Rationally designed biosynthetic models provide fantastic advantages for addressing important issues in chemistry and biology. Previously, two distal histidines were introduced in the heme pocket of myoglobin (Mb) at positions 29 and 43. The resultant His29 and His43, together with the native His64, formed a metal-binding site in the designed L29H/F43H Mb mutant, which closely mimics the heterobinuclear center of native cytochrome c oxidase (CcO). Instead of studying the oxidase activity, we herein investigated the cross-reactivity, i.e., the peroxidase activity of this mutant, as well as the ...
