Spectral changes of light-harvesting complex 2 lacking B800 bacteriochlorophyll a under neutral pH conditions.
Autor: | Kawato S; Faculty of Science and Engineering, Kindai University, Higashi-Osaka, Osaka, 577-8502, Japan., Sato S; Faculty of Science and Engineering, Kindai University, Higashi-Osaka, Osaka, 577-8502, Japan., Kitoh-Nishioka H; Faculty of Science and Engineering, Kindai University, Higashi-Osaka, Osaka, 577-8502, Japan., Saga Y; Faculty of Science and Engineering, Kindai University, Higashi-Osaka, Osaka, 577-8502, Japan. saga@chem.kindai.ac.jp. |
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Jazyk: | angličtina |
Zdroj: | Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology [Photochem Photobiol Sci] 2024 May; Vol. 23 (5), pp. 871-879. Date of Electronic Publication: 2024 Apr 02. |
DOI: | 10.1007/s43630-024-00560-3 |
Abstrakt: | Exchange of B800 bacteriochlorophyll (BChl) a in light-harvesting complex 2 (LH2) is promising for a better understanding of the mechanism on intracomplex excitation energy transfer of this protein. Structural and spectroscopic properties of LH2 lacking B800 BChl a (B800-depleted LH2), which is an important intermediate protein in the B800 exchange, will be useful to tackle the energy transfer mechanism in LH2 by the B800 exchange strategy. In this study, we report a unique spectral change of B800-depleted LH2, in which the Q (© 2024. The Author(s), under exclusive licence to European Photochemistry Association, European Society for Photobiology.) |
Databáze: | MEDLINE |
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