Peroxidase Activity of Cationic Metalloporphyrin-Antibody Complexes

✍ Scribed by Hiroyasu Yamaguchi; Kaori Tsubouchi; Kazuhide Kawaguchi; Eri Horita; Akira Harada

• Book ID: 101830735
• Publisher: John Wiley and Sons
• Year: 2004
• Tongue: English
• Weight: 338 KB
• Volume: 10
• Category: Article
• ISSN: 0947-6539
• DOI: 10.1002/chem.200305692

✦ Synopsis

Abstract

Peroxidase activity of a complex of water‐soluble cationic metalloporphyrin with anti‐cationic porphyrin antibody is reported. Antibody 12E11G, which was prepared by immunization with a conjugate of 5‐(4‐carboxyphenyl)‐10,15,20‐tris(4‐methylpyridyl)porphine iodide (3MPy1C), bound to tetramethylpyridylporphyrin iron complex (Fe^III^–TMPyP) with the dissociation constant of 2.6×10^−7^ M. The complex of antibody 12E11G with Fe^III^–TMPyP catalyzed oxidation of pyrogallol, catechol, and guaiacol. A Lineweaver–Burk plot for the oxidation of pyrogallol catalyzed by the Fe^III^–TMPyP–antibody complex showed K~m~=8.6 mM and k~cat~=680 min^−1^. Under the same conditions, K~m~ and k~cat~ for horseradish peroxidase (HRP) were 0.8 mM and 1750 min^−1^, respectively. Although the binding interaction of the antibody to the substrates was one order lower than that of native HRP, the peroxidase activity of this system was in the same order of magnitude as that of HRP.