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ATP Synthase: Mechanism01:48

ATP Synthase: Mechanism

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In animals, the mitochondrial F1F0 ATP synthase is the key protein that synthesizes ATP molecules through a complex catalytic mechanism. While the nuclear genome encodes the majority of ATP synthase subunits, the mitochondrial genome encodes some of the enzyme's most critical components. The formation of this multi-subunit enzyme is a complex multi-step process regulated at the level of transcription, translation, and assembly. Defects in one or more of these steps can result in decreased...
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ATP Synthase: Structure01:18

ATP Synthase: Structure

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ATP synthase or ATPase is among the most conserved proteins found in bacteria, mammals, and plants. This enzyme can catalyze a forward reaction in response to the electrochemical gradient, producing ATP from ADP and inorganic phosphate. ATP synthase can also work in a reverse direction by hydrolyzing ATP and generating an electrochemical gradient. Different forms of ATP synthases have evolved special features to meet the specific demands of the cell. Based on their specific feature, ATP...
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ATP Driven Pumps I: An Overview01:27

ATP Driven Pumps I: An Overview

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ATP-driven pumps, also known as transport ATPases, are integral membrane proteins. They have binding sites for ATP located on the membrane's cytosolic side and the ion-conducting domain in the transmembrane region. These pumps use the free energy released from ATP hydrolysis to move the solutes across cell membranes against an electrochemical gradient.
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Chemiosmosis and ATP Synthesis01:22

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The electron transport chain is a critical component of cellular respiration, occurring in the inner mitochondrial membrane. It facilitates the transfer of high-energy electrons from reduced cofactors NADH and FADH₂ to molecular oxygen, the final electron acceptor. This transfer of electrons through a series of protein complexes is tightly coupled to the translocation of protons across the membrane, generating a proton gradient essential for ATP synthesis.Electron Flow and Proton...
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ATP Energy Storage and Release01:31

ATP Energy Storage and Release

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ATP is a highly unstable molecule. Unless quickly used to perform work, ATP spontaneously dissociates into ADP and inorganic phosphate (Pi), and the free energy released during this process is lost as heat. The energy released by ATP hydrolysis is used to perform work inside the cell and depends on a strategy called energy coupling. Cells couple the exergonic reaction of ATP hydrolysis with endergonic reactions, allowing them to proceed.
One example of energy coupling using ATP involves a...
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Mechanical Protein Functions01:58

Mechanical Protein Functions

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Proteins perform many mechanical functions in a cell. These proteins can be classified into two general categories- proteins that generate mechanical forces and proteins that are subjected to mechanical forces. Proteins providing mechanical support to the structure of the cell, such as keratin, are subjected to mechanical force, whereas proteins involved in cell movement and transport of molecules across cell membranes, such as an ion pump, are examples of generating mechanical force. 
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  1. Home
  3. Nucleotide Exchange Mechanism Involving Angle-dependent Rate Constants Extracted From F1-atpase Single-molecule Rotation Trajectories.
  1. Home
  3. Nucleotide Exchange Mechanism Involving Angle-dependent Rate Constants Extracted From F1-atpase Single-molecule Rotation Trajectories.

Related Experiment Video

Use of Stopped-Flow Fluorescence and Labeled Nucleotides to Analyze the ATP Turnover Cycle of Kinesins
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Use of Stopped-Flow Fluorescence and Labeled Nucleotides to Analyze the ATP Turnover Cycle of Kinesins

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Nucleotide Exchange Mechanism Involving Angle-Dependent Rate Constants Extracted from F1-ATPase Single-Molecule

Sándor Volkán-Kacsó1, Ricardo A Matute2, Maria-Elisabeth Michel-Beyerle3

  • 1Segerstrom Science Center, Azusa Pacific University, 901 E. Alosta Ave., Azusa, California 91702, United States.

The Journal of Physical Chemistry. B
|November 10, 2025

View abstract on PubMed

Summary
This summary is machine-generated.

Researchers explored the F1-ATPase enzyme

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Area of Science:

  • Biochemistry and Molecular Biology
  • Enzyme kinetics
  • Biophysical chemistry

Background:

  • F1-ATPase is a rotary motor enzyme crucial for cellular energy production.
  • Previous studies suggested a million-fold acceleration in ADP release due to concerted ATP binding and ADP release.
  • Understanding the kinetics of nucleotide exchange is vital for elucidating F1-ATPase function.

Purpose of the Study:

  • To investigate the relationship between concerted nucleotide exchange and experimental data for F1-ATPase.
  • To develop a theoretical framework explaining the observed kinetics of F1-ATPase.
  • To uncover the underlying mechanisms driving the accelerated ADP release.

Main Methods:

  • Developed a theory of reaction kinetics to model F1-ATPase rotational cycles.
  • Extracted angle-dependent rate constants for nucleotide binding and release from single-molecule data.
  • Integrated these rate constants into a unified kinetic scheme to derive analytical equations for nucleotide occupancy.

    • Main Results:

    • The developed kinetic scheme accurately predicts nucleotide occupancy across a wide range of ATP concentrations.
    • Identified correlated conformational changes in the F1-ATPase ring as the basis for the concerted mechanism.
    • Demonstrated that the kinetic signature of this mechanism is an angle-dependent function of rate constants, independent of ATP concentration.

    Conclusions:

    • The concerted nucleotide exchange mechanism in F1-ATPase is driven by coordinated conformational dynamics.
    • This mechanism provides a unified explanation for accelerated ADP release observed in various experimental settings.
    • The findings offer novel insights into the intricate rotary mechanism of F1-ATPase.