Peroxidase Activity of .BETA..ALPHA..BETA..ALPHA.-Polypeptide Containing Iron-porphyrin and Arginine.

Accession number;00A0163483
Title;Peroxidase Activity of .BETA..ALPHA..BETA..ALPHA.-Polypeptide Containing Iron-porphyrin and Arginine.
Author; NISHINO HIDEKAZU (Kyushu Inst. of Technol., Fac. of Eng.) TOMIZAKI KIN'YA (Kyushu Inst. of Technol., Fac. of Eng.) NISHINO NORIKAZU (Kyushu Inst. of Technol., Fac. of Eng.)
Journal Title;Abstracts. Symposium on Biofunctional Chemistry
Journal Code:L0836A
ISSN:
VOL.14th;NO.;PAGE.48-49(1999)
Figure&Table&Reference;
Pub. Country;Japan
Language;Japanese
Abstract;Cytochrome c peroxidase which catalyzes the oxidation of a substrate has one heme and two histidine residues (distal His and proximal His) at its active site. The distal His could serve as a proton donor and cooperate with charged arginine(Arg) to make the distal side substantially polar (pull effect). The proximal imidazolate ligand of His could serve as a strong internal electron donor to destabilize the O-O bond of the hydroperoxoiron(III)-porphyrin (push effect). In order to develop the de novo designed polypeptide in enzymatic activity, we attempted to engineer the iron(III)-porphyrin linked .BETA..ALPHA..BETA..ALPHA.-polypeptide by attachment of positive charged Arg to its active site. (author abst.)