Using electron microscopy and high-speed atomic force microscopy, researchers show the internal molecular motor behind the gliding mechanism for Mycoplasma mobile to consist of two ATP synthase-like ...

The stoichiometry of c subunits in the H+-transporting Fo rotary motor of ATP synthase is uncertain, the most recent suggestions varying from 10 to 14. The stoichiometry will determine the number of ...

F1-ATPase is the catalytic component of the ATP synthase molecular machine responsible for most of the uphill synthesis of ATP in living systems. The enormous advances in biochemical and structural ...

The mitochondrial ATP synthase is energy-converting macromolecular machine that uses the electrochemical potential across the bioenergetic membrane called cristae. This potential is maintained via a ...

Scientists have solved the structure of mitochondrial ATP synthase, an enzyme that makes ATP, adenosine triphosphate, the major energy source of cells. A team of scientists headed by Rosalind Franklin ...

Found inside mitochondria, ATP synthase generates the energy storage molecule adenosine triphosphate, which the cells of all living things use for fuel. The enzyme generally looks similar in shape ...

Scientists have redesigned one of nature's molecular machines to make the world's smallest switchable motor. The rotating machine can be turned on and off like a pocket fan - but it is only about 14 ...

For more than 20 years, Makoto Miyata from Osaka City University has been studying the gliding motility of the parasitic bacterium Mycoplasma mobile (M. mobile). It is a mechanism consisting of an ...