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A new functional biomimetic model of cytochrome c oxidase is reported. It is synthesized in 32 steps. Single turnover reaction with oxygen leads to the same intermediates as the ones reported in the enzyme: Fe(III)O2·-/Cu(I)/PhOH (oxygen complex), and Fe(IV)=O/Cu(II)/PhO· (PM). A sister model derivatized with an alkyne was immobilized on azide-functionnalized self-assembled monolayer (SAM) coated gold electrodes by Cu(I)-catalyzed click chemistry. The rate of electron transfer from the electrode to the model was controlled by the length of the linker in the SAM. Steady-state turnover was achieved at biologically relevant electron transfer, where CuB and Tyr244 mimics rapidly deliver their electrons, hence minimizing the release of partially reduced oxygen species (PROS).

Using Functional Models to Understand the Four-Electron Reduction of Dioxygen by Cytochrome c Oxidase Under Steady State Conditions