Cited by 120ATP Synthase and ATPases ResearchProtein Structure and DynamicsForce Microscopy Techniques and Applications

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The mechanism of rotating proton pumping ATPases

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Nakanishi-Matsui, Mayumi, Sekiya, Mizuki, Nakamoto, Robert K., Futai, Masamitsu·2010·Biochimica et Biophysica Acta (BBA) - Bioenergetics

DOI 10.1016/j.bbabio.2010.02.014

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Abstract

Two proton pumps, the F-ATPase (ATP synthase, FoF1) and the V-ATPase (endomembrane proton pump), have different physiological functions, but are similar in subunit structure and mechanism. They are composed of a membrane extrinsic (F1 or V1) and a membrane intrinsic (Fo or Vo) sector, and couple catalysis of ATP synthesis or hydrolysis to proton transport by a rotational mechanism. The mechanism of rotation has been extensively studied by kinetic, thermodynamic and physiological approaches. Techniques for observing subunit rotation have been developed. Observations of micron-length actin filaments, or polystyrene or gold beads attached to rotor subunits have been highly informative of the rotational behavior of ATP hydrolysis-driven rotation. Single molecule FRET experiments between fluorescent probes attached to rotor and stator subunits have been used effectively in monitoring proton motive force-driven rotation in the ATP synthesis reaction. By using small gold beads with diameters of 40-60 nm, the E. coli F1 sector was found to rotate at surprisingly high speeds (>400 rps). This experimental system was used to assess the kinetics and thermodynamics of mutant enzymes. The results revealed that the enzymatic reaction steps and the timing of the domain interactions among the beta subunits, or between the beta and gamma subunits, are coordinated in a manner that lowers the activation energy for all steps and avoids deep energy wells through the rotationally-coupled steady-state reaction. In this review, we focus on the mechanism of steady-state F1-ATPase rotation, which maximizes the coupling efficiency between catalysis and rotation.

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Authors: Nakanishi-Matsui, M., Sekiya, M., Nakamoto, R. K., & Futai, M.
Affiliations: Iwate Medical University (JP)
University of Virginia (US)
ORCID: Sekiya, Mizuki
Nakamoto, Robert K.
Venue: Biochimica et Biophysica Acta (BBA) - Bioenergetics
Publisher: Elsevier BV
Published: 2010-08
Volume: 1797
Issue: 8
Pages: 1343-1352
ISSN: 0005-2728 (ISSN-L)
DOI: 10.1016/j.bbabio.2010.02.014
OpenAlex: W2140969249
Cited by: 120
References: 103
Citations by year: 2026: 3 · 2025: 2 · 2024: 3 · 2023: 23 · 2022: 2 · 2021: 8 · 2020: 7 · 2019: 2 · 2018: 5 · 2017: 6 · 2016: 8 · 2015: 7 · 2014: 7 · 2013: 10 · 2012: 11
FWCI: 1.04
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 1082 d)
doi.org/10.15223/policy-017 (stm-asf)
doi.org/10.15223/policy-037 (stm-asf)
doi.org/10.15223/policy-012 (stm-asf)
doi.org/10.15223/policy-029 (stm-asf)
doi.org/10.15223/policy-004 (stm-asf)
Locations: Biochimica et Biophysica Acta (BBA) - Bioenergetics (publishedVersion)
PubMed (publishedVersion)
Funders: CREST (Core Research for Evolutional Science and Technology)
JST (Japan Science and Technology Agency)
Japanese Ministry of Education, Culture, and Science
Terumo Life Science Foundation
Japan Foundation for Applied Enzymology
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Physical Sciences › Physics and Astronomy › Atomic and Molecular Physics, and Optics › Force Microscopy Techniques and Applications
Keywords: F1-ATPase, V-ATPase, proton-pumping ATPase, ATP production, single-molecule FRET, Escherichia coli
MeSH terms: Adenosine Triphosphate, Animals, Catalysis, Proton-Translocating ATPases, Humans, Rotation, Thermodynamics, Vacuolar Proton-Translocating ATPases

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