Catalytic Activities of α3β3γ Complexes of F1-ATPase with 1, 2, or 3 Incompetent Catalytic Sites

This publication has 31 references indexed in Scilit:

• A minimum catalytic unit of F₁‐ATPase shows non‐cooperative ATPase activity inherent in a single catalytic site with a K_m 70 μM
  FEBS Letters, 1995
• Structural model of the ATP‐binding domain of the F₁‐β subunit based on analogy to the RecA protein
  FEBS Letters, 1994
• Spatial precision of a catalytic carboxylate of F₁‐ATPase β subunit probed by introducing different carboxylate‐containing side chains
  FEBS Letters, 1994
• Fluoroaluminum and fluoroberyllium nucleoside diphosphate complexes as probes of the enzymic mechanism of the mitochondrial F1-ATPase
  Biochemistry, 1991
• [6] Efficient site-directed mutagenesis using uracil-containing DNA
  Published by Elsevier ,1991
• 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
• Azidonaphthoyl‐ADP: a specific photolabel for the high‐affinity nucleotide‐binding sites of F₁‐ATPase
  European Journal of Biochemistry, 1984
• A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
  Analytical Biochemistry, 1976
• Corrigendum
  FEBS Letters, 1975
• Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
  Nature, 1970