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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Citations
Cites
McCord, J. M., & Fridovich, I. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)63504-5 · Cited by 12,952
Rapid chromatographic technique for preparative separations with moderate resolution
Still, W. C., Kahn, M., & Mitra, A. (1978) · The Journal of Organic Chemistry · doi:10.1021/jo00408a041 · Cited by 5,841
Oxygen-Derived Free Radicals in Postischemic Tissue Injury
Epstein, F. H., & McCord, J. M. (1985) · New England Journal of Medicine · doi:10.1056/nejm198501173120305 · Cited by 5,399
Handbook of methods for oxygen radical research
Greenwald, R. A. (1987) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(87)80012-6 · Cited by 2,381
Sawyer, D. T., & Valentine, J. S. (1981) · Accounts of Chemical Research · doi:10.1021/ar00072a005 · Cited by 1,358
Superoxide and superoxide dismutases
Fridovich, I. (1993) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(93)90188-z · Cited by 526
Superoxide radical and superoxide dismutase
Fridovich, I. (1972) · Accounts of Chemical Research · doi:10.1021/ar50058a001 · Cited by 469
Hassan, H. M., & Fridovich, I. (1977) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)41019-2 · Cited by 390
Induction of Superoxide Dismutase by Molecular Oxygen
Gregory, E. M., & Fridovich, I. (1973) · Journal of Bacteriology · doi:10.1128/jb.114.2.543-548.1973 · Cited by 320
Effects of Cobalt γ-Radiation on Water and Aqueous Solutions
Hochanadel, C. J. (1952) · The Journal of Physical Chemistry · doi:10.1021/j150497a008 · Cited by 302
Oxy-radicals in molecular biology and pathology
(1989) · Journal of Steroid Biochemistry · doi:10.1016/0022-4731(89)90343-9 · Cited by 252
Masarwa, M., Cohen, H., Meyerstein, D., Hickman, D. L., Bakac, A., & Espenson, J. H. (1988) · Journal of the American Chemical Society · doi:10.1021/ja00221a031 · Cited by 249
A novel metal-free low molecular weight superoxide dismutase mimic.
Samuni, A., Krishna, C. M., Riesz, P., Finkelstein, E., & Russo, A. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)81304-2 · Cited by 233
Self-citationRush, J. D., & Koppenol, W. H. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)62677-3 · Cited by 200
Inhibition of Lipid Peroxidation by Spin Labels
Nilsson, U. A., Olsson, L. I., Carlin, G., & Bylund-Fellenius, A. C. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)60439-9 · Cited by 176
Superoxide reaction with nitroxide spin-adducts
Samuni, A., Krishna, C. M., Riesz, P., Finkelstein, E., & Russo, A. (1989) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(89)90111-1 · Cited by 139
Self-citationA mimic of superoxide dismutase activity based upon desferrioxamine B and manganese(IV)
Darr, D. J., Zarilla, K. A., & Fridovich, I. (1987) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(87)90354-7 · Cited by 99
Scavenging of radicals by vitamin E in the membranes as studied by spin labeling
Takahashi, M., Tsuchiya, J., & Niki, E. (1989) · Journal of the American Chemical Society · doi:10.1021/ja00198a054 · Cited by 90
Role of hydrogen peroxide in the cytotoxicity of the xanthine/xanthine oxidase system
Link, E. M., & Riley, P. A. (1988) · Biochemical Journal · doi:10.1042/bj2490391 · Cited by 85
Reaction of superoxide radicals with copper(II)-histidine complexes
Weinstein, J., & Bielski, B. H. J. (1980) · Journal of the American Chemical Society · doi:10.1021/ja00535a014 · Cited by 80
The Effects of Cellular Glutathione Elevation on the Oxygen Enhancement Ratio
Russo, A., Mitchell, J. B., Finkelstein, E., DeGraff, W., Spiro, I. J., & Gamson, J. (1985) · Radiation Research · doi:10.2307/3576577 · Cited by 69
Self-citationCatalysis of superoxide dismutation by manganese aminopolycarboxylate complexes
Koppenol, W. H., Levine, F., Hatmaker, T. L., et al. (1986) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(86)90368-1 · Cited by 56
An evaluation of paramagnetic broadening agents for spin probe studies of intact mammalian cells
Lai, C., Froncisz, W., & Hopwood, L. E. (1987) · Biophysical Journal · doi:10.1016/s0006-3495(87)83253-8 · Cited by 23
Cited by
Schnackenberg, C. G., Welch, W. J., & Wilcox, C. S. (1998) · Hypertension · doi:10.1161/01.hyp.32.1.59 · Cited by 498
Pike, L. S., Smift, A. L., Croteau, N. J., Ferrick, D. A., & Wu, M. (2011) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2010.10.022 · Cited by 469
Harman, D. (2001) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2001.tb05631.x · Cited by 417
Do Nitroxide Antioxidants Act as Scavengers of O2−˙or as SOD Mimics?
Krishna, M. C., Russo, A., Mitchell, J. B., Goldstein, S., Dafni, H., & Samuni, A. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.42.26026 · Cited by 342
Self-citationLambert, G. P., Gisolfi, C. V., Berg, D. J., Moseley, P. L., Oberley, L. W., & Kregel, K. C. (2002) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00787.2001 · Cited by 326
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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