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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 the other to zinc. The mutant proteins, as expressed in Escherichia coli, result in an essential zinc-free enzyme which...

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Identifiers

PMID: 1848181
DOI: 10.1111/j.1432-1033.1991.tb15794.x

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