Structural Asymmetry of F1-ATPase Caused by the γ Subunit Generates a High Affinity Nucleotide Binding Site

This publication has 28 references indexed in Scilit:

• 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
• In Vitro Assembly of the Core Catalytic Complex of the Chloroplast ATP Synthase
  Journal of Biological Chemistry, 1995
• Structure at 2.8 Â resolution of F1-ATPase from bovine heart mitochondria
  Nature, 1994
• Asymmetry of the Three Catalytic Sites on β Subunits of TF1 from a Thermophilic Bacillus Strain PS31
  The Journal of Biochemistry, 1994
• The α1β1 heterodimer, the unit of ATP synthase
  Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1991
• Electron microscopy of the reconstituted complexes of the F₁‐ATPase with various subunit constitution revealed the location of the γ subunit in the central cavity of the molecule
  FEBS Letters, 1990
• Cryoelectron microscopy of Escherichia coli F1 adenosinetriphosphatase decorated with monoclonal antibodies to individual subunits of the complex
  Biochemistry, 1989
• ADP Binding to TF1 and Its Subunits Induces Ultraviolet Spectral Changes1
  The Journal of Biochemistry, 1986
• Biological activities and spectroscopic properties of chromophoric and fluorescent analogs of adenine nucleoside and nucleotides, 2′,3′-O-(2,4,6-trinitrocyclohexadienylidene) adenosine derivatives
  Biochimica et Biophysica Acta (BBA) - General Subjects, 1982
• Preparation and properties of 2′(or 3′)-O-(2,4,6-trinitrophenyl) adenosine 5′-triphosphate, an analog of adenosine triphosphate
  Biochimica et Biophysica Acta (BBA) - General Subjects, 1973