A characterization of copper/zinc superoxide dismutase mutants at position 124. Zinc-deficient proteins.

doi:10.1111/j.1432-1033.1991.tb15794.x

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Article

A characterization of copper/zinc superoxide dismutase mutants at position 124. Zinc-deficient proteins.

European journal of biochemistry - 26 Feb 1991

Banci L, Bertini I, Cabelli D E, Hallewell R A, Tung J W, Viezzoli M S

Abstract excerpt

Substitution of the completely conserved aspartic acid residue at position 124 of Cu,Zn superoxide dismutase with asparagine and glycine has been performed through site-directed mutagenesis on the human enzyme. Asp124 is H-bonded to the NH of two histidines, one of which is bound to copper and th...

Topics

Cobalt
Copper
Electron Spin Resonance Spectroscopy
Hydrogen-Ion Concentration
Magnetic Resonance Spectroscopy
Mutation
Superoxide Dismutase
Zinc

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