[HTML][HTML] Transient accumulation of elastic energy in proton translocating ATP synthase

DA Cherepanov, AY Mulkidjanian, W Junge - FEBS letters, 1999‏ - Elsevier
ATP synthase is conceived as a rotatory engine with two reversible drives, the proton-
transporting membrane portion, F0, and the catalytic peripheral portion, F1. They are …

[HTML][HTML] The structure of the H+-ATP synthase from chloroplasts and its subcomplexes as revealed by electron microscopy

B Böttcher, P Gräber - Biochimica et Biophysica Acta (BBA)-Bioenergetics, 2000‏ - Elsevier
The electron microscopic data available on CF0F1 and its subcomplexes, CF0, CF1, subunit
III complex are collected and the CF1 data are compared with the high resolution structure of …

F0F1-ATPase/synthase is geared to the synthesis mode by conformational rearrangement of ϵ subunit in response to proton motive force and ADP/ATP balance

T Suzuki, T Murakami, R Iino, J Suzuki, S Ono… - Journal of Biological …, 2003‏ - jbc.org
The ϵ subunit in F 0 F 1-ATPase/synthase undergoes drastic conformational rearrangement,
which involves the transition of two C-terminal helices between a hairpin" down"-state and …

Direct observation of the rotation of ε subunit in F1-ATPase

Y Kato-Yamada, H Noji, R Yasuda, K Kinosita… - Journal of Biological …, 1998‏ - jbc.org
Rotation of the ε subunit in F 1-ATPase from thermophilic Bacillusstrain PS3 (TF 1) was
observed under a fluorescence microscope by the method used for observation of the γ …

[HTML][HTML] F-ATPase: specific observation of the rotating c subunit oligomer of EFoEF1

O Pänke, K Gumbiowski, W Junge, S Engelbrecht - Febs Letters, 2000‏ - Elsevier
The rotary motion in response to ATP hydrolysis of the ring of c subunits of the membrane
portion, Fo, of ATP synthase, FoF1, is still under contention. It was studied with EFoEF1 …

ATP synthase and other motor proteins

W Junge - Proceedings of the National Academy of Sciences, 1999‏ - pnas.org
Proteins, the working machines of the cell, operate as enzymes to catalyze chemical
synthesis, as ion pumps to generate electrical voltage, and as motors to generate …

F0 of ATP Synthase Is a Rotary Proton Channel: OBLIGATORY COUPLING OF PROTON TRANSLOCATION WITH ROTATION OF c-SUBUNIT RING∗

T Suzuki, H Ueno, N Mitome, J Suzuki… - Journal of Biological …, 2002‏ - jbc.org
Coupling of proton flow and rotation in the F 0 motor of ATP synthase was investigated using
the thermophilic Bacillus PS3 enzyme expressed functionally in Escherichia coli cells …

Direct indication for the existence of a double stalk in CF0F1

B Böttcher, L Schwarz, P Gräber - Journal of molecular biology, 1998‏ - Elsevier
The H+-ATPase from chloroplasts (CF0F1) was investigated by electron microscopy of
negatively stained single molecules followed by image processing. The analysis of about …

Direct visualisation of conformational changes in EF0F1 by electron microscopy

B BoÈttcher, I Bertsche, R Reuter, P GraÈber - Journal of Molecular Biology, 2000‏ - Elsevier
The isolated H+-ATPase from Escherichia coli (EF0F1) was investigated by electron
microscopy of samples of negatively stained monodisperse molecules, followed by single …

[HTML][HTML] Epistatic interactions of deletion mutants in the genes encoding the F1‐ATPase in yeast Saccharomyces cerevisiae

J Lai‐Zhang, Y **ao, DM Mueller - The EMBO journal, 1999‏ - embopress.org
The F 1‐ATPase is a multimeric enzyme (α 3 β 3 γδϵ) primarily responsible for the synthesis
of ATP under aerobic conditions. The entire coding region of each of the genes was deleted …