Engineering Fe Site Into Host Proteins

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This award in the Inorganic, Bioinorganic and Organometallic Chemistry program with instrumentation funding from the Office of Multidisciplinary Activities supports research in the laboratory of Professor John Caradonna at Yale University. The research involves a semisynthetic design approach to probe the protein effects on the reduction potential and electron transfer activity of the Fe/S cube in iron-sulfur proteins and the iron site in iron-containing superoxide dismutase (SOD). Selectively mutated proteins have already been designed by computer methods and constructed by biological techniques. The SOD protein exhibits catalytic activity. The proteins will now be characterized by an array of physical methods to systematically determine the effects of hydrogen bonding, localized charges and dipoles on the electron transfer activities of the metal centers in the proteins. This research utilizes a new achievement in the study of metal centers in proteins by incorporating iron sites into host proteins. The objective is to construct functional metalloprotein active sites inside host proteins of known structure. This allows a high degree of control of the environment of the metal center, which provdes for systematically studying the effects of the protein on the metal site's activity.