Structure and Mechanism of F ₀ F ₁ ‐Type ATP Synthases and ATPases

This publication has 145 references indexed in Scilit:

• Gene duplication as a means for altering H⁺/ATP ratios during the evolution of F_o F₁ ATPases and synthases
  FEBS Letters, 1990
• Site directed mutagenesis of the β-subunit of the yeast mitochondrial ATPase
  Biochemical and Biophysical Research Communications, 1989
• Identification of a mutation in Escherichia coli F₁‐ATPase β‐subunit conferring resistance to aurovertin
  FEBS Letters, 1989
• The mitochondrial ATP synthase inhibitor protein binds near the C‐terminus of the F₁ β‐subunit
  FEBS Letters, 1988
• On the rate of F₁‐ATPase turnover during ATP hydrolysis by the single catalytic site Evidence that hydrolysis with a slow rate of product release does not occur at the alternating active site
  FEBS Letters, 1987
• Invitro mutated β subunits from the F1-ATPase of the thermophilic bacterium, PS3, containing glutamine in place of glutamic acid in positions 190 or 201 assembles with the α and γ subunits to produce inactive complexes
  Biochemical and Biophysical Research Communications, 1987
• Structure of the complex of yeast adenylate kinase with the inhibitor P1,P5-di(adenosine-5′-)pentaphosphate at 2.6 Å resolution
  Journal of Molecular Biology, 1987
• Structure of the nucleotide‐binding domain in the β‐subunit of Escherichia coli F₁‐ATPase
  FEBS Letters, 1986
• The DCCD-reactive aspartyl-residue of subunit c from the Escherichiacoli ATP-synthase is important for the conformation of FO
  Biochemical and Biophysical Research Communications, 1984
• Nucleotide sequence of the genes for β and ε subunits of proton-translocating ATPase from Escherichia coli
  Biochemical and Biophysical Research Communications, 1982