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. 1985 Jan 1;225(1):203–208. doi: 10.1042/bj2250203

Dye-sensitized photo-oxidation of enzymes.

C S Tsai, J R Godin, A J Wand
PMCID: PMC1144570  PMID: 3156581

Abstract

Heart lipoamide dehydrogenase, liver alcohol dehydrogenase and egg-white lysozyme are photo-oxidized in the presence of various dye sensitizers. The photodynamic process is preceded by the binding between the enzyme and the sensitizers. Among the commonly used dyes, halogenated xanthines and thiazine are effective sensitizers for the photo-inactivation of these three enzymes. Histidine residues are the primary target for the sensitized photo-oxidation that inactivates lipoamide dehydrogenase and alcohol dehydrogenase. However, the destruction of tryptophan residues is responsible for the photo-inactivation of lysozyme. The deuterium medium effect and the quenching effect by various scavengers of the potential photo-oxidative intermediates implicate the participation of the mixed type I-type II mechanism, with the involvement of singlet oxygen being of greater importance, in the photo-inactivation of the enzymes.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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