Metal sites in biology often exhibit unique spectroscopic features that reflect novel geometric and electronic structures imposed by the protein that are key to reactivity. The Blue copper active site involved in long range, rapid biological electron transfer is a classic example. This talk presents an overview of both traditional and synchrotron based spectroscopic methods and their coupling to electronic structure calculations to understand the unique features of the Blue copper active site and their contributions to function. The relation of this active site to other biological electron transfer sites is further developed. In particular ultrafast XFEL spectroscopy is used to evaluate the met-S-Fe bond in cyt c, and its control by the protein (called the “entatic state”) in determining the function (electron transfer vs. apoptosis).

Activating metal sites for biological electron transfer

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.