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Volumn 132, Issue 22, 2010, Pages 7784-7793

Tuning of the thermochemical and kinetic properties of ascorbate by its local environment: Solution chemistry and biochemical implications

Author keywords

[No Author keywords available]

Indexed keywords

ACETONITRILE SOLUTIONS; ADDED WATER; AQUEOUS SOLUTION CHEMISTRY; BIOCHEMICAL IMPLICATIONS; BIOLOGICAL IMPLICATIONS; COFACTORS; DRIVING FORCES; ENZYME ACTIVE SITES; HYDROGEN ATOMS; HYDROGEN-ATOM TRANSFER; IN-VIVO; KINETIC EFFECT; KINETIC PROPERTIES; LARGE SHIFTS; LOCAL ENVIRONMENTS; MEMBRANE INTERFACE; POLAR SOLUTES; REDUCING POWER; SOLUTION CHEMISTRY; SOLVENT EFFECTS; TEMPO RADICAL; VITAMIN C;

EID: 77953100064     PISSN: 00027863     EISSN: 15205126     Source Type: Journal    
DOI: 10.1021/ja102337n     Document Type: Article
Times cited : (101)

References (61)
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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
    • 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. Bashtovyy, D., Bérczi, A., Asard, H., and Páli, R. Protoplasma 2003, 221, 31-40
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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: Valgimigli, L., Banks, J. T., Ingold, K. U., and Lusztyk, J. J. Am. Chem. Soc. 1995, 117, 9966-9971
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    • note
    • • (see Supporting Information).


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.