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• W2020051656 abstract "EPR spectra of ubiquinone-0 (UQ0) and UQ10 anion radicals selectively labeled with 13C at the 4-CO position are reported. The environmental effect on the 4-13C splitting constant was studied in mixed solvents in which the molar fraction of the protic component was changed over a wide range. The quinones were electrochemically reduced, with cyclic voltammetry and concomitant optical spectroscopy being performed as controls. The value and the sign of the 4-13C hyperfine splitting constant strongly depend on the H-bonding properties (proticity) of the solvent, due to the formation of mono- and disolvates through hydrogen bonding of the carbonyl oxygens in protic solvents. The formation of disolvates is less favorable by a factor of 80 than formation of the monosolvated anion. The results are discussed in light of recent EPR, FTIR, and NMR experiments on the primary 13C-labeled acceptor quinone QA in bacterial photosynthetic reaction centers. We propose that in the neutral state both carbonyls of QA are not or only weakly hydrogen bonded to the protein and that formation of anionic QA•- results in a much stronger H-bond for the 4-carbonyl only. The large shift of the 4-CO IR signal reported for UQ in vivo is in our view mostly due to a change in bond order induced by binding of UQ to the protein, perhaps through a change in sp2 hybridization at the 4-C position." @default.
• W2020051656 created "2016-06-24" @default.
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• W2020051656 date "1996-01-01" @default.
• W2020051656 modified "2023-09-27" @default.
• W2020051656 title "Hydrogen-Bonding Effect on ¹³C and Proton Hyperfine Couplings of [4-¹³C]-Labeled Ubisemiquinones <i>in Vitro</i>" @default.
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• W2020051656 doi "https://doi.org/10.1021/jp960059l" @default.
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