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•) for hydroxylic substrates ROH such as ascorbate, which can form strong hydrogen bonds with H-bond-accepting solvents.
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24
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0017333009
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It has been suggested that the ascorbate oxidation reaction at the extravesicular active site utilizes an essential histidine residue that acts as a proton acceptor from ascorbate. (4, 45a, 45b) If this histidine is bound to the iron that accepts the electron, we would still call this H-atom transfer, (10) but it is possible that it could have different properties than the classical HAT from ascorbate to TEMPO described here. More detailed structural data would aid in understanding the nature of the ascorbate/ascorbyl binding pockets and the potential proton acceptors and hydrogen bonding interactions
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This prediction assumes that α-tocopherol is not affected by H-bond donors in the same unusual way that ascorbate is and that the α-tocopherol BDFE is not unusually shifted by local solvation. This assumption is supported by the BDFE data in the Supporting Information and by reports of similar solvent effects on α-tocopherol and phenol reactions in a variety of solvents
-
This prediction assumes that α-tocopherol is not affected by H-bond donors in the same unusual way that ascorbate is and that the α-tocopherol BDFE is not unusually shifted by local solvation. This assumption is supported by the BDFE data in the Supporting Information and by reports of similar solvent effects on α-tocopherol and phenol reactions in a variety of solvents: Valgimigli, L., Banks, J. T., Ingold, K. U., and Lusztyk, J. J. Am. Chem. Soc. 1995, 117, 9966-9971
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