Comparative studies in series of cytochrome c oxidase models

This study compares the behavior as cytochrome c oxidase (CcO) functional and structural models of a series of reported and unreported ligands that provide either a binding site for copper without a built-in proximal base, or both a flexible binding site for copper and a built-in proximal base, or a fixed binding site for copper with a built-in proximal base. The comparisons of the models show that the relative position of the two metal sites is not only a crucial parameter in the control of the catalytic behavior but also essential in mimicking other features of the enzyme such as CO exchange between the ferrous heme a3 and the cuprous CuB center.

CO binding studies as well as electrocatalytic studies in a series of models of the bimetallic active site of cytochrome c oxidase confirm that the relative positioning of the two metals is a crucial parameter of the catalytic behavior.Figure optionsDownload as PowerPoint slide