Inside Cover: Precise Design of Artificial Cofactors for Enhancing Peroxidase Activity of Myoglobin: Myoglobin Mutant H64D Reconstituted with a “Single-Winged Cofactor” Is Equivalent to Native Horseradish Peroxidase in Oxidation Activity (Chem. Asian J. 9

Abstract

Single-winged heme co-factor brings about the drastic enhancement of the catalytic oxidation activity in myoglobin, an oxygen-storage protein. In their Full Paper on page 2491 ff, Matsuo, Hayashi et al. propose a versatile strategy to alter or enhance the functions of naturally occurring hemoproteins using a combination of “genetic mutation” and the “introduction of a synthetic co-factor”. This synergistic strategy develops unique proteins with ultra-native functions.