Please use this identifier to cite or link to this item: http://hdl.handle.net/20.500.12779/4023
Title: X-ray, Nmr and Molecular-dynamics Studies On Reduced Bovine Superoxide-dismutase - Implications For the Mechanism
Authors: L., Banci
I., Bertini
B., Bruni
P., Carloni
C., Luchinat
Mangani, Stefano 
P. L., Orioli
M., Piccioli
W., Ripniewski
K. S., Wilson
Keywords: crystal structure; x-ray; superoxide dismutase; mechanism
Issue Date: 1994
Project: None 
Journal: BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Abstract: 
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.
Description: 
47984
URI: http://hdl.handle.net/20.500.12779/4023
ISSN: 0006-291X
DOI: 10.1006/bbrc.1994.2040
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