Histidinyl Radical Formation in the Self-peroxidation Reaction of Bovine Copper-Zinc Superoxide Dismutase
Open Access
- 1 March 2002
- journal article
- Published by Elsevier
- Vol. 277 (11) , 9160-9166
- https://doi.org/10.1074/jbc.m107342200
Abstract
No abstract availableKeywords
This publication has 36 references indexed in Scilit:
- Increased reactive oxygen species in familial amyotrophic lateral sclerosis with mutations in SOD1Journal of the Neurological Sciences, 2000
- Bicarbonate Is Required for the Peroxidase Function of Cu,Zn-Superoxide Dismutase at Physiological pHPublished by Elsevier ,1999
- Protein Oxidative Damage in a Transgenic Mouse Model of Familial Amyotrophic Lateral SclerosisJournal of Neurochemistry, 1998
- Reexamination of the mechanism of hydroxyl radical adducts formed from the reaction between familial amyotrophic lateral sclerosis-associated Cu,Zn superoxide dismutase mutants and H 2 O 2Proceedings of the National Academy of Sciences, 1998
- Increased 3‐nitrotyrosine and oxidative damage in mice with a human copper/zinc superoxide dismutase mutationAnnals of Neurology, 1997
- A Familial Amyotrophic Lateral Sclerosis-associated A4V Cu,Zn-Superoxide Dismutase Mutant Has a Lower K for Hydrogen PeroxidePublished by Elsevier ,1997
- Mutations in copper-zinc superoxide dismutase that cause amyotrophic lateral sclerosis alter the zinc binding site and the redox behavior of the protein.Proceedings of the National Academy of Sciences, 1996
- Altered Reactivity of Superoxide Dismutase in Familial Amyotrophic Lateral SclerosisScience, 1996
- Interaction of bovine erythrocyte superoxide dismutase with hydrogen peroxide. Inactivation of the enzymeBiochemistry, 1975
- Interaction of bovine erythrocyte superoxide dismutase with hydrogen peroxide. Chemiluminescence and peroxidationBiochemistry, 1975