Single crystals of the reduced form of Cu, Zn superoxide dismutase (space group P2(1)2(1)2(1), one dimer per asymmetric unit) have been obtained and their X-ray structure refined at 1.9 Angstrom resolution. The structure shows that the imidazolate bridge is maintained in the present crystalline form. It is confirmed that in solution the bridge is broken and the involved histidine is protonated on the side of copper. Based on the NOE constraints, and with the aid of molecular dynamics calculations, a structural model is proposed for the molecule in solution. Both structures are considered significant as far as the enzymatic mechanism is concerned. (C) 1994 Academic Press, Inc.
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|Titolo:||X-ray, Nmr and Molecular-dynamics Studies On Reduced Bovine Superoxide-dismutase - Implications For the Mechanism|
|Citazione:||L., B., I., B., B., B., P., C., C., L., Mangani, S., et al. (1994). X-ray, Nmr and Molecular-dynamics Studies On Reduced Bovine Superoxide-dismutase - Implications For the Mechanism. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 202(2), 1088-1095.|
|Appare nelle tipologie:||1.1 Articolo in rivista|
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