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• W2522969256 abstract "Phycocyanin (PC) is the most abundant accessory light-harvesting pigmented protein found in cyanobacteria. In the present investigation, prominent roles of tyrosine residue (Tyr) in excitation energy transfer between chromophores in PC of hot-spring cyanobacteria were studied. The expression pattern of codons suggests that Tyr was most abundant amino acids in α subunits as compared to β subunits in total aromatic amino acids. The α subunits of PC model (PDB 3O18) have one chromophore at cysteine (Cys) α-84 position (~ 10 Tyr) and β subunits contains two chromophores located at β-84 (~ 5 Tyr) and β-155 (~ 3 Tyr) in the cyanobacterium Thermosynechococcus vulcanus. The hydrophobic and hydrogen bond interaction was most favored between Tyr and buried amino acids near α-84 chromophore. The aromatic-aromatic interaction, aromatic-sulphur interaction, cation-pi interaction were mostly linked with Cys (α-84) as compared to β-84 and β-155. Phenylalanine (Phe) was demonstrating fewer interactions with chromophores due to nature of weak internal fluorescence. The coordinates of PC chromophore showed that internal fluorescence was very high close to Cys (α-84) residue which transmits excited photonic energy between intra-monomeric subunits Cys α84adg-Cys β84bch and inter-monomer Cys β84b-Cys β84c-Cys β84h. The lateral transmission of energy between adjacent hexamer-hexamer was feasible by Cys β155 chromophore. In contrast to total aromatic amino acids, tyrosine appeared exclusive for internal energy transfer by property of high internal fluorescence. These findings provide the illustrated role of tyrosine amino acids in rapid energy transfer mechanism inside PC which may be incorporated for making energy devices and various biotechnological sciences." @default.
• W2522969256 created "2016-09-30" @default.
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• W2522969256 date "2016-12-01" @default.
• W2522969256 modified "2023-10-16" @default.
• W2522969256 title "Structural and functional dynamics of tyrosine amino acid in phycocyanin of hot-spring cyanobacteria: A possible pathway for internal energy transfer" @default.
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• W2522969256 doi "https://doi.org/10.1016/j.genrep.2016.09.005" @default.
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