Many critical biochemical processes are made possible by the evolutionary inclusion of transition metals, yet the inherent reactivity of metals renders them toxic to living organisms in even slight excess. At the host-pathogen interface, this toxicity is actually exploited and used as a killing tool, with both participants in an arms race to dominate. Periplasmic bacterial RND (resistance nodulation division) pumps have been the subjects of great interest due both to their diverse substrates and to their potential for antimicrobial targeting. My recent work on the RND heavy metal export pump CusCBA has probed the chemistry of Cu+/Ag+ binding and the biological mechanism of metal-ion flux. Yet, two major pieces of the puzzle are missing: the rate at which the metals are transferred, and how that rate is controlled by specific structural elements of the interacting protein components. Here I will describe our lab’s promising developments using rapid flow x-ray absorption and native fluorescence spectroscopic techniques to probe the chemical kinetics of protein-to-protein metal transfer in the mechanism of CusC(F)BA metal ion efflux.

Decoding a secret handshake: Tracking protein-to-protein Cu(I) transfer by rapid x-ray absorption and intrinsic fluorescence techniques

253rd National Meeting (2017)

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