ATP synthase is a membrane protein complex that synthesizes adenosine triphosphate (ATP), an integral molecule that provides energy to all forms of life. The complex is comprised of two rotary motors, the soluble F1 sector and the membrane embedded Fo sector. ATP synthesis is catalyzed by conformational changes within F1, which are driven by the rotation of the c-ring (rotor) of Fo. The Fo motor is powered by the electrochemical gradient of H+ across the cell membrane, and movement of H+ through Fo is facilitated by two aqueous half-channels within subunit a (stator) and at the rotor-stator interface. The mechanism of how H+-driven rotation in Fo is generated is not fully understood. Cryo-electron microscopy has provided medium resolution structures of E. coli F1Fo ATP synthase, but inconsistencies between this structural data and previous cross-linking data within subunit a suggest the existence of multiple conformations. In order to gain insight into suspected conformational dynamics of the stator, we have utilized site-directed spin labeling and electron paramagnetic resonance (EPR) spectroscopy to observe backbone mobility at several points in subunit a. We demonstrate the feasibility of this approach to report on the structure of subunit a and discuss the results of these mobility measurements.

Spectroscopic observation of structural dynamics in the Fo motor of E. coli ATP synthase

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.