Nickel Superoxide Dismutase Structure and Mechanism

The 1.30 Å resolution crystal structure of nickel superoxide dismutase (NiSOD) identifies a novel SOD fold, assembly, and Ni active site. NiSOD is a hexameric assembly of right-handed 4-helix bundles of up−down−up−down topology with N-terminal hooks chelating the active site Ni ions. This newly iden...

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Veröffentlicht in:	Biochemistry (Easton) 2004-06, Vol.43 (25), p.8038-8047
Hauptverfasser:	Barondeau, David P, Kassmann, Carey J, Bruns, Cami K, Tainer, John A, Getzoff, Elizabeth D
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Azides - pharmacology Binding Sites Conserved Sequence Crystallography, X-Ray Cyanides - pharmacology Electron Spin Resonance Spectroscopy Enzyme Inhibitors - pharmacology Escherichia coli - genetics Escherichia coli - metabolism Models, Molecular Molecular Sequence Data Nickel - chemistry Nickel - metabolism Oxidation-Reduction Protein Structure, Quaternary Protein Subunits Recombinant Proteins - antagonists & inhibitors Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - metabolism Sequence Alignment Static Electricity Streptomyces - enzymology Streptomyces - genetics Superoxide Dismutase - antagonists & inhibitors Superoxide Dismutase - chemistry Superoxide Dismutase - genetics Superoxide Dismutase - metabolism
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