Intramolecular Rotation in ATP Synthase: Dynamic and Crystallographic Studies on Thermophilic F1

• Published in: Biochemical and biophysical research communications Vol. 240; no. 2; pp. 247 - 256
• Main Authors: Kagawa, Yasuo, Hamamoto, Toshiro
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 17-11-1997
• Subjects: Adenosine Triphosphate - metabolism; Binding Sites; Catalysis; Crystallography, X-Ray; Electrochemistry; Hot Temperature; Hydrogen-Ion Concentration; Macromolecular Substances; Models, Molecular; Protein Conformation; Proton-Translocating ATPases - chemistry; Proton-Translocating ATPases - metabolism; Thermodynamics; Torque
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1006/bbrc.1997.7574

A single molecule of ATP synthase (F0F1) is by itself a rotary motor, the smallest ever found, and this biomotor is driven by an electrochemical potential of H
+(ΔμH
+). F0F1 is composed of an ion- conducting portion (F0) and a catalytic portion (F1). The major breakthroughs in studies on the mechanochemical coupling have been the direct observation of the rotation of a stable α3β3γ complex of thermophilic F1 (TF1), and X-ray crystallography of the α3β3γ portion of mitochondrial F1 (MF1) and the α3β3 oligomer of TF1. This review focuses on the dynamics of TF1, demonstrated by a crucial experiment. The torque of the rotation was estimated to be 42 pN·nm from the ΔμH
+and frictional force. Important unsolved problems are the crystallography of F0, elastic energy conversion, and the stator and rotor of this biomotor.