Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

ATP Synthase: Structure01:18

ATP Synthase: Structure

16.9K
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...
16.9K
ATP Synthase: Mechanism01:48

ATP Synthase: Mechanism

18.3K
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...
18.3K
ATP Driven Pumps I: An Overview01:27

ATP Driven Pumps I: An Overview

10.3K
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...
10.3K
ATP Driven Pumps III: V-type Pumps01:30

ATP Driven Pumps III: V-type Pumps

5.1K
V-type pumps are ATP-driven pumps found in the vacuolar membranes of plants, yeast, endosomal and lysosomal membranes of animal cells, plasma membranes of a few specialized eukaryotic cells, and some prokaryotes. They are also known as the V1Vo-ATPase, that couple ATP hydrolysis to transport protons against a concentration gradient.
The peripheral or cytosolic V1 domain with eight subunits is involved in ATP hydrolysis. The integral or transmembrane V0 domain containing at least five subunits...
5.1K
ATP Driven Pumps II: P-type Pumps01:34

ATP Driven Pumps II: P-type Pumps

6.7K
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...
6.7K
Chemiosmosis and ATP Synthesis01:22

Chemiosmosis and ATP Synthesis

2.9K
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...
2.9K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Let there be light: how to use photoswitchable cross-linker to reprogram proteins.

Biochemical Society transactions·2017
Same author

Design of Light-Controlled Protein Conformations and Functions.

Methods in molecular biology (Clifton, N.J.)·2016
Same author

A Model for the Molecular Mechanism of an Engineered Light-Driven Protein Machine.

Structure (London, England : 1993)·2016
Same author

Reprogramming an ATP-driven protein machine into a light-gated nanocage.

Nature nanotechnology·2013
Same author

Dynamics of light-induced activation in the PAS domain proteins LOV2 and PYP probed by time-resolved tryptophan fluorescence.

Biochemistry·2010
Same author

Strong hydrogen bond between glutamic acid 46 and chromophore leads to the intermediate spectral form and excited state proton transfer in the Y42F mutant of the photoreceptor photoactive yellow protein.

Biochemistry·2009

Related Experiment Video

Updated: Mar 16, 2026

Isolation of F1-ATPase from the Parasitic Protist Trypanosoma brucei
08:44

Isolation of F1-ATPase from the Parasitic Protist Trypanosoma brucei

Published on: January 22, 2019

7.8K

Engineering a light-controlled F1 ATPase using structure-based protein design.

Daniel Hoersch1

  • 1Experimental Molecular Biophysics, Department of Physics, Freie Universität Berlin , Berlin , Germany.

Peerj
|August 23, 2016
PubMed
Summary

Researchers engineered the F1 ATPase nanomotor using a photoswitchable crosslinker. This synthetic ATPase

Keywords:
AzobenzeneLight controlMolecular machineProtein design

More Related Videos

Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation
08:00

Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation

Published on: October 4, 2024

1.2K
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

31.2K

Related Experiment Videos

Last Updated: Mar 16, 2026

Isolation of F1-ATPase from the Parasitic Protist Trypanosoma brucei
08:44

Isolation of F1-ATPase from the Parasitic Protist Trypanosoma brucei

Published on: January 22, 2019

7.8K
Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation
08:00

Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation

Published on: October 4, 2024

1.2K
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

31.2K

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Nanotechnology

Background:

  • ATP synthase's F1 sub-complex functions as a highly efficient biological nanomotor.
  • This nanomotor converts chemical energy from ATP hydrolysis into mechanical work.
  • Understanding its mechanics is crucial for bio-inspired machine design.

Purpose of the Study:

  • To probe the mechanics of the F1 ATPase nanomotor.
  • To engineer a synthetic ATPase with light-controlled activity.
  • To explore structure-based protein design for dynamic constraint.

Main Methods:

  • Employed a structure-based protein design approach to re-engineer the E. coli F1 ATPase active site.
  • Incorporated a site-specific, photoswitchable crosslinker.
  • Modulated inter-atomic distances between α and β subunits using light of different wavelengths.

Main Results:

  • Crosslinking reduced ATP hydrolysis activity in four engineered designs.
  • One design exhibited reversibly modulated ATPase activity upon illumination with near-UV and blue light.
  • Demonstrated light-induced dynamic constraint on the nanomotor's subunits.

Conclusions:

  • The study presents a novel method for creating light-controllable biological nanomachines.
  • This work is a foundational step towards designing light-controlled nanomachines using biological components.
  • Highlights the potential of protein engineering for creating synthetic molecular machines.