Kinetics and Mechanisms of Fe(III) and Cu(II) Reduction by Heme Proteins

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This is a project supported by an award from the Chemistry Office of Special Projects under the aegis of the Chemistry of Life Processes Initiative. The fundamental goal is to understand the bioinorganic mechanisms for electron transport in heme proteins and their role in the metabolism of trace metals by cells. Several heme proteins including hemoglobin, myoglobin, cytochrome c and b5 are effective reductants for complexes of Fe(III) and Cu(II). Electrons can be transferred from the heme Fe(II) to the metal complex over distances as great as 20 A by an outer sphere electron transfer mechanism. The questions addressed in this research are: 1) What kinetic parameters regulate and control the electron transfer? 2) What mechanisms are operating in the non-specific outer sphere electron transport at the heme edge and in site-specific binding of the metal complex prior to electron transfer? 3) What are the physical-chemical characteristics of low molecular weight complexes of Fe(III) and Cu(II) that may be of biochemical significance?