Biological nano motor, ATP synthase F(o)F(1): from catalysis to gammaepsilonc(10-12) subunit assembly rotation.
Proton translocating ATPase (ATP synthase), a chemiosmotic enzyme, synthesizes ATP from ADP and phosphate coupling with the electrochemical ion gradient across the membrane. This enzyme has been studied extensively by combined genetic, biochemical and biophysical approaches. Such studies revealed a unique mechanism which transforms an electrochemical ion gradient into chemical energy through the rotation of a subunit assembly. Thus, this enzyme can be defined as a nano motor capable of coupling a chemical reaction and ion translocation, or more simply, as a protein complex carrying out rotational catalysis. In this article, we briefly discuss our recent work, emphasizing the rotation of subunit assembly (gammaepsilonc(10-12)) which is formed from peripheral and intrinsic membrane subunits.
Wada
Y
Y
Division of Biological Sciences, The Institute of Scientific and Industrial Research, Osaka University, CREST of Japan Science and Technology Corporation, Ibaraki, 567-0047, Japan.
Sambongi
Y
Y
Futai
M
M
D000818:Animals; D002384:Catalysis; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D008565:Membrane Proteins / Q000737:chemistry*; D008958:Models, Molecular; D020409:Molecular Motor Proteins; D015394:Molecular Structure; D009154:Mutation; D006180:Proton-Translocating ATPases / Q000737:chemistry* / Q000235:genetics; D011522:Protons; D012399:Rotation
D008565:Membrane Proteins; D020409:Molecular Motor Proteins; D011522:Protons; D006180:Proton-Translocating ATPases