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  • Thomas M Duncan, Vladimir V. Bulygin, Yuxiang Zhou, Marcia Hutcheon, Richard L. Cross
  • Chemistry, Medicine
  • Proceedings of the National Academy of Sciences…
  • 1995 (First Publication: 21 November 1995)
  • During oxidative and photo-phosphorylation, F0F1-ATP synthases couple the movement of protons down an electrochemical gradient to the synthesis of ATP. One proposed mechanistic feature that hasContinue Reading
  • Paul David Boyer, Richard L. Cross, William E. Momsen
  • Chemistry, Medicine
  • Proceedings of the National Academy of Sciences…
  • 1973 (First Publication: 1 October 1973)
  • 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 arrowContinue Reading
  • Richard L. Cross, William E. Kohlbrenner
  • Chemistry, Medicine
  • The Journal of biological chemistry
  • 1978 (First Publication: 25 July 1978)
  • Results are presented that confirm and extend earlier findings that efrapeptin is a potent inhibitor of oxidative phosphorylation. Binding of efrapeptin is shown to be reversible, and a dissociationContinue Reading
  • Pia D. Vogel, Richard L. Cross
  • Chemistry, Medicine
  • The Journal of biological chemistry
  • 1991 (First Publication: 5 April 1991)
  • Nucleotide-depleted mitochondrial F1-ATPase (F1[0,0]) is inhibited by the diadenosine oligophosphate compounds, AP4A, AP5A, and AP6A (where APxA stands for 5',5'-diadenosine oligophosphates having aContinue Reading
  • Ren Rao, D. Cunningham, Richard L. Cross, Alan E. Senior
  • Chemistry, Medicine
  • The Journal of biological chemistry
  • 1988 (First Publication: 25 April 1988)
  • Pyridoxal 5'-diphospho-5'-adenosine (PLP-AMP), an adenine nucleotide affinity analog, was found to bind in a saturable fashion to isolated alpha-subunit from Escherichia coli F1-ATPase with aContinue Reading
  • Richard L. Cross, Paul David Boyer
  • Chemistry, Medicine
  • Biochemistry
  • 1975 (First Publication: 28 January 1975)
  • Evidence is presented that extends and amplifies the concept that in oxidative phosphorylation energy input serves to bring about release of ATP formed at a catalytic site by reversal of hydrolysis.Continue Reading