The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Atomic structures of wild-type and thermostable mutant recombinant human Cu,Zn superoxide dismutase.
Open accessAbstract
Superoxide dismutase enzymes protect aerobic organisms from oxygen-mediated free-radical damage. Crystallographic structures of recombinant human Cu,Zn superoxide dismutase have been determined, refined, and analyzed at 2.5 A resolution for wild-type and a designed thermostable double-mutant enzyme (Cys-6----Ala, Cys-111----Ser). The 10 subunits (five dimers) in the crystallographic asymmetric unit form an unusual stable open lattice with 80-A-diameter channels. The 10 independently fit and refined subunits provide high accuracy, error analysis, and insights on loop conformations. There is a helix dipole interaction with the Zn site, and 14 residues form two or more structurally conserved side-chain to main-chain hydrogen bonds that appear critical to active-site architecture, loop conformation, and the increased stability resulting from the Cys-111----Ser mutation.
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Cites
Electrostatic recognition between superoxide and copper, zinc superoxide dismutase
Getzoff, E. D., Tainer, J. A., Weiner, P. K., Kollman, P. A., Richardson, J. S., & Richardson, D. C. (1983) · Nature · doi:10.1038/306287a0 · Cited by 554
Self-citationElectrostatic interactions in the reaction mechanism of bovine erythrocyte superoxide dismutase
Cudd, A., & Fridovich, I. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)33779-7 · Cited by 211
Cited by
Rosen, D. R., Siddique, T., Patterson, D., Figlewicz, D. A., Sapp, P., Hentati, A., Donaldson, D., Goto, J., O'Regan, J. P., Deng, H.-X., et al. (1993) · Nature · doi:10.1038/362059a0 · Cited by 7,062
Recent Advances in Zinc Enzymology
Lipscomb, W. N., & Sträter, N. (1996) · Chemical Reviews · doi:10.1021/cr950042j · Cited by 1,366
Regulation of superoxide dismutase genes: Implications in disease
Miao, L., & St. Clair, D. K. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.05.018 · Cited by 912
Beckman, J. S., Carson, M., Smith, C. D., & Koppenol, W. H. (1993) · Nature · doi:10.1038/364584a0 · Cited by 870
An Expanded Eukaryotic Genetic Code
Chin, J. W., Cropp, T. A., Anderson, J. C., Mukherji, M., Zhang, Z., & Schultz, P. G. (2003) · Science · doi:10.1126/science.1084772 · Cited by 820
Metadata
- Authors
- Parge, H. E., Hallewell, R. A., & Tainer, J. A.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1992-07
- Volume
- 89
- Issue
- 13
- Pages
- 6109-6113
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W1968735793
- Cited by
- 304
- References
- 2
- FWCI
- 9.53
- Type
- journal article
- Language
- en
- Open access
- green
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- Parge, H. E., Hallewell, R. A., & Tainer, J. A. (1992). Atomic structures of wild-type and thermostable mutant recombinant human Cu,Zn superoxide dismutase. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.89.13.6109
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