Wherland Sandbox 2

Introduction

Azurin is a bacterial protein that has been extensively studied by bioinorganic and biophysical chemists as a prototype of a Type 1 or "blue" copper protein. It contains a single copper ion that can be in the Cu⁺ or Cu²⁺ or the Cu state. The intensely blue color is due to a charge transfer transition from the cysteine thiolate ligand to the Cu in the Cu²⁺ state. It functions as an electron transfer mediator. The electron transfer reactivity of azurin has been extensively studied, including studies of its reactivity with natural and artificial partners, and intramolecular electron transfer from intrinsic and covalently attached electron transfer partners. The latter studies have been instrumental in defining and evaluating the factors influencing electron transfer reactivity through proteins. These factors include the electron transfer distance, the structure of the intervening peptide medium, the thermodynamic driving force, and the structure of the donor and acceptor. These studies have been instrumental in the iterative testing and advancing of electron transfer theory. One series of studies, delineated here, involves measurement of the rate constant for electron transfer from a disulfide radical, produced by pulse radiolysis, to the Cu²⁺ ion. This reaction can be made to occur because of particular structural features of azurin, the Cu²⁺ site is relatively buried and at the opposite end of the protein from the only disulfide, which is exposed to solvent and electron transfer reagents.

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