The kinetic mechanism of glutathione peroxidase from human platelets
Abstract
Human platelet glutathione peroxidase (GSH-Px) exhibits a ping-pong type kinetic mechanism. Peroxide changes the redox state of the enzyme and renders it highly stable against attack by alkylating agents. Peroxide seems also to act as a positive homotropic modulator modifying the allosteric kinetics of the enzyme. The combination of these two mechanisms accelerates response against peroxides. This finding reassesses importance of GSH-Px for the platelet protection.
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During enzymatic reduction of hydrogen peroxide, selenocysteine undergoes sequential oxidation by hydrogen peroxide to form selenenic acid, followed by reaction with GSH to form a Se-SG intermediate before a second GSH combines to form GSSG, resolving the active site to Se-H.
“During the enzymatic reduction of hydrogen peroxide, Sec undergoes sequential oxidation by hydrogen peroxide to form a selenenic acid, Se-OH, followed by reaction with GSH to form a Se-SG intermediate before a second GSH combines to form GSSG, resolving the active site to Se-H (133, 278).”
From Redox regulation of mitochondrial function (2012) · cites this paper as [278]
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- Authors
- Ramos Martínez, J. I., Díaz García, R., & Galarza, A. M.
- Affiliations
- Universidade de Santiago de Compostela (ES)
- Venue
- Thrombosis Research
- Publisher
- Elsevier BV
- Published
- 1982-07
- Volume
- 27
- Issue
- 2
- Pages
- 197-203
- ISSN
- 0049-3848 (ISSN-L)
- OpenAlex
- W1997990935
- Cited by
- 11
- References
- 23
- Citations by year
- 2026: 1 · 2025: 1 · 2022: 1 · 2020: 2 · 2018: 1 · 2014: 1 · 2013: 1 · 2012: 1
- FWCI
- 0.00
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Thrombosis Research (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Health Sciences › Nursing › Nutrition and Dietetics › Selenium in Biological Systems
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glutathione Transferases and Polymorphisms
- Keywords
- glutathione peroxidase, human platelets, ping-pong mechanism, peroxide activation, redox state, alkylating agent resistance, allosteric modulation, homotropic cooperativity, enzyme kinetics
- MeSH terms
- Adult, Blood Platelets, Glutathione, Glutathione Peroxidase, Humans, Kinetics, Oxidation-Reduction, Peroxidases, Peroxides, tert-Butylhydroperoxide
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