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. 2024 Aug;161(1-2):93-103.
doi: 10.1007/s11120-023-01068-0. Epub 2024 Jan 15.

Spectral and conformational characteristics of phycocyanin associated with changes of medium pH

E Yu Parshina  1   2 , W Liu  3 , A I Yusipovich  4 , D A Gvozdev  4 , Y He  3 , S K Pirutin  3   4   5 , E A Klimanova  4 , E G Maksimov  4 , G V Maksimov  4
Affiliations

Spectral and conformational characteristics of phycocyanin associated with changes of medium pH

E Yu Parshina et al. Photosynth Res. 2024 Aug.

Abstract

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.

Keywords: C-phycocyanin (C-PC); Fluorescence anisotropy decay; Infrared (IR) spectroscopy; Raman spectroscopy.

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