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.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1997
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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.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2004
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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.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2005
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