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Related Concept Videos

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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SN1 Reaction: Mechanism02:25

SN1 Reaction: Mechanism

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Kinetic studies of ionization of a tertiary halide in a protic solvent suggest that only the substrate participates in the rate-determining step (slow step). The nucleophile is involved only after the slowest step. The SN1 reaction takes place in a multiple-step mechanism. 
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The Electron Transport Chain01:30

The Electron Transport Chain

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The electron transport chain or oxidative phosphorylation is an exothermic process in which free energy released during electron transfer reactions is coupled to ATP synthesis. This process is a significant source of energy in aerobic cells, and therefore inhibitors of the electron transport chain can be detrimental to the cell's metabolic processes.
Inhibitors of the electron transport chain
Rotenone, a widely used pesticide, prevents electron transfer from Fe-S cluster to ubiquinone or Q...
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Hydrolysis of ATP01:08

Hydrolysis of ATP

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The bonds of adenosine triphosphate (ATP) can be broken through the addition of water, releasing one or two phosphate groups in an exergonic process called hydrolysis. This reaction liberates the energy in the bonds for use in the cell—for instance, to synthesize proteins from amino acids.
If one phosphate group is removed, a molecule of ADP—adenosine diphosphate—remains, along with inorganic phosphate. ADP can be further hydrolyzed to AMP—adenosine...
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Chemiosmosis01:32

Chemiosmosis

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Oxidative phosphorylation is a highly efficient process that generates large amounts of adenosine triphosphate (ATP), the basic unit of energy that drives many cellular processes. Oxidative phosphorylation involves two processes— the electron transport chain and chemiosmosis.
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The electron transport chain involves a series of protein complexes on the inner mitochondrial membrane that undergo a series of redox reactions. At the end of this chain, the electrons...
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Related Experiment Video

Updated: Aug 20, 2025

Biochemical Assays for Analyzing Activities of ATP-dependent Chromatin Remodeling Enzymes
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H2A.Z deposition by SWR1C involves multiple ATP-dependent steps.

Jiayi Fan1,2, Andrew T Moreno3, Alexander S Baier1,4

  • 1Program in Molecular Medicine, University of Massachusetts Chan Medical School, Worcester, MA, 01605, USA.

Nature Communications
|November 17, 2022
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Summary

Histone variant H2A.Z deposition involves three ATP-dependent phases. The chromatin remodeler SWR1C uses ATP for nucleosome editing, priming, and H2A/H2B dimer release, enabling precise genomic regulation.

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Area of Science:

  • Chromatin biology
  • Molecular genetics
  • Biochemistry

Background:

  • Histone variant H2A.Z is crucial for nucleosomes at protein-coding genes.
  • ATP-dependent chromatin remodelers, like yeast SWR1C, mediate H2A.Z deposition.
  • The mechanism of ATP utilization by these remodelers is not fully understood.

Purpose of the Study:

  • To elucidate the ATP-dependent mechanism of H2A.Z deposition by SWR1C.
  • To identify distinct phases of the nucleosome editing reaction.
  • To understand how ATP concentration influences the reaction rates.

Main Methods:

  • Single-molecule and ensemble biochemical assays.
  • Real-time analysis of nucleosome remodeling events.
  • Investigation of ATP concentration effects on reaction kinetics.

Main Results:

  • Identified three distinct ATP-dependent phases in H2A.Z deposition.
  • Observed an initial ATP-dependent priming step involving DNA unwrapping and octamer deformation.
  • Demonstrated that both priming and H2A/H2B dimer release rates are sensitive to ATP concentration.

Conclusions:

  • The H2A.Z deposition reaction proceeds through a complex, multi-phase pathway.
  • ATP hydrolysis drives specific conformational changes and histone exchange.
  • The reaction's sensitivity to ATP offers regulatory control points for H2A.Z localization.