Rotation and structure of FoF1-ATP synthase.

@article{Okuno2011RotationAS,
  title={Rotation and structure of FoF1-ATP synthase.},
  author={Daichi Okuno and Ryota Iino and Hiroyuki Noji},
  journal={Journal of biochemistry},
  year={2011},
  volume={149 6},
  pages={655-64}
}
F(o)F(1)-ATP synthase is one of the most ubiquitous enzymes; it is found widely in the biological world, including the plasma membrane of bacteria, inner membrane of mitochondria and thylakoid membrane of chloroplasts. However, this enzyme has a unique mechanism of action: it is composed of two mechanical rotary motors, each driven by ATP hydrolysis or proton flux down the membrane potential of protons. The two molecular motors interconvert the chemical energy of ATP hydrolysis and proton… CONTINUE READING
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