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Intracellular Glutathione Peroxidases — Structure, Regulation, and Function

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Selenium in Biology and Human Health

Abstract

Glutathione peroxidase (glutathione:H202 oxidoreductase E.C. 1.11.1.9) was discovered by Mills (1) in 1957 in his search for the factors that function in the protection of erythrocytes against oxidative hemolysis. Similarly, John Rotruck, working in Professor Hoekstra’s laboratory, focused on GPX in his search for an enzymatic function that made selenium (Se) an antioxidant (2). The unraveling of the Se/GPX story has fascinated a generation of scientists, and it has led to the use of GPX activity as one of the best indicators of Se status as well as to its use as the index of choice for the determination of Se requirements. The form of Se in GPX and the mechanism of Se insertion into the enzyme have become, together, an academic subject matter of their own; the study of this enzyme has now moved into the exciting world of molecular biology, and these investigations are helping us learn much more about the regulation of GPX and Se. This research suggests that the important function of classical GPX in some tissues is to regulate Se metabolism and Se flux to selenoproteins.

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  1. Roger A. Sunde
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  1. Division of Gastroenterology Department of Medicine School of Medicine, Vanderbilt University, 37232, Nashville, TN, USA

    Raymond F. Burk

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Sunde, R.A. (1994). Intracellular Glutathione Peroxidases — Structure, Regulation, and Function. In: Burk, R.F. (eds) Selenium in Biology and Human Health. Springer, New York, NY. https://doi.org/10.1007/978-1-4612-2592-8_4

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  • DOI: https://doi.org/10.1007/978-1-4612-2592-8_4

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