Oxidation of the α3(βD311C/R333C)3γ Subcomplex of the Thermophilic Bacillus PS3 F1-ATPase Indicates That Only Two β Subunits Can Exist in the Closed Conformation Simultaneously

This publication has 22 references indexed in Scilit:

• Cross-linking of Two β Subunits in the Closed Conformation in F1-ATPase
  Published by Elsevier ,1999
• F₁-ATPase: A Molecular Motor That Hydrolyzes ATP with Sequential Opening and Closing of Catalytic Sites Coupled to Rotation of Its γ Subunit
  Accounts of Chemical Research, 1998
• F1-ATPase Is a Highly Efficient Molecular Motor that Rotates with Discrete 120° Steps
  Cell, 1998
• Mutations in the Nucleotide Binding Domain of the α Subunits of the F₁-ATPase from Thermophilic Bacillus PS3 That Affect Cross-Talk between Nucleotide Binding Sites
  Biochemistry, 1998
• The crystal structure of the nucleotide-free α3β3 subcomplex of F1-ATPase from the thermophilic Bacillus PS3 is a symmetric trimer
  Structure, 1997
• Direct observation of the rotation of F1-ATPase
  Nature, 1997
• The Trapping of Different Conformations of the Escherichia coli F1 ATPase by Disulfide Bond Formation
  Journal of Biological Chemistry, 1996
• The .alpha.3.beta.3.gamma. complex of the F1-ATPase from thermophilic Bacillus PS3 containing the .alpha.D261N substitution fails to dissociate inhibitory MgADP from a catalytic site when ATP binds to noncatalytic sites
  Biochemistry, 1995
• Expression of the wild-type and the Cys-/Trp-less α3β3γ complex of thermophilic F1-ATPase in Escherichia coli
  Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1995
• A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
  Analytical Biochemistry, 1976