Unique rotary ATP synthase and its biological diversity.
F1F0 ATP synthases convert energy stored in an electrochemical gradient of H+ or Na+ across the membrane into mechanical rotation, which is subsequently converted into the chemical bond energy of ATP. The majority of cellular ATP is produced by the ATP synthase in organisms throughout the biological kingdom and therefore under diverse environmental conditions. The ATP synthase of each particular cell is confronted with specific challenges, imposed by the specific environment, and thus by necessity must adapt to these conditions for optimal operation. Examples of these adaptations include diverse mechanisms for regulating the ATP hydrolysis activity of the enzyme, the utilization of different coupling ions with distinct ion binding characteristics, different ion-to-ATP ratios reflected by variations in the size of the rotor c ring, the mode of ion delivery to the binding sites, and the different contributions of the electrical and chemical gradients to the driving force.
Institut für Mikrobiologie, ETH Zürich, Wolfgang-Pauli Strasse 10, CH-8093 Zürich, Switzerland.
Christoph
C
von Ballmoos
Gregory M
GM
Cook
Peter
P
Dimroth
D001695:Biology / Q000639:trends; D008954:Models, Biological; D008956:Models, Chemical; D008958:Models, Molecular; D020409:Molecular Motor Proteins / Q000737:chemistry / Q000502:physiology / Q000648:ultrastructure; D006180:Proton-Translocating ATPases / Q000737:chemistry / Q000502:physiology / Q000648:ultrastructure; D012399:Rotation
D020409:Molecular Motor Proteins; D006180:Proton-Translocating ATPases