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Related Concept Videos

ATP Driven Pumps I: An Overview01:27

ATP Driven Pumps I: An Overview

9.5K
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...
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ATP Driven Pumps III: V-type Pumps01:30

ATP Driven Pumps III: V-type Pumps

4.5K
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...
4.5K
ATP Driven Pumps II: P-type Pumps01:34

ATP Driven Pumps II: P-type Pumps

6.0K
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...
6.0K
ATP Synthase: Mechanism01:48

ATP Synthase: Mechanism

16.4K
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...
16.4K
Chemiosmosis and ATP Synthesis01:22

Chemiosmosis and ATP Synthesis

1.5K
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...
1.5K
Hydrolysis of ATP01:08

Hydrolysis of ATP

80.6K
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...
80.6K

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Related Experiment Video

Updated: Dec 26, 2025

Detergent-free Ultrafast Reconstitution of Membrane Proteins into Lipid Bilayers Using Fusogenic Complementary-charged Proteoliposomes.
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Detergent-free Ultrafast Reconstitution of Membrane Proteins into Lipid Bilayers Using Fusogenic Complementary-charged Proteoliposomes.

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Light-Driven ATP Regeneration in Diblock/Grafted Hybrid Vesicles.

Christin Kleineberg1, Christian Wölfer1, Amirhossein Abbasnia1

  • 1Max Planck Institute for Dynamics of Complex Technical Systems Process Systems Engineering, Sandtorstraße 1, 39106, Magdeburg, Germany.

Chembiochem : a European Journal of Chemical Biology
|March 19, 2020
PubMed
Summary

Synthetic biology utilizes light-driven systems for energy regeneration. This study demonstrates superior long-term stability and biocompatibility of hybrid polymer membranes for artificial cell energy supplies.

Keywords:
ATP synthasebacteriorhodopsindiblock polymersenergy conversiongraft polymerspermeability

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Author Spotlight: Tackling Challenges in Synthetic Cell Engineering
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Author Spotlight: Tackling Challenges in Synthetic Cell Engineering

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Area of Science:

  • Synthetic biology
  • Biomaterials science
  • Biochemistry

Background:

  • Artificial protocells require energy sources for biochemical reactions.
  • Lipid and polymer membranes are common for protocell construction.
  • Integrating membrane proteins into these compartments is challenging.

Purpose of the Study:

  • To investigate membrane protein functionality in hybrid lipid/polymer and polymer/polymer vesicles.
  • To compare the performance of ATP regeneration systems in different membrane types.
  • To assess the biocompatibility and long-term stability of these hybrid systems.

Main Methods:

  • Constructing hybrid vesicles using graft polymer PDMS-g-PEO and diblock copolymer PBd-PEO.
  • Incorporating light-driven ATP regeneration systems (ATP synthase and bacteriorhodopsin).
  • Measuring membrane protein activity, biocompatibility, and long-term stability.

Main Results:

  • Lipid/polymer hybrid vesicles exhibited over 90% activity, indicating excellent biocompatibility.
  • Polymer/polymer hybrid vesicles demonstrated enhanced long-term stability, retaining 80% activity after 42 days.
  • The study highlights the potential of polymer-based hybrids for robust energy supply systems.

Conclusions:

  • Hybrid polymer membranes offer a promising platform for stable and efficient energy regeneration in synthetic biology.
  • The choice of membrane composition significantly impacts the performance and longevity of artificial cell systems.
  • Further research into polymer/polymer hybrids can advance the development of robust artificial cells.