36 degrees step size of proton-driven c-ring rotation in FoF1-ATP synthase.
Synthesis of adenosine triphosphate ATP, the 'biological energy currency', is accomplished by F(o)F(1)-ATP synthase. In the plasma membrane of Escherichia coli, proton-driven rotation of a ring of 10 c subunits in the F(o) motor powers catalysis in the F(1) motor. Although F(1) uses 120 degrees stepping during ATP synthesis, models of F(o) predict either an incremental rotation of c subunits in 36 degrees steps or larger step sizes comprising several fast substeps. Using single-molecule fluorescence resonance energy transfer, we provide the first experimental determination of a 36 degrees sequential stepping mode of the c-ring during ATP synthesis.
Düser
Monika G
MG
3. Physikalisches Institut, Universität Stuttgart, Stuttgart, Germany.
Zarrabi
Nawid
N
Cipriano
Daniel J
DJ
Ernst
Stefan
S
Glick
Gary D
GD
Dunn
Stanley D
SD
Börsch
Michael
M
D000255:Adenosine Triphosphate / Q000378:metabolism; D001703:Biophysics / Q000379:methods; D002384:Catalysis; D004926:Escherichia coli / Q000201:enzymology; D031541:Fluorescence Resonance Energy Transfer / Q000379:methods; D008051:Lipid Bilayers / Q000737:chemistry; D008954:Models, Biological; D009010:Monte Carlo Method; D009154:Mutation; D017785:Photons; D010957:Plasmids / Q000378:metabolism; D011487:Protein Conformation; D006180:Proton-Translocating ATPases / Q000378:metabolism / Q000502:physiology*; D011522:Protons; D012399:Rotation
D008051:Lipid Bilayers; D011522:Protons; D000255:Adenosine Triphosphate; D006180:Proton-Translocating ATPases