Conformational Changes in the Escherichia coli ATP Synthase (ECF1F0) Monitored by Nucleotide-dependent Differences in the Reactivity of Cys-87 of the γ Subunit in the Mutant βGlu-381 → Ala

This publication has 28 references indexed in Scilit:

• Differentiation of Catalytic Sites on Escherichia coli F₁ATPase by Laser Photoactivated Labeling with [³H]-2-Azido-ATP Using the Mutant βGlu381Cys:εSer108Cys To Identify Different β Subunits by Their Interactions with γ and ε Subunits
  Biochemistry, 1996
• Asymmetry of Escherichia coli F1-ATPase as a Function of the Interaction of α-β Subunit Pairs with the γ and ∊ Subunits
  Published by Elsevier ,1995
• The γ subunit in the Escherichia coli ATP synthase complex (ECF₁F₀) extends through the stalk and contacts the c subunits of the F₀ part
  FEBS Letters, 1995
• Disulfide Bond Formation between the COOH-terminal Domain of the β Subunits and the γ and ε Subunits of the Escherichia coli F1-ATPase
  Published by Elsevier ,1995
• ATP binding causes a conformational change in the .gamma. subunit of the Escherichia coli F1ATPase which is reversed on bond cleavage
  Biochemistry, 1994
• Coupling between catalytic sites and the proton channel in F1F0-type ATPases
  Trends in Biochemical Sciences, 1994
• Structure-function relationships of domains of the δ subunit in Escherichia coli adenosine triphosphatase
  Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1991
• The stalk connecting the F₁ and F₀ domains of ATP synthase visualized by electron microscopy of unstained specimens
  FEBS Letters, 1987
• Interconversion of high and low ATPase activity forms of ECF1 by the detergent lauryldimethylamine oxide
  Biochemistry, 1984
• Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
  Nature, 1970