Catalytic cooperativity of beef heart mitochondrial F1-ATPase revealed by using 2′,3′-O-(2,4,6-trinitrophenyl)-ATP as a substrate; an indication of mutually activating catalytic sites

This publication has 18 references indexed in Scilit:

• Adenine nucleotide binding at a noncatalytic site of mitochondrial F1-ATPase accelerates a magnesium- and ADP-dependent inactivation during ATP hydrolysis
  Biochemistry, 1992
• Fluoroaluminum and fluoroberyllium nucleoside diphosphate complexes as probes of the enzymic mechanism of the mitochondrial F1-ATPase
  Biochemistry, 1991
• Hydrolysis of ATP by F1 can be described only on the basis of a dual-site mechanism
  Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1991
• Activation/inactivation and uni-site catalysis by the reconstituted ATP-synthase from chloroplasts
  Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1990
• Kinetic analysis of proton translocation catalyzed by F0 F1 ATPase
  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
• Demonstration of two exchangeable non-catalytic and two cooperative catalytic sites in isolated bovine heart mitochondrial F1, using the photoaffinity labels [2-3H]8-azido-ATP and [2-3H]8-azido-ADP
  Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1986
• Kinetics of ATP hydrolysis by F1-ATPase and the effects of anion activation, removal of tightly bound nucleotides, and partial inhibition of the ATPase by covalent modification
  Biochemistry, 1984
• Azidonaphthoyl‐ADP: a specific photolabel for the high‐affinity nucleotide‐binding sites of F₁‐ATPase
  European Journal of Biochemistry, 1984
• Interaction of photoreactive and fluorescent nucleotides with chloroplast coupling factor 1
  Biochemistry, 1979