By José H Zagal; Fethi Bedioui; Jean-Pol Dodelet

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The origin of the low FeIII/II potentials of synthetic heme/Cu analogs is not known. It may be related to the stabilization of the charged ferric state in the more polar environment experienced by an electrode-confined catalyst vis-`a-vis the heme/Cu site buried in a nonpolar protein matrix51 . 3. Possible Physiological Role of CuB from Biomimetic Electrocatalytic Studies Elucidating the function of distal CuB in O2 reduction by HCOs has recently been the major focus of biomimetic studies of HCOs32, 34 .

No adequate explanation for this unexpected result was offered by the authors63 . It may originate from Cu-mediated homolysis of the O-O bond in H2 O2 , which is generated during O2 reduction at the Fe porphyrin moiety. Cu, being an efficient Fenton reagent, generates • OH in the presence of H2 O2 . 15. O2 adducts of (A) the heme/Cu site of HCOs (compound A) and (B and C) two heme/Cu analogs53, 61 . Structure A is derived from resonance Raman spectroscopy18 . 2) is based on resonance Raman and 1 H NMR spectroscopic data53 and structure C is determined by single-crystal X-ray 61 analysis; counterion (BPh− 4 ) is omitted for clarity .

2. E. I. Chan (2001). Structures and proton-pumping strategies of mitochondrial respiratory enzymes. Annu. Rev. Biophys. Biomol. Struct. 30, 23–65. 3. G. (1982). Bioenergetics: An Introduction to the Chemiosmotic Theory. Academic Press, London.

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