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논문 기본 정보

자료유형
학술저널
저자정보
Kim, Se Hwan (Dept. of Life Science and Institute of Biological Interfaces, Sogang University) Cho, Jang-Cheon (Dept. of Biological Sciences, Inha University) Jung, Kwang-Hwan (Dept. of Life Science and Institute of Biological Interfaces, Sogang University)
저널정보
한국광과학회 Rapid communication in photoscience : RCP Rapid communication in photoscience : RCP 제2권 제2호
발행연도
2013.1
수록면
60 - 63 (4page)

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Rhodopsins belong to a family of membrane-embedded photoactive retinylidene proteins. One opsin gene was isolated from ${\beta}$-proteobacterium (IMCC9480) which had been collected at the North Pole. It is very similar to Xanthorhodopin (XR) of HTCC2181. In this study, we carried out basic characterization of the rhodopsin. It has ${\lambda}max$ of 536, 554, and 546 nm at pH 4.0, 7.0, and 10.0, respectively. Since the pKa of its proton acceptor is around 6.27, we measured its proton pumping activity and photocycling rate at pH 8.0. It has a typical proton acceptor (D99) and donor (E110) which mediate proton translocation from intracellular to extracellular region when deduced from the sequence alignments. On the basis of in vitro proton pumping activity, it was proposed to have fast photocycling rate with M and O intermediates, indicating that it is a typical ion-pumping rhodopsin. Since the XR has not yet been expressed in any other heterologous expression system, we tried to get much more information about the XR through the XR-homologue rhodopsin.

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