Phycobiliproteins of the cyanobacterium Arthrospira platensis, known as Spirulina, are protein-chromophore complexes which are used by the organism to capture light energy. Allophycocyanin and C-phycocyanin are prominent in providing a natural source of blue food coloring. An unresolved issue remains the rapid loss of the native conformation of the pigment, leading to altered color with changing pH. This study investigates color changes on a quantum mechanics scale. A model was established to predict color shifts upon environmental changes, while proposing a mechanism to elucidate pH-dependent chromophore dynamics. On average, the model predicts a hypsochromic shift of 34 nm, in close alignment with the experimentally determined 36 nm. Results show several key non-covalent interactions governing the dynamics of the pyrrole rings of allophycocyanin, particularly influenced by solvents and pH. Particularly noteworthy are the hydrogen bonds with arginine (R 86) and aspartic acid (D 87), contributing to the distinctive optical absorption properties. These findings aid in pigment selection and the targeting of specific phycocyanin regions for stabilization, reducing the dependence on artificial food colors.
Keywords: Band-shape assumption; Chromophore torsion; Phycobiliprotein; Phycocyanobilin; Protein chromophore interactions.
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