From Human Serum Albumin to Rotational Catalysis by ATP Synthase

@article{Boyer1995FromHS,
  title={From Human Serum Albumin to Rotational Catalysis by ATP Synthase},
  author={P. Boyer},
  journal={The FASEB Journal},
  year={1995},
  volume={9}
}
  • P. Boyer
  • Published 1995
  • Biology, Medicine
  • The FASEB Journal
  • Deadline: December 1, 1995 MILESTONES IN BIOLOGICAL RESEARCH Vol. 9 April1995 The FASEB Journal 561 translocation toATP synthesis and toactive transport. FEBS LeO. 58, 1-6 9. Cross, R. L.,Grubmeyer, C., and Penefsky, H. S. (1982)Mechanism of AP hydrolysis by beef heart mitochondrial AFPase: Rate enhancements resulting fromcooperative interactins betswen multiple catalytic sites.] Blot Chem. 257, 12101-12105 10. Boyer, P. D. (1979) The binding change mechanism of ATP synthesis. InMembrane… CONTINUE READING
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    References

    SHOWING 1-10 OF 22 REFERENCES
    Structure at 2.8 Â resolution of F1-ATPase from bovine heart mitochondria
    • 2,694
    • Highly Influential
    Oxygen-18 probes of enzymic reactions of phosphate compounds.
    • 67
    A chemiosmotic molecular mechanism for proton‐translocating adenosine triphosphatases
    • 208
    Evidence that energizaion of the chloroplast ATP synthase favors ATP fbrmation at the tight binding catalytic site and increases the affinity for ADP at another catalytic site. j Blot Chem
    • 1993
    Mitochondrial ATP Synthase: Quaternaiy structure of the F, moiety at 3.6 A determined by X-ray diffraction. j Blot. C/ins
    • 1991
    Mitochondrial ATP Synthase: Quaternaiy structure ofthe F, moiety at 3.6 A determined by X-ray diffraction
    • j Blot. C/ins
    • 1991