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Related Concept Videos

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...
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 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...
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...
Chemiosmosis01:32

Chemiosmosis

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.
Electron Transport Chain
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Updated: Jun 20, 2026

Light-driven Molecular Motors on Surfaces for Single Molecular Imaging
08:40

Light-driven Molecular Motors on Surfaces for Single Molecular Imaging

Published on: March 13, 2019

Structural dynamics of light-driven proton pumps.

Magnus Andersson1, Erik Malmerberg, Sebastian Westenhoff

  • 1Department of Chemical and Biological Engineering, Chalmers University of Technology, Göteborg, Sweden.

Structure (London, England : 1993)
|September 15, 2009
PubMed
Summary
This summary is machine-generated.

Bacteriorhodopsin and proteorhodopsin proton pumps use light energy to move protons. Time-resolved X-ray scattering reveals key helical motions and three states crucial for their light-driven function.

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Proton Transfer and Protein Conformation Dynamics in Photosensitive Proteins by Time-resolved Step-scan Fourier-transform Infrared Spectroscopy
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Single Liposome Measurements for the Study of Proton-Pumping Membrane Enzymes Using Electrochemistry and Fluorescent Microscopy
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Single Liposome Measurements for the Study of Proton-Pumping Membrane Enzymes Using Electrochemistry and Fluorescent Microscopy

Published on: February 21, 2019

Area of Science:

  • Biophysics
  • Structural Biology
  • Photochemistry

Background:

  • Bacteriorhodopsin and proteorhodopsin are microbial proton pumps.
  • They utilize a retinal chromophore and a protonated Schiff base.
  • Photon absorption triggers isomerization and conformational changes for proton transport.

Purpose of the Study:

  • To visualize real-time helical motions during proton pumping.
  • To understand the dynamics of bacteriorhodopsin and proteorhodopsin photocycles.
  • To identify key conformational states and their associated movements.

Main Methods:

  • Time-resolved wide-angle X-ray scattering (TR-WAXS).
  • Real-time observation of protein dynamics.
  • Analysis of helical motions in proton pumps.

Main Results:

  • Three distinct conformational states characterize the photocycles.
  • Significant motions in helix F (cytoplasmic) and helix C (extracellular) occur.
  • These motions precede and intensify after proton transfer.

Conclusions:

  • The study simplifies structural descriptions of bacteriorhodopsin.
  • Shared dynamical principles govern proton pumping in both proteins.
  • Identified motions are critical for vectorial proton transport.