Brent L. Iverson, Sheila A. Iverson, Victoria A. Roberts, Elizabeth D. Getzoff, John A. Tainer, Stephen J. Benkovic, Richard A. Lerner

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111 Scopus citations


A metalloantibody has been constructed with a coordination site for metals in the antigen binding pocket. The Zn(II) binding site from carbonic anhydrase B was used as a model. Three histidine residues have been placed in the light chain complementarity determining regions of a single chain antibody molecule. In contrast to the native protein, the mutant displayed metal-dependent fluorescence-quenching behavior. This response was interpreted as evidence for metal binding in the three-histidine site with relative affinities in the order Cu(II) > Zn(II) > Cd(II). The presence of metal cofactors in immunoglobulins should facilitate antibody catalysis of redox and hydfolytic reactions.

Original languageEnglish (US)
Pages (from-to)659-666
Number of pages8
Issue number4969
StatePublished - Aug 10 1990

All Science Journal Classification (ASJC) codes

  • General


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