The evolution of A‐, F‐, and V‐type ATP synthases and ATPases: reversals in function and changes in the H+/ATP coupling ratio

  title={The evolution of A‐, F‐, and V‐type ATP synthases and ATPases: reversals in function and changes in the H+/ATP coupling ratio},
  author={Richard L. Cross and Volker M{\"u}ller},
  journal={FEBS Letters},
An intermediate step in the evolution of ATPases − the F1F0‐ATPase from Acetobacterium woodii contains F‐type and V‐type rotor subunits and is capable of ATP synthesis
This is the first demonstration that an ATPase with a V0–F0 hybrid motor is capable of ATP synthesis, and the purification protocol was revised to improve the subunit recovery.
An intermediate step in the evolution of ATPases – a hybrid F0–V0 rotor in a bacterial Na+ F1F0 ATP synthase
These analyses clearly demonstrate, for the first time, an F0–V0 hybrid motor in an ATP synthase, and isolate and study the composition of the c’ring, which contains both types of c subunits.
Conformational dynamics of the rotary subunit F in the A3B3DF complex of Methanosarcina mazei Gö1 A‐ATP synthase monitored by single‐molecule FRET
This work investigated the nucleotide‐dependent conformational changes of subunit F relative to subunit D during ATP hydrolysis in the A3B3DF complex of the Methanosarcina mazei Gö1 A‐ATP synthase using single‐molecule Förster resonance energy transfer and found two conformations.
Structure and conformational plasticity of the intact Thermus thermophilus V/A-type ATPase
To uncover mechanistic differences in energy coupling between F- and V/A-type enzymes, Zhou and Sazanov determined structures of a V- and A-type ATP synthase from the bacterium Thermus thermophilus, revealing a rotor coupling mechanism.
ATP Synthases With Novel Rotor Subunits: New Insights into Structure, Function and Evolution of ATPases
A duplicated c subunit with only one ion-translocating group was found along with “normal” F0c subunits in the Na+ F1F0 ATP synthase of the bacterium Acetobacterium woodii.
Function and Subunit Interactions of the N-terminal Domain of Subunit a (Vph1p) of the Yeast V-ATPase*
Results suggest that a localized region of the N-terminal domain is important in anchoring the peripheral stator in V1V0, suggesting that in vivo dissociation of the V-ATPase generates a V0 domain that does not passively conduct protons.
Domain Architecture of the Stator Complex of the A1A0-ATP Synthase from Thermoplasma acidophilum*
A structural model of the A-ATPase peripheral stalk is proposed, which finds that the isolated C-terminal domain of the E subunit exists as a dimer in solution, consistent with a recent crystal structure of the related Pyrococcus horikoshii A- ATPase E subunits.


ATP synthases: structure, function and evolution of unique energy converters
Recent studies on the molecular biology of the AO/FO/VO domains revealed surprising findings about duplicated and triplicated versions of the proteolipid subunit and shed new light on the evolution of these ion pumps.
Arg-735 of the 100-kDa subunit a of the yeast V-ATPase is essential for proton translocation
It is suggested that Arg-735 is absolutely required for proton transport by the V-ATPases and is discussed in the context of a revised model of the topology of the 100-kDa subunit a.
The Intriguing Evolution of the “b” and “G” Subunits in F-type and V-type ATPases: Isolation of the vma-10 Gene from Neurospora crassa
The vma-10 gene which encodes the G subunit of the vacuolar ATPase in Neurospora crassa is characterized and the observation that this region could form an alpha helix in which all of the conserved residues are clustered on one face is striking.
The Membrane Domain of the Na+-motive V-ATPase from Enterococcus hirae Contains a Heptameric Rotor*
Symmetry mismatch between the catalytic and membrane domains appears to be an intrinsic feature of both V- and F-ATPases.
H+/ATP ratio of proton transport‐coupled ATP synthesis and hydrolysis catalysed by CF0F1—liposomes
The H+/ATP ratio and the standard Gibbs free energy of ATP synthesis were determined with a new method using a chemiosmotic model system. The purified H+‐translocating ATP synthase from chloroplasts
Evolution of the vacuolar H+-ATPase: implications for the origin of eukaryotes.
It is reported that the same vacuolar H-ATPase subunits are approximately equal to 50% identical to the alpha and beta subunits, respectively, of the sulfur-metabolizing Sulfolobus acidocaldarius, an archaebacterium (Archaeobacterium).
The Na(+)-F(1)F(0)-ATPase operon from Acetobacterium woodii. Operon structure and presence of multiple copies of atpE which encode proteolipids of 8- and 18-kda.
The results unequivocally prove that the Na(+)-ATPase from A. woodii is an enzyme of the F(1)F(0) class and the gene encoding the proteolipid underwent quadruplication.
The ATP synthase--a splendid molecular machine.
  • P. Boyer
  • Chemistry
    Annual review of biochemistry
  • 1997
An X-ray structure of the F1 portion of the mitochondrial ATP synthase shows asymmetry and differences in nucleotide binding of the catalytic beta subunits that support the binding change mechanism
A simple energy-conserving system: Proton reduction coupled to proton translocation
It is demonstrated that the production of hydrogen gas by membrane vesicles of P. furiosus is directly coupled to the synthesis of ATP by means of a proton-motive force that has both electrochemical and pH components.