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Free radical metabolites of L-cysteine oxidation.
Open accessAbstract
The oxidation of L-cysteine by horseradish peroxidase in the presence of oxygen forms a thiyl free radical as demonstrated with the spin-trapping ESR technique. Reactions of this thiyl free radical result in oxygen consumption, which is inhibited by the spin trap 5,5'-dimethyl-1-pyrroline-N-oxide. Cysteine sulfinic acid, a cysteine metabolite, is a poorer substrate for horseradish peroxidase than cysteine and is oxidized to form both sulfur-centered and carbon-centered free radicals.
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Citations
Cited by
Spin Trapping: ESR parameters of spin adducts 1474 1528V
Buettner, G. R. (1987) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(87)80033-3 · Cited by 1,827
Molecular and Cellular Aspects of Thiol–Disulfide Exchange
Gilbert, H. F. (1990) · Advances in Enzymology - and Related Areas of Molecular Biology · doi:10.1002/9780470123096.ch2 · Cited by 758
Huycke, M. M., Abrams, V., & Moore, D. R. (2002) · Carcinogenesis · doi:10.1093/carcin/23.3.529 · Cited by 489
(2001) · Current Topics in Cellular Regulation · doi:10.1016/s0070-2137(01)80007-8 · Cited by 427
Qian, Z.-J., Jung, W.-K., & Kim, S.-K. (2008) · Bioresource Technology · doi:10.1016/j.biortech.2007.04.005 · Cited by 411
Metadata
- Authors
- Harman, L. S., Mottley, C., & Mason, R. P.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1984-05
- Volume
- 259
- Issue
- 9
- Pages
- 5606-5611
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1524926009
- Cited by
- 244
- References
- 0
- FWCI
- 6.60
- Type
- journal article
- Language
- en
- Open access
- hybrid
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