Spectroscopic and photochemical analysis of proteorhodopsin variants from the surface of the Arctic Ocean

  • Jung, Jae Yong
  • Choi, Ah Reum
  • Lee, Yoo Kyung
  • Lee, Hong Kum
  • Jung, Kwang-Hwan
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21

초록

Proteorhodopsin (PR), a retinal-containing seven transmembrane helix protein, functions as a light-driven proton pump. Using PCR, we isolated 18 PR variants originating from the surface of the Arctic Ocean. Their absorption maxima were between 517 and 546 nm at pH 7. One of the isolates turned out to be identical to GPR (green light-absorbing proteorhodopsin) from Monterey Bay. Interestingly, 10 isolates had replaced a tyrosine in the retinal-binding site (Tyr200 in GPR) with Asn. They showed a slower photocycle, more blue-shifted absorption maxima at pH 10, and relatively larger Delta H and Delta S of activation of the transition between the O intermediate and the ground state compared to GPR. (C) 2008 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

키워드

proteorhodopsinretinal binding sitephotocycling rateY200N variantsbiofilmANABAENA SENSORY RHODOPSINBACTERIORHODOPSINSUBSTITUTIONPHOTOTROPHY
제목
Spectroscopic and photochemical analysis of proteorhodopsin variants from the surface of the Arctic Ocean
저자
Jung, Jae YongChoi, Ah ReumLee, Yoo KyungLee, Hong KumJung, Kwang-Hwan
DOI
10.1016/j.febslet.2008.04.025
발행일
2008-05-28
유형
Article
저널명
FEBS Letters
582
12
페이지
1679 ~ 1684