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Wednesday, April 26 • 8:30am - 10:00am
Spectroscopic Study of mechanical movement in the F o motor of E. coli ATP synthase

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F1Fo ATP synthase is present in all life and is responsible for the production of almost all adenosine triphosphate (ATP), which is one of the most prolific energy molecules that are synthesized during metabolism. Fo converts electrochemical potential into mechanical rotation, which drives conformational changes in F1 that facilitate the synthesis of ATP. The mechanism of rotation of the subunit c ring is not known, but there are currently two hypotheses. This study will look for evidence of the ratcheting mechanism of rotation, which states that the helices of subunits a and c act like mechanical gears during rotation. This mechanism would require the α-helices of subunit a that lie on the a-c interface to move during rotation. Site directed mutagenesis was used to mutate a residue on one of these helices into a cysteine. This mutant ATP synthase will be purified and then chemically modified with a spin label, which can be observed using electron paramagnetic resonance (EPR) spectroscopy. The EPR signal is sensitive to the protein environment and will provide data on the mobility of the residue to which the spin label is attached. This could also clarify the possibility of mechanical movement in the Fo complex.

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Wednesday April 26, 2017 8:30am - 10:00am
Concourse - Wilma Sherrill Center

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