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

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

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.

MeSH terms

  • Bacterial Proteins* / chemistry
  • Fluorescence Polarization
  • Hydrogen-Ion Concentration
  • Light-Harvesting Protein Complexes* / chemistry
  • Phycocyanin* / chemistry
  • Protein Folding
  • Protein Structure, Secondary
  • Spectrophotometry, Infrared
  • Spectrum Analysis, Raman
  • Spirulina* / enzymology

Substances

  • Phycocyanin
  • Light-Harvesting Protein Complexes
  • Bacterial Proteins