helix titling during photocycle and association of the transducer.

#Photocycle #Proton transport #Flash photolysis #Sn0 $_2$ electrode #Helix tilting, Photo-taxis

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