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- Title
Redshifting and Blueshifting of β82 Chromophores in the Phycocyanin Hexamer of Porphyridium purpureum Phycobilisomes Due to Linker Proteins.
- Authors
Kikuchi, Hiroto
- Abstract
The chromophore bound to the 84th amino acid in the -subunit ( 84), the chromophore bound to the 82nd amino acid in the -subunit ( 82), and the chromophore bound to the 153th amino acid in the -subunit ( 153) are depicted using blue stick, purple spacefill, and black stick representations, respectively. Based on the structural data obtained by Ma et al. [[11]], the absorption wavelength of each 82 chromophore in the PC hexamer located next to the top of core B was calculated using quantum chemical treatment, including the electric effect from its surrounding phycocyanin proteins and two linker proteins. Conclusions According to the quantum chemical calculations of this research, the 82 chromophore in the N2 chain, which is the closest of those in the phycocyanin (PC) hexamer to the core, is significantly redshifted by L SB RC sb 1, indicating that it is the energy sink of the rod. The hexameric structure modulates the optical absorption wavelength of the outside chromophore and effectively transfers the light energy absorbed at the outer chromophore to the inner chromophores [[23]].
- Subjects
PHYCOBILISOMES; PHYCOCYANIN; CHROMOPHORES; PROTEINS; HELMHOLTZ equation; OSCILLATOR strengths; MOLECULAR orbitals; REDSHIFT
- Publication
Life (2075-1729), 2022, Vol 12, Issue 11, p1833
- ISSN
2075-1729
- Publication type
Article
- DOI
10.3390/life12111833