The cysteine introduced into the alpha subunit of the Escherichia coli F1-ATPase by the mutation alpha R376C is near the alpha-beta subunit interface and close to a noncatalytic nucleotide binding site.

This publication has 36 references indexed in Scilit:

• Introduction of reactive cysteine residues in the .epsilon. subunit of Escherichia coli F1 ATPase, modification of these sites with (azidotetrafluorophenyl)maleimides, and examination of changes in the binding of the .epsilon. subunit when different nucleotides are in catalytic sites
  Biochemistry, 1992
• Nucleotide-dependent and dicyclohexylcarbodiimide-sensitive conformational changes in the .epsilon. subunit of Escherichia coli ATP synthase
  Biochemistry, 1991
• Monoclonal antibody modification of the ATPase activity of Escherichia coli F1 ATPase
  Biochemistry, 1990
• Activation/inactivation and uni-site catalysis by the reconstituted ATP-synthase from chloroplasts
  Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1990
• Molecular architecture of Escherichia coli F1 adenosinetriphosphatase
  Biochemistry, 1989
• Labeling of the ATP synthase of Escherichia coli from the head-group region of the lipid bilayer
  Biochemistry, 1987
• Specificity of the proton adenosine triphosphatase of Escherichia coli for adenine, guanine, and inosine nucleotides in catalysts and binding
  Biochemistry, 1984
• Inhibition of ATPase activity of E. coli F1 by the water-soluble carbodiimide EDC is due to modification of several carboxyls in the .beta. subunit
  Biochemistry, 1984
• Defective proton ATPase of uncA mutants of Escherichia coli. 5'-adenylyl 5'-imidodiphosphate binding and ATP hydrolysis
  Biochemistry, 1984
• Photophosphorylation by swiss-chard chloroplasts
  Biochimica et Biophysica Acta, 1959