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

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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 hydrolytic reactions.

Original languageEnglish (US)
Pages (from-to)659-662
Number of pages4
Issue number4969
Publication statusPublished - Jan 1 1990


All Science Journal Classification (ASJC) codes

  • General

Cite this

Iverson, B. L., Iverson, S. A., Roberts, V. A., Getzoff, E. D., Tainer, J. A., Benkovic, S., & Lerner, R. A. (1990). Metalloantibodies. Science, 249(4969), 659-662.