Department of Chemistry, Nagaoka University of Technology, Nagaoka, 940-2188 Japan.
J Phys Chem B. 2012 Sep 13;116(36):11098-102. doi: 10.1021/jp3057338. Epub 2012 Aug 29.
Glutathione is a tripeptide capable of diminishing active oxygen species in living cells. The photocatalytic decomposition of glutathione and related amino acids in TiO(2) suspension was investigated with (1)H NMR spectroscopy. The results suggest that both glutathione in reduced and oxidative forms is adsorbed on the TiO(2) surface by carboxyl or amino groups but not by the thiol group of the side chain which plays a crucial role in the glutathione cycle, to be degraded. This means that the function of glutathione cycle should be deteriorated in living cells by the adsorption. However, the decomposition rates are considerably low as compared with those of the constituent amino acids (Glu, Cys, and Gly), possibly reflecting the self-defensive property against active oxygen species.
谷胱甘肽是一种三肽,能够减少活细胞中的活性氧物质。用 (1)H NMR 光谱法研究了谷胱甘肽和 TiO(2)悬浮液中相关氨基酸的光催化分解。结果表明,还原和氧化形式的谷胱甘肽均通过羧基或氨基而不是巯基吸附在 TiO(2)表面,巯基在谷胱甘肽循环中起关键作用,会被降解。这意味着在活细胞中,吸附作用会使谷胱甘肽循环的功能恶化。然而,与组成氨基酸(Glu、Cys 和 Gly)相比,其分解速率相当低,这可能反映了其对活性氧物质的自我防御特性。