Janda, K.D.; Lerner, R.A.

J. Am. Chem. Soc. 1993, 115, 4906-4907, 10.1021/ja00064a068

n/a

Pan, Y.

RSC Adv. 2013, 3, 22976, 10.1039/c3ra43784a

Horseradish Peroxidase (HRP) is a commercially available and prevalently used peroxidase with no specific substrate binding domain. However, after being incorporated with different metal cations, new catalytic functions were found in biomimetic oxidation of resveratrol. Based on the results of screening, Ca, Cu, Fe and Mn incorporated enzymes showed distinctive effects, either decomposition or dimerization products were observed.

Lerner, R.A.

Science 1989, 243, 1184-1188, 10.1126/science.2922606

Monoclonal antibodies have been induced that are capable of catalyzing specific hydrolysis of the Gly-Phe bond of peptide substrates at neutral pH with a metal complex cofactor. The antibodies were produced by immunizing with a Co(III) triethylenetetramine (trien)-peptide hapten. These antibodies as a group are capable of binding trien complexes of not only Co(III) but also of numerous other metals. Six peptides were examined as possible substrates with the antibodies and various metal complexes. Two of these peptides were cleaved by several of the antibodies. One antibody was studied in detail, and cleavage was observed for the substrates with the trien complexes of Zn(II), Ga(III), Fe(III), In(III), Cu(II), Ni(II), Lu(III), Mg(II), or Mn(II) as cofactors. A turnover number of 6 x 10(-4) per second was observed for these substrates. These results demonstrate the feasibility of the use of cofactor-assisted catalysis in an antibody binding site to accomplish difficult chemical transformations.