• Publications
  • Influence
The ATP synthase--a splendid molecular machine.
  • P. Boyer
  • Chemistry, Medicine
  • Annual review of biochemistry
  • 1997
An X-ray structure of the F1 portion of the mitochondrial ATP synthase shows asymmetry and differences in nucleotide binding of the catalytic beta subunits that support the binding change mechanismExpand
  • 1,624
  • 64
  • PDF
The binding change mechanism for ATP synthase--some probabilities and possibilities.
  • P. Boyer
  • Chemistry, Medicine
  • Biochimica et biophysica acta
  • 8 January 1993
IV. Protein and synthase structure as related to mechanism . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 217 A. Protein structure . . . . . . . . . . . . . . . . . . . . . . . . . . .Expand
  • 887
  • 34
Kinetic analysis of enzyme reactions. II. The potassium activation and calcium inhibition of pyruvic phosphoferase.
Muscle pyruvic phosphoferase,l catalyzing the reaction PEPA + ADP a pyruvate + ATP,2 has been shown to require both Mg+ (3) and K+ or NHb+ ions (4-6) for maximum activity and to be strongly inhibitedExpand
  • 253
  • 5
  • PDF
A new concept for energy coupling in oxidative phosphorylation based on a molecular explanation of the oxygen exchange reactions.
The P(i) right arrow over left arrow HOH exchange reaction of oxidative phosphorylation is considerably less sensitive to uncouplers than the P(i) right arrow over left arrow ATP and ATP right arrowExpand
  • 258
  • 4
  • PDF
A model for conformational coupling of membrane potential and proton translocation to ATP synthesis and to active transport
  • P. Boyer
  • Chemistry, Medicine
  • FEBS letters
  • 15 October 1975
Acceptance of a membrane potential and/or a proton gradient as a possible means of transmitting energy from oxidations to ATP synthesis rests in part on a satisfactory hypothesis for how theExpand
  • 176
  • 4
Energization of active transport by Escherichia coli.
  • W. Klein, P. Boyer
  • Medicine, Chemistry
  • The Journal of biological chemistry
  • 25 November 1972
Abstract An activated membrane state necessary for the active transport of certain amino acids, carbohydrates, and cations by Escherichia coli can be generated by either oxidative energy or phosphateExpand
  • 131
  • 4
Catalytic site forms and controls in ATP synthase catalysis.
  • P. Boyer
  • Chemistry, Medicine
  • Biochimica et biophysica acta
  • 31 May 2000
A suggested minimal scheme for substrate binding by and interconversion of three forms of the catalytic sites of the ATP synthase is presented. Each binding change, that drives simultaneousExpand
  • 91
  • 4
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