Gene duplication as a means for altering H+/ATP ratios during the evolution of Fo F1 ATPases and synthases

@article{Cross1990GeneDA,
  title={Gene duplication as a means for altering H+/ATP ratios during the evolution of Fo F1 ATPases and synthases},
  author={Richard L. Cross and Lincoln Taiz},
  journal={FEBS Letters},
  year={1990},
  volume={259}
}
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80 Citations

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Recent discoveries concerning the structure of the ATPases, their assembly and the stoichiometry of their numerous subunits, particularly the proton-carrying proteolipid (subunit c) of the FO and V0 sectors, have shed new light on this question and raise the possibility of variable coupling ratios modulated by variable proteolIPid stoichiometries.
ATP synthases: structure, function and evolution of unique energy converters
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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.
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The data show that the thermodynamic H+/ATP ratio depends on the stoichiometry of the c-subunit, although it is not identical to the c/β ratio.
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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.
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References

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The proteolipid of a mutant ATPase from Escherichia coli defective in H+‐conduction contains a glycine instead of the carbodiimide‐reactive aspartyl residue
The membrane-associated ATPase from Sulfolobus acidocaldarius is distantly related to F1-ATPase as assessed from the primary structure of its alpha-subunit.
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TLDR
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