Keeping up with the F(sub1)-ATPase
Article Abstract:
Work by Kinosita, Yoshida and colleagues on F(sub1)ATPase, visualizes rotation of the gamma-subunit relative to alternating sets of alpha- and beta-subunits. A histidine tag is attached to one end of the beta-subunits, which were inverted over glass and an actin filament was attached to the gamma-stalk, via biotin-streptavidin-biotin links. Kinosita and colleagues believe that the near-100% efficiency with which F(sub1)-ATPase converts chemical to mechanical energy accords with the reversible nature of the native enzyme.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1998
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Energy transduction in ATP synthase
Article Abstract:
It has been possible to establish a mechanism for transducing free energy stored in an ion gradient into a rotary torque. It was shown that biased diffusion, boosted by electrostatic forces, produces sufficient torque to account for ATP production. In this model, the motor works as well when other ions are substituted for protons. The model offers an explanation for the impact of mutations in the vital rotor and stator amino acids.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1998
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Energy transduction in the F(sub1) motor of ATP synthase
Article Abstract:
The enzyme ATP synthase manufactures ATP from ADP and phosphate using energy from a transmembrane protonmotive gradient. A rotary mechanism regulates both the synthetic and hydrolytic cycles of ATP synthase. A model for the ATP rotary engine is presented, and it is concluded that the F(sub1) motor derives is high mechanical torque and nearly 100% efficiency from the conversion of free energy of ATP binding into elastic strain.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1998
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