Nucleotide binding sites on beef heart mitochondrial F1-ATPase. Cooperative interactions between sites and specificity of noncatalytic sites.

This publication has 57 references indexed in Scilit:

• The ‘non‐exchangeable’ nucleotides of F₁‐F₀)ATP synthase
  FEBS Letters, 1993
• The mechanism of stimulation of MgATPase activity of chloroplast F₁‐ATPase by non‐catalytic adeninenucleotide binding
  European Journal of Biochemistry, 1992
• When beef‐heart mitochondrial F₁‐ATPase is inhibited by inhibitor protein a nucleotide is trapped in one of the catalytic sites
  European Journal of Biochemistry, 1991
• Characteristics of the combination of inhibitory magnesium and azide with the F1 ATPase from chloroplasts
  Biochemistry, 1991
• Guanosine and formycin triphosphates bind at non‐catalytic nucleotide binding sites of CF₁ ATPase and inhibit ATP hydrolysis
  FEBS Letters, 1990
• Three adenine nucleotide binding sites in F₁‐F₀ mitochondrial ATPase as revealed by presteady‐state and steady‐state kinetics of ATP hydrolysis Evidence for two inhibitory ADP‐specific noncatalytic sites
  FEBS Letters, 1988
• The complex of mitochondrial F₁‐ATPase with the natural inhibitor protein is unable to catalyze single‐site ATP hydrolysis
  FEBS Letters, 1988
• Tightly bound adenosine diphosphate, which inhibits the activity of mitochondrial F₁‐ATPase, is located at the catalytic site of the enzyme
  FEBS Letters, 1985
• The interactions of coupling ATPases with nucleotides
  Biochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics, 1978
• Active/inactive state transitions of mitochondrial ATPase molecules influenced by Mg²⁺, anions and aurovertin
  FEBS Letters, 1975