Molecules and Cells

  • 제46권8호
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  • Pages.513-525
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  • 2023
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  • 1016-8478(pISSN)
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  • 0219-1032(eISSN)
한국분자세포생물학회 (Korean Society for Molecular and Cellular Biology)
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Color-Tuning Mechanism of the Lit Form of Orange Carotenoid Protein

  • Man-Hyuk Han (Department of Physics, Korea Advanced Institute of Science and Technology (KAIST)) ;
  • Hee Wook Yang (Department of Biological Sciences, Chungnam National University) ;
  • Jungmin Yoon (Department of Biological Sciences, KI for the BioCentury, KAIST) ;
  • Yvette Villafani (Department of Biological Sciences, Chungnam National University) ;
  • Ji-Young Song (Department of Biological Sciences, Chungnam National University) ;
  • Cheol Ho Pan (Natural Product Informatics Research Center, KIST Gangneung Institute of Natural Products) ;
  • Keunwan Park (Natural Product Informatics Research Center, KIST Gangneung Institute of Natural Products) ;
  • Youngmoon Cho (Department of Physics, Korea Advanced Institute of Science and Technology (KAIST)) ;
  • Ji-Joon Song (Department of Biological Sciences, KI for the BioCentury, KAIST) ;
  • Seung Joong Kim (Department of Physics, Korea Advanced Institute of Science and Technology (KAIST)) ;
  • Youn-Il Park (Department of Biological Sciences, Chungnam National University) ;
  • Jiyong Park (Center for Catalytic Hydrocarbon Functionalizations, Institute for Basic Science (IBS))
  • 투고 : 2022.11.30
  • 심사 : 2023.07.13
  • 발행 : 2023.08.31
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초록

Orange carotenoid protein (OCP) of photosynthetic cyanobacteria binds to ketocarotenoids noncovalently and absorbs excess light to protect the host organism from light-induced oxidative damage. Herein, we found that mutating valine 40 in the α3 helix of Gloeocapsa sp. PCC 7513 (GlOCP1) resulted in blue- or red-shifts of 6-20 nm in the absorption maxima of the lit forms. We analyzed the origins of absorption maxima shifts by integrating X-ray crystallography, homology modeling, molecular dynamics simulations, and hybrid quantum mechanics/molecular mechanics calculations. Our analysis suggested that the single residue mutations alter the polar environment surrounding the bound canthaxanthin, thereby modulating the degree of charge transfer in the photoexcited state of the chromophore. Our integrated investigations reveal the mechanism of color adaptation specific to OCPs and suggest a design principle for color-specific photoswitches.

키워드

과제정보

This work was supported by grants from the KIST Open Research Program (2E30642-20-152) and the KRIBB Research Initiative Program (KGM1002311) in Korea to Y.I.P.; the Institute for Basic Science (IBS-R010-A1) in Korea to J.P.; the KAIST Grand Challenge 30 project (KC30) to J.J.S.; the National Research Foundation of Korea (NRF-2020R1A2B5B03001517) to J.J.S.; KC30 (N11200138) to M.H.H.; and the Korea Advanced Institute of Science and Technology (KAIST; G04180038), the National Research Foundation of Korea (NRF; 2020R1A2C1013246, 2020K1A3A7A09080399, and 2020R1A4A3079755), and the Basic Science Research Program through NRF (2019R1A6A1A10073887) to S.J.K.

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