The DOI matches its Crossref record; 23 of the 23 references it cites were found in a registry or an index.
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 H2O2, 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.
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Metadata
- Authors
- Mitchell, J. B., Samuni, A., Krishna, M. C., DeGraff, W. G., Ahn, M. S., Samuni, U., & Russo, A.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1990-03-20
- Volume
- 29
- Issue
- 11
- Pages
- 2802-2807
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W2042582442
- Cited by
- 428
- References
- 23
- FWCI
- 16.56
- Type
- journal article
- Language
- en
- Open access
- closed
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