The Behaviors of Glutathione and Related Amino Acids in the TiO2 Photocatalytic System

Glutathione is a tripeptide capable of diminishing active oxygen species in living cells. The photocatalytic decomposition of glutathione and related amino acids in TiO2 suspension was investigated with 1H NMR spectroscopy. The results suggest that both glutathione in reduced and oxidative forms is...

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Bibliographic Details
Published in:The journal of physical chemistry. B 2012-09, Vol.116 (36), p.11098-11102
Main Authors: Nosaka, Atsuko Y, Tanaka, Goro, Nosaka, Yoshio
Format: Article
Language:English
Subjects:
Adsorption
Amino Acids - chemistry
Catalysis
Glutathione - chemistry
Magnetic Resonance Spectroscopy
Oxidation-Reduction
Photochemical Processes
Titanium - chemistry
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Summary:Glutathione is a tripeptide capable of diminishing active oxygen species in living cells. The photocatalytic decomposition of glutathione and related amino acids in TiO2 suspension was investigated with 1H NMR spectroscopy. The results suggest that both glutathione in reduced and oxidative forms is adsorbed on the TiO2 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.
ISSN:1520-6106
1520-5207
DOI:10.1021/jp3057338