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Inactivation of Human Manganese-superoxide Dismutase by Peroxynitrite Is Caused by Exclusive Nitration of Tyrosine 34 to 3-Nitrotyrosine
Open accessAbstract
Peroxynitrite has recently been implicated in the inactivation of many enzymes. However, little has been reported on the structural basis of the inactivation reaction. This study proposes that nitration of a specific tyrosine residue is responsible for inactivation of recombinant human mitochondrial manganese-superoxide dismutase (Mn-SOD) by peroxynitrite. Mass spectroscopic analysis of the peroxynitrite-inactivated Mn-SOD showed an increased molecular mass because of a single nitro group substituted onto a tyrosine residue. Single peptides that had different elution positions between samples from the native and peroxynitrite-inactivated Mn-SOD on reverse-phase high performance liquid chromatography were isolated after successive digestion of the samples by staphylococcal serine protease and lysylendopeptidase and subjected to amino acid sequence and molecular mass analyses. We found that tyrosine 34 of the enzyme was exclusively nitrated to 3-nitrotyrosine by peroxynitrite. This residue is located near manganese and in a substrate O-2 gateway in Mn-SOD.
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Poderoso, J. J., Carreras, M. C., Lisdero, C., Riobó, N., Schöpfer, F., & Boveris, A. (1996) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1996.0146 · Cited by 726
Cited by
Nitric Oxide and Peroxynitrite in Health and Disease
Pacher, P., Beckman, J. S., & Liaudet, L. (2007) · Physiological Reviews · doi:10.1152/physrev.00029.2006 · Cited by 6,390
Peroxynitrite: biochemistry, pathophysiology and development of therapeutics
Szabó, C., Ischiropoulos, H., & Radi, R. (2007) · Nature Reviews Drug Discovery · doi:10.1038/nrd2222 · Cited by 2,134
Antioxidant enzymes and human diseases
MatÉs, J. M., Pérez-Gómez, C., & De Castro, I. N. (1999) · Clinical Biochemistry · doi:10.1016/s0009-9120(99)00075-2 · Cited by 2,099
Onset of Maternal Arterial Blood Flow and Placental Oxidative Stress
Jauniaux, E., Watson, A. L., Hempstock, J., Bao, Y.-P., Skepper, J. N., & Burton, G. J. (2000) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)64849-3 · Cited by 1,057
Chemical biology of peroxynitrite: Kinetics, diffusion, and radicals
Ferrer-Sueta, G., & Radi, R. (2009) · ACS Chemical Biology · doi:10.1021/cb800279q · Cited by 776
Metadata
- Authors
- Yamakura, F., Taka, H., Fujimura, T., & Murayama, K.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1998-06
- Volume
- 273
- Issue
- 23
- Pages
- 14085-14089
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2024994588
- Cited by
- 442
- References
- 1
- FWCI
- 7.43
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- CoChat. (2026). Citation check: Inactivation of Human Manganese-superoxide Dismutase by Peroxynitrite Is Caused by Exclusive Nitration of Tyrosine 34 to 3-Nitrotyrosine. https://app.cochat.ai/papers/10.1074/jbc.273.23.14085
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- Yamakura, F., Taka, H., Fujimura, T., & Murayama, K. (1998). Inactivation of Human Manganese-superoxide Dismutase by Peroxynitrite Is Caused by Exclusive Nitration of Tyrosine 34 to 3-Nitrotyrosine. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.273.23.14085
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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