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Friday, February 3, 2017
 

Apr 2019
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Today is:
Mon, Apr 22, 2019


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12:20pm
to
1:20pm
  VTLSS Seminar: Robustness of rotary catalysis of F1-ATPase  
(Research)

Location:
Biocomplexity Institute of Virginia Tech, Conference Center (145)

Presenter:
Hiroyuki Noji
Professor of Applied Chemistry, University of Tokyo

Abstract: F1-ATPase is a rotary motor protein in which the inner subunit rotates against the surrounding stator ring upon ATP hydrolysis(1,2). The stator ring is composed of 3 a and 3 b subunits, and the catalytic reaction centers are located on the 3 a-b interfaces, mainly on the b subunits.

The unique feature of F1-ATPase that discriminates it from other molecular motors is the high energy conversion efficiency and the reversibility of the chemomechanical coupling; when the rotation is forcibly reversed, F1-ATPase catalyzes ATP synthesis reaction against large free energy of ATP hydrolysis(3). The experimental verification that the rotary angle of the rotary shaft controls the chemical equilibrium of ATP hydrolysis/synthesis was thought to suggest that the 3 reaction centers communicate via the atomically fine-tuned molecular interaction of the b subunits with the rotary shaft subunit.

However, recent experiments showed the rotation mechanism is far more robust than we though before; even after removing the rotary shaft, the remaining stator ring undergoes cooperative power stroke motion among 3 b subunits(4).

This finding suggests that the allostery is programmed in the stator ring, pointing the possibility that an artificial rod-shaped molecule would be rotated in the stator ring of F1-ATPase. We tested this hypothesis by incorporating a xenogeneic protein in the stator ring. The artificial molecule showed unidirectional rotation although the generated torque is evidently lower than the wild-type F1-ATPase(5).
More information...


Location: Biocomplexity Institute of Virginia Tech, Conference Center (145)
Price: free
Sponsor: Fralin Life Science Institute
Contact: Dr. Zhaomin Yang
E-Mail: zmyang@vt.edu
   
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