Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Synthase (H(+) ATPase): coupling between catalysis, mechanical work, and proton translocation.

M Futai1, H Omote, Y Sambongi

  • 1Division of Biological Sciences, Institute of Scientific and Industrial Research, Osaka University, CREST, Japan Science and Technology Corporation, Ibaraki, 567-0047, Osaka, Japan. m-futai@sanken.osaka-u.ac.jp

Biochimica Et Biophysica Acta
|June 6, 2000
PubMed
Summary

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Different properties of two types of auxin-binding sites in membranes from maize coleoptiles.

Planta·2013
Same author

Multidrug and toxic compound extrusion (MATE)-type proteins as anchor transporters for the excretion of metabolic waste products and xenobiotics.

Xenobiotica; the fate of foreign compounds in biological systems·2008
Same author

Distinct expression patterns of different subunit isoforms of the V-ATPase in the rat epididymis.

Biology of reproduction·2005
Same author

A biological molecular motor, proton-translocating ATP synthase: multidisciplinary approach for a unique membrane enzyme.

Journal of bioenergetics and biomembranes·2004
Same author

[Functions of acidic compartments in mammalian system].

Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme·2002
Same author

Association of mouse sorting nexin 1 with early endosomes.

Journal of biochemistry·2001

ATP synthase (F(0)F(1)) uses proton gradients to create ATP. This study explores the catalytic mechanism of the beta subunit and the energy coupling role of the rotating gamma subunit in ATP synthesis.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Bioenergetics

Background:

  • ATP synthase (F(0)F(1)) is a crucial membrane enzyme responsible for cellular energy production.
  • Understanding its mechanism is key to comprehending fundamental biological processes.

Purpose of the Study:

  • To elucidate the catalytic mechanism within the beta subunit of the F(1) sector of ATP synthase.
  • To investigate the role of the gamma subunit in energy coupling and its rotation during catalysis.

Main Methods:

  • Utilized high-resolution structural studies.
  • Employed mutational analyses to probe enzyme function.

Main Results:

  • Detailed the catalytic mechanism of the beta subunit.

Related Experiment Videos

  • Highlighted the significance of the gamma subunit in energy transduction.
  • Provided insights into the rotational dynamics of the gamma subunit during ATP synthesis.

    • Conclusions:

    • The study enhances the understanding of ATP synthase's intricate mechanism.
    • The findings contribute to the knowledge of how electrochemical proton gradients drive ATP production via enzyme rotation.