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Nonenzymatic cleavage of proteins by reactive oxygen species generated by dithiothreitol and iron.
Open accessAbstract
Many enzymes, represented by yeast glutamine synthetase, are inactivated and degraded in the presence of dithiothreitol (DTT), oxygen, and catalytic amounts of iron salts. The roles of DTT and iron can be replaced by ascorbate and copper, respectively. Experimental data suggest that reactive oxygen species, likely hydroxyl radicals, are generated locally around irons bound at specific sites on enzymes, and these species are responsible for the inactivation and degradation. Since many biochemicals are contaminated with metal salts in quantities sufficient for some hydroxyl radical formation to occur, the possibility of oxidative modification and degradation should be considered when an enzyme is exposed to DTT.
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Cited by
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Imlay, J. A., & Linn, S. (1988) · Science · doi:10.1126/science.3287616 · Cited by 1,974
Rhee, S. G., Chae, H. Z., & Kim, K. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.02.026 · Cited by 1,409
Self-citationMetal ion-catalyzed oxidation of proteins: Biochemical mechanism and biological consequences
Stadtman, E. R. (1990) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(90)90006-5 · Cited by 1,153
Self-citationReactive Oxygen-Mediated Protein Oxidation in Aging and Disease
Stadtman, E. R., & Berlett, B. S. (1998) · Drug Metabolism Reviews · doi:10.3109/03602539808996310 · Cited by 891
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Metadata
- Authors
- Kim, K., Rhee, S. G., & Stadtman, E. R.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1985-12
- Volume
- 260
- Issue
- 29
- Pages
- 15394-15397
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1529662354
- Cited by
- 272
- References
- 0
- FWCI
- 5.40
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Kim, K., Rhee, S. G., & Stadtman, E. R. (1985). Nonenzymatic cleavage of proteins by reactive oxygen species generated by dithiothreitol and iron. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(17)36264-6
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