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

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...

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Bibliographic Details
Published in:Photosynthesis research 2024-08, Vol.161 (1-2), p.93-103
Main Authors: Parshina, E. Yu, Liu, W., Yusipovich, A. I., Gvozdev, D. A., He, Y., Pirutin, S. K., Klimanova, E. A., Maksimov, E. G., Maksimov, G. V.
Format: Article
Language:English
Subjects:
Anisotropy
Biochemistry
Biomedical and Life Sciences
Chromophores
Cyanobacteria
Infrared spectroscopy
Lasers
Life Sciences
Light emitting diodes
Microenvironments
pH effects
Phycobilisomes
Plant Genetics and Genomics
Plant Physiology
Plant Sciences
Protein structure
Proteins
Secondary structure
Spectrum analysis
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Summary: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.
ISSN:0166-8595
1573-5079
1573-5079
DOI:10.1007/s11120-023-01068-0