Rotation of subunits during catalysis by Escherichia coli F1-ATPase.

@article{Duncan1995RotationOS,
  title={Rotation of subunits during catalysis by Escherichia coli F1-ATPase.},
  author={Thomas M. Duncan and Vladimir V. Bulygin and Y L Zhou and Marcus L. Hutcheon and Richard L. Cross},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1995},
  volume={92 24},
  pages={
          10964-8
        }
}
During oxidative and photo-phosphorylation, F0F1-ATP synthases couple the movement of protons down an electrochemical gradient to the synthesis of ATP. One proposed mechanistic feature that has remained speculative is that this coupling process requires the rotation of subunits within F0F1. Guided by a recent, high-resolution structure for bovine F1 [Abrahams, J. P., Leslie, A. G., Lutter, R. & Walker, J. E. (1994) Nature (London) 370, 621-628], we have developed a critical test for rotation of… 

Figures from this paper

Proton ATPases in bacteria: comparison to Escherichia coli F1F0 as the prototype.

The F1F0 ATP synthase complex of Escherichia coli functions reversibly in coupling proton translocation to ATP synthesis or hydrolysis and the oligomeric structure of subunit c will be considered and related to the H+/ATP pumping ratio, P/O ratios and the cation-binding site in other types of F0.

Rotational Catalysis of Escherichia coli ATP Synthase F1 Sector

Results indicate that the domain between β-sheet 4 (βSer-174) and P-loop (βGly-149) is important to drive rotation in ATP synthase (FoF1) coupled with proton transport.

Rotation of the c subunit oligomer in fully functional F1Fo ATP synthase.

It is shown that the ring of c subunits in the F(o) part moves along with the gamma and epsilon subunits, and unequivocally place the c subunit oligomer in the rotor part of this molecular machine.

Rotation of a complex of the gamma subunit and c ring of Escherichia coli ATP synthase. The rotor and stator are interchangeable.

Results indicate that the gammaepsilonc(10-14) complex is a mechanical unit of the enzyme and that it can be used as a rotor or a stator experimentally, depending on the subunit immobilized.

Rotor/Stator Interactions of the ϵ Subunit in Escherichia coli ATP Synthase and Implications for Enzyme Regulation*

Disulfide cross-linking of substituted cysteines on functionally coupled ATP synthase is used to characterize interactions of ϵ with an F0 component of the rotor (subunit c) and with an C-terminal domain of the stator ( subunit β) to demonstrate the ability ofπ to span the central stalk region from the surface of the membrane (ϵ-c) to the bottom of F1 (β-ϵ).

Redox Regulation of the Rotation of F1-ATP Synthase*

It is revealed that the suppressed enzymatic activity of the oxidized F1-ATPase complex was characterized by more frequent long pauses in the rotation of the γ subunit, providing new insights into the mechanisms of enzyme regulation.

Rotation of the ε Subunit during Catalysis by Escherichia coli FOF1-ATP Synthase*

Evidence for catalysis-dependent rotation of the single ε subunit relative to the three catalytic β subunits of functionally coupled, membrane-bound FOF1-ATP synthase is reported, concluding that ε is part of the rotor that couples proton transport to ATP synthesis.

Intersubunit rotation in active F-ATPase

An intersubunit rotation in real time in the functional enzyme F-ATPase is recorded by applying polarized absorption relaxation after photobleaching to immobilized F1 with eosin-labelled γ in a timespan of 100 ms, compatible with the rate of ATP hydrolysis by immobilization F1.

Subunit movement during catalysis by F1-F0-ATP synthases

Evidence argues that the rotation of the complete γ subunit during ATP hydrolysis is not mandatory for activity, and Mechanisms other than rotary catalysis should be considered.

Rotary F1-ATPase

The rotation of γ within hours is compatible with the spectroscopically detected blockade of rotation in the AMP-PNP-inhibited enzyme in the time-range of seconds.
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