Molecular mechanisms of rotational catalysis in the F(0)F(1) ATP synthase.
Rotation of the F(0)F(1) ATP synthase gamma subunit drives each of the three catalytic sites through their reaction pathways. The enzyme completes three cycles and synthesizes or hydrolyzes three ATP for each 360 degrees rotation of the gamma subunit. Mutagenesis studies have yielded considerable information on the roles of interactions between the rotor gamma subunit and the catalytic beta subunits. Amino acid substitutions, such as replacement of the conserved gammaMet-23 by Lys, cause altered interactions between gamma and beta subunits that have dramatic effects on the transition state of the steady state ATP synthesis and hydrolysis reactions. The mutations also perturb transmission of specific conformational information between subunits which is important for efficient conversion of energy between rotation and catalysis, and render the coupling between catalysis and transport inefficient. Amino acid replacements in the transport domain also affect the steady state catalytic transition state indicating that rotation is involved in coupling to transport.
Nakamoto
R K
RK
Department of Molecular Physiology and Biological Physics, University of Virginia, P.O. Box 10011, Charlottesville, VA 22906-0011, USA. rkn3c@virginia.edu
Ketchum
C J
CJ
Kuo
P H
PH
Peskova
Y B
YB
Al-Shawi
M K
MK
D000255:Adenosine Triphosphate / Q000096:biosynthesis / Q000378:metabolism; D001665:Binding Sites; D004789:Enzyme Activation; D004926:Escherichia coli / Q000201:enzymology; D008958:Models, Molecular; D020409:Molecular Motor Proteins / Q000737:chemistry*; D009154:Mutation; D011487:Protein Conformation; D006180:Proton-Translocating ATPases / Q000737:chemistry* / Q000235:genetics
D020409:Molecular Motor Proteins; D000255:Adenosine Triphosphate; D006180:Proton-Translocating ATPases