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2018-12-25
Mechanism and atomic structure of superoxide dismutase
Mechanism and atomic structure of superoxide dismutase. [1991];_WJD_2018-1225_V001R01_IR93_
Source (資訊來源):
https://www.ncbi.nlm.nih.gov/pubmed/1649094
Info cited on 2018-12-25-WD2 (資訊引用於 中華民國107年12月25日) by 湯偉晉 (WeiJin Tang)
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Free Radic Res Commun. 1991;12-13 Pt 1:269-78.
Mechanism and atomic structure of superoxide dismutase.
Mechanism and atomic structure of superoxide dismutase.
Mechanism and atomic structure of superoxide dismutase.
Roberts VA1, Fisher CL, Redford SM, McRee DE, Parge HE, Getzoff ED, Tainer JA.
Author information
1
Department of Molecular Biology, Research Institute of Scripps Clinic, La Jolla, California 92037.
Abstract
The active site Cu ion in Cu,Zn superoxide dismutase is alternately oxidized and reduced during the enzymatic dismutation of superoxide to hydrogen peroxide and molecular oxygen. For oxidized Cu,Zn superoxide dismutase, an atomic structure has been determined for the human enzyme at 2.5 A resolution. The resolution of the bovine enzyme structure has been extended to 1.8 A. Atomic resolution data has been collected for reduced and inhibitor-bound Cu,Zn superoxide dismutases, and the interpretation of the electron density difference maps is in progress. The geometry and molecular surfaces of the active sites in these structures, together with biochemical data, suggest a specific model for the enzyme mechanism. Similarities in the active site geometry of the Mn and Fe superoxide dismutases with the Cu,Zn enzyme suggest that dismutation in these enzymes may follow a similar mechanism.
PMID: 1649094
[Indexed for MEDLINE]
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