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Title: Biologically active metal-independent superoxide dismutase mimics

Abstract

Superoxide dismutase (SOD) is an enzyme that detoxifies superoxide (O2.-), a potentially toxic oxygen-derived species. Attempts to increase intracellular concentrations of SOD by direct application are complicated because SOD, being a relatively large molecule, does not readily cross cell membranes. We have identified a set of stable nitroxides that possess SOD-like activity, have the advantage of being low molecular weight, membrane permeable, and metal independent, and at pH 7.0 have reaction rate constants with O2.- ranging from 1.1 x 10(3) to 1.3 x 10(6) M-1 s-1. These SOD mimics protect mammalian cells from damage induced by hypoxanthine/xanthine oxidase and H{sub 2}O{sub 2}, although they exhibit no catalase-like activity. In addition, the nitroxide SOD mimics rapidly oxidize DNA-FeII and thus may interrupt the Fenton reaction and prevent formation of deleterious OH radicals and/or higher oxidation states of metal ions. Whether by SOD-like activity and/or interception of an electron from redox-active metal ions they protect cells from oxidative stress and may have use in basic and applied biological studies.

Authors:
; ; ; ; ; ;  [1]
  1. National Cancer Institute, National Institutes of Health, Bethesda, MD (USA)
Publication Date:
OSTI Identifier:
6714379
Resource Type:
Journal Article
Journal Name:
Biochemistry; (USA)
Additional Journal Information:
Journal Volume: 29:11; Journal ID: ISSN 0006-2960
Country of Publication:
United States
Language:
English
Subject:
63 RADIATION, THERMAL, AND OTHER ENVIRON. POLLUTANT EFFECTS ON LIVING ORGS. AND BIOL. MAT.; HYDROGEN PEROXIDE; TOXICITY; SUPEROXIDE DISMUTASE; BIOLOGICAL FUNCTIONS; CELL CULTURES; CYTOCHROMES; DNA; ELECTRON SPIN RESONANCE; HAMSTERS; OXIDOREDUCTASES; REDOX REACTIONS; ANIMALS; CHEMICAL REACTIONS; ENZYMES; FUNCTIONS; HYDROGEN COMPOUNDS; MAGNETIC RESONANCE; MAMMALS; NUCLEIC ACIDS; ORGANIC COMPOUNDS; OXYGEN COMPOUNDS; PEROXIDES; PIGMENTS; PROTEINS; RESONANCE; RODENTS; VERTEBRATES; 560300* - Chemicals Metabolism & Toxicology

Citation Formats

Mitchell, J B, Samuni, A, Krishna, M C, DeGraff, W G, Ahn, M S, Samuni, U, and Russo, A. Biologically active metal-independent superoxide dismutase mimics. United States: N. p., 1990. Web. doi:10.1021/bi00463a024.
Mitchell, J B, Samuni, A, Krishna, M C, DeGraff, W G, Ahn, M S, Samuni, U, & Russo, A. Biologically active metal-independent superoxide dismutase mimics. United States. https://doi.org/10.1021/bi00463a024
Mitchell, J B, Samuni, A, Krishna, M C, DeGraff, W G, Ahn, M S, Samuni, U, and Russo, A. 1990. "Biologically active metal-independent superoxide dismutase mimics". United States. https://doi.org/10.1021/bi00463a024.
@article{osti_6714379,
title = {Biologically active metal-independent superoxide dismutase mimics},
author = {Mitchell, J B and Samuni, A and Krishna, M C and DeGraff, W G and Ahn, M S and Samuni, U and Russo, A},
abstractNote = {Superoxide dismutase (SOD) is an enzyme that detoxifies superoxide (O2.-), a potentially toxic oxygen-derived species. Attempts to increase intracellular concentrations of SOD by direct application are complicated because SOD, being a relatively large molecule, does not readily cross cell membranes. We have identified a set of stable nitroxides that possess SOD-like activity, have the advantage of being low molecular weight, membrane permeable, and metal independent, and at pH 7.0 have reaction rate constants with O2.- ranging from 1.1 x 10(3) to 1.3 x 10(6) M-1 s-1. These SOD mimics protect mammalian cells from damage induced by hypoxanthine/xanthine oxidase and H{sub 2}O{sub 2}, although they exhibit no catalase-like activity. In addition, the nitroxide SOD mimics rapidly oxidize DNA-FeII and thus may interrupt the Fenton reaction and prevent formation of deleterious OH radicals and/or higher oxidation states of metal ions. Whether by SOD-like activity and/or interception of an electron from redox-active metal ions they protect cells from oxidative stress and may have use in basic and applied biological studies.},
doi = {10.1021/bi00463a024},
url = {https://www.osti.gov/biblio/6714379}, journal = {Biochemistry; (USA)},
issn = {0006-2960},
number = ,
volume = 29:11,
place = {United States},
year = {Tue Mar 20 00:00:00 EST 1990},
month = {Tue Mar 20 00:00:00 EST 1990}
}