Spectral and conformational characteristics of phycocyanin associated with changes of medium pH.
Autor: | Parshina EY; Faculty of Biology, Shenzhen MSU-BIT University, Shenzhen, 518172, China. parshinae@gmail.com.; Faculty of Biology, Lomonosov Moscow State University, Moscow, Russia, 119991. parshinae@gmail.com., Liu W; Faculty of Biology, Shenzhen MSU-BIT University, Shenzhen, 518172, China., Yusipovich AI; Faculty of Biology, Lomonosov Moscow State University, Moscow, Russia, 119991., Gvozdev DA; Faculty of Biology, Lomonosov Moscow State University, Moscow, Russia, 119991., He Y; Faculty of Biology, Shenzhen MSU-BIT University, Shenzhen, 518172, China., Pirutin SK; Faculty of Biology, Shenzhen MSU-BIT University, Shenzhen, 518172, China.; Faculty of Biology, Lomonosov Moscow State University, Moscow, Russia, 119991.; Institute of Theoretical and Experimental Biophysics of Russian Academy of Sciences, Institutskaya St. 3, Pushchino, Russia, 142290., Klimanova EA; Faculty of Biology, Lomonosov Moscow State University, Moscow, Russia, 119991., Maksimov EG; Faculty of Biology, Lomonosov Moscow State University, Moscow, Russia, 119991., Maksimov GV; Faculty of Biology, Lomonosov Moscow State University, Moscow, Russia, 119991. |
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Jazyk: | angličtina |
Zdroj: | Photosynthesis research [Photosynth Res] 2024 Aug; Vol. 161 (1-2), pp. 93-103. Date of Electronic Publication: 2024 Jan 15. |
DOI: | 10.1007/s11120-023-01068-0 |
Abstrakt: | C-phycocyanin (C-PC) is the main component of water-soluble light-harvesting complexes (phycobilisomes, PBS) of cyanobacteria. PBS are involved in the absorption of quantum energy and the transfer of electronic excitation energy to the photosystems. A specific environment of C-PC chromophoric groups is provided by the protein matrix structure including protein-protein contacts between different subunits. Registration of C-PC spectral characteristics and the fluorescence anisotropy decay have revealed a significant pH influence on the chromophore microenvironment: at pH 5.0, a chromophore is more significantly interacts with the solvent, whereas at pH 9.0 the chromophore microenvironment becomes more viscous. Conformations of chromophores and the C-PC protein matrix have been studied by Raman and infrared spectroscopy. A decrease in the medium pH results in changes in the secondary structure either the C-PC apoproteins and chromophores, the last one adopts a more folded conformation. (© 2024. The Author(s), under exclusive licence to Springer Nature B.V.) |
Databáze: | MEDLINE |
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