Enzyme function of copper, zinc superoxide dismutase as a free radical generator.
نویسندگان
چکیده
منابع مشابه
Enzyme function of copper, zinc superoxide dismutase as a free radical generator.
The peroxidative activity of Cu,Zn-containing superoxide dismutase (Cu, Zn-SOD) was studied by using a chromogen, 2,2'-azinobis-(3-ethylbenzthiazoline-6-sulfonate) (ABTS) which reacts with .OH radicals to form ABTS+, and the spin traps, N-tert-butyl-alpha-phenylnitrone (PBN) and 5,5-dimethyl-1-pyrroline N-oxide (DMPO). The formation of ABTS+. in this study required both active Cu,Zn-SOD and H2O...
متن کاملTotal reconstitution of copper-zinc superoxide dismutase.
The total reconstitution of copper-zinc superoxide dismutase by stoichiometric addition of the metals to completely metal-free apoprotein is described. Reconstitution has been monitored by electron paramagnetic resonance (EPR) and absorption spectroscopy, enzymic activity, and acrylamide gel el%ctrophoresis. Under the same conditions, it has been possible to prepare highly active enzymes with c...
متن کامل(Bi)sulfite Oxidation by Copper,Zinc-Superoxide Dismutase: Sulfite-Derived, Radical-Initiated Protein Radical Formation
BACKGROUND Sulfur dioxide, formed during the combustion of fossil fuels, is a major air pollutant near large cities. Its two ionized forms in aqueous solution, sulfite and (bi)sulfite, are widely used as preservatives and antioxidants to prevent food and beverage spoilage. (Bi)sulfite can be oxidized by peroxidases to form the very reactive sulfur trioxide anion radical (*SO(3)-). This free rad...
متن کاملAberrant zinc binding to immature conformers of metal-free copper-zinc superoxide dismutase triggers amorphous aggregation.
Superoxide dismutase 1 (SOD1) is a Cu/Zn metalloenzyme that aggregates in amyotrophic lateral sclerosis (ALS), a fatal neurodegenerative disorder. Correct metal insertion during SOD1 biosynthesis is critical to prevent misfolding; however Zn(2+) can bind to the copper-site leading to an aberrantly metallated protein. These effects of Zn(2+) misligation on SOD1 aggregation remain to be explored,...
متن کاملEscherichia coli expresses a copper- and zinc-containing superoxide dismutase.
A mutant of Escherichia coli, unable to produce manganese- or iron-containing superoxide dismutase (SOD), was found to contain modest levels of an SOD that was judged to be a copper- and zinc-containing SOD on the basis of inhibition by cyanide and inactivation by either H2O2 or diethyldithiocarbamate. Moreover, the diethyldithiocarbamate-inactivated enzyme could be reactivated with Cu(II), and...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1993
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)53585-7