Encyclopedia of Biophysics

2013 Edition
| Editors: Gordon C. K. Roberts

F1-ATPase: Fundamental Properties and Structure

  • Daichi Okuno
  • Ryota Iino
  • Hiroyuki NojiEmail author
Reference work entry
DOI: https://doi.org/10.1007/978-3-642-16712-6_205



ATP synthase, termed as F 0F 1-ATP synthase, exists in thylakoid membrane, mitochondrial inner membrane, and bacterial membrane. It consists of a combination of a water soluble F 1 part with a membrane embedded F 0 part (Fig.  1). This enzyme catalyzes adenosine triphosphate (ATP) synthesis reaction from adenosine diphosphate (ADP) and inorganic phosphate (Pi) using the proton flow across the membrane. Both F 1 and F 0 are rotary motors, but driving forces are different: rotation of F 1 is driven by the free energy of ATP hydrolysis (Fig.  1, lower right), and that of F 0 is driven by the electrochemical potential of proton (the proton motive force) across the membrane (Fig.  1, upper right). In bacteria, F 1 is composed of α 3β 3γδε subunits. The minimum complex that functions as a motor is α 3β 3γ subcomplex. α and β subunits have non-catalytic and catalytic ATP-binding sites near at the α/β interface, respectively. They form a hexamer ring in...
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Copyright information

© European Biophysical Societies' Association (EBSA) 2013

Authors and Affiliations

  1. 1.Laboratory for Cell Dynamics Observation, Quantitative Biology CenterRIKENSuitaJapan
  2. 2.Department of Applied ChemistryGraduate School of Engineering, The University of TokyoBunkyo-kuJapan