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Related Concept Videos

ATP Synthase: Structure01:18

ATP Synthase: Structure

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...
ATP Synthase: Mechanism01:48

ATP Synthase: Mechanism

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 ATP...
ATP Driven Pumps II: P-type Pumps01:34

ATP Driven Pumps II: P-type Pumps

The P-type pumps are a large family of integral membrane transporter ATPases. They are divided into five major types based on substrate specificity, from I to V.
A typical P-type pump has three cytosolic domains: nucleotide-binding (N), phosphorylation (P), and activator (A) domains. These domains are connected to the membrane-spanning helices by short amino acid segments. ATP hydrolysis and covalent phosphoenzyme intermediate formation are crucial parts of the catalytic cycle. At the highly...
Chemiosmosis and ATP Synthesis01:22

Chemiosmosis and ATP Synthesis

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...
ATP Driven Pumps I: An Overview01:27

ATP Driven Pumps I: An Overview

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.
There are four main types of ATP-driven pumps - P-type, V-type, F-type, and ABC transporter. All these pumps are of varying complexities and are...
Electron Transport Chain Components01:29

Electron Transport Chain Components

The electron transport chain (ETC) is a crucial metabolic pathway that facilitates energy conversion in prokaryotic and eukaryotic cells. In eukaryotes, the ETC comprises four membrane-associated protein complexes in the inner mitochondrial membrane. In prokaryotes, the ETC in the plasma membrane can vary in composition, with fewer or different complexes depending on the organism and environmental conditions. These complexes transfer electrons from electron donors, such as NADH and FADH2, to...

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Related Experiment Video

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Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography
10:39

Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography

Published on: September 14, 2014

Electric field driven torque in ATP synthase.

John H Miller1, Kimal I Rajapakshe, Hans L Infante

  • 1Department of Physics and Texas Center for Superconductivity, University of Houston, Houston, Texas, United States of America.

Plos One
|September 17, 2013
PubMed
Summary
This summary is machine-generated.

This study proposes a mechanism for how electric fields drive the FO-ATP synthase rotary motor. The model links proton motive force to ATP production rates, revealing an inverse scaling with proton binding sites.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Bioenergetics

Background:

  • FO-ATP synthase is a crucial rotary motor enzyme.
  • It converts ion potential energy into mechanical work for ATP synthesis.
  • Understanding its precise mechanism is key to bioenergetics.

Purpose of the Study:

  • To propose a novel mechanism for FO-ATP synthase rotation.
  • To model the relationship between electric fields, proton motive force, and torque.
  • To compute ATP production rates based on biophysical principles.

Main Methods:

  • Development of a theoretical model for FO-ATP synthase function.
  • Analysis of electric field interactions with the c-ring's charge distribution.
  • Application of Brownian motion analogy to calculate ATP synthesis rates.

Main Results:

  • Electric fields from proton channels drive c-ring rotation via asymmetric charge interactions.
  • A scaling relationship between time-averaged torque and proton motive force is predicted.
  • ATP production rate exhibits a minimum dependency on proton motive force, inversely scaling with c-ring binding sites.

Conclusions:

  • The proposed electric field mechanism provides a framework for FO-ATP synthase function.
  • Proton motive force and c-ring structure are critical determinants of ATP synthesis efficiency.
  • Mutations affecting proton channels can impair enzyme function.