Direct observation of the rotation of F(sub 1)-ATPase

Article Abstract:

A direct observation of the motion of a single molecule of F(sub 1)-adenosine triphosphatase (ATPase) shows that the molecule acts as a rotary motor. Earlier studies have concluded that the gamma-subunit of F(sub 1)-ATPase rotates within the alpha beta-hexamer. In the presence of ATP, the gamma-subunit was observed to rotate for more than 100 revolutions in an anticlockwise direction when seen from the 'membrane' side.

Analysis, Cells, Cell migration

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Mechanically driven ATP synthesis by F1-ATPase

Article Abstract:

The chemical synthesis of ATP with the use of mechanical energy is reported. The results of the analysis states that, the chemo-mechanical coupling in the F1 motor of ATP synthase is reversible and is achieved by manipulating the rotary angle of the gamma-subunit.

Chemical synthesis

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Highly coupled ATP synthesis by F1-ATPase single molecules

Article Abstract:

The F1 ATPase is the tiniest identified rotary motor and it revolves in an anticlockwise direction since it hydrolyses ATP(super 1-5). It indicates that E subunit contains an important part to be performed at the time of ATP synthesis.

ATP synthesis

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