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

Protein Networks02:26

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
Protein Networks02:26

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
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...
Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
Protein-Protein Interfaces02:04

Protein-Protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
Electron Transport Chain: Complex III and IV01:43

Electron Transport Chain: Complex III and IV

During the electron transport chain, electrons from NADH and FADH2 are first transferred to complexes I and II, respectively. These two complexes then transfer the electrons to ubiquinol, which carries them further to complex III. Complex III passes the electrons across the intermembrane space to Cyt c, which carries them further to complex IV. Complex IV donates electrons to oxygen and reduces it to water. As electrons pass through complexes I, III, and IV, the energy released aids the pumping...

You might also read

Related Articles

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

Sort by
Same author

Phosphate ions modulate enzyme activity and epistatic effects in two clavulanic acid-resistant β-lactamase mutants.

Protein science : a publication of the Protein Society·2025
Same author

Directed evolution of a beta-lactamase samples a wide variety of conformational states.

Protein science : a publication of the Protein Society·2025
Same author

A glycine at position 105 leads to clavulanic acid and avibactam resistance in class A β-lactamases.

The Journal of biological chemistry·2025
Same author

The Nature of Nanodisc Lipids Influences Fragment-Based Drug Discovery Results.

Chemical biology & drug design·2025
Same author

Terminal spin labeling of xylotriose strongly affects interactions in the active site of xylanase BcX.

Journal of biomolecular NMR·2025
Same author

Stabilizing Mutations Enhance Evolvability of BlaC β-lactamase by Widening the Mutational Landscape.

Journal of molecular biology·2025
Same journal

Decoding Galectin-Glycan Recognition with <sup>19</sup>F-Tagged Lectins: from Simple Glycans to the Cellular Glycocalyx.

Journal of the American Chemical Society·2026
Same journal

Open- and Closed-Shell Roles of Sensitizer and Annihilator in Pseudo-Single Component Mixtures for Upconversion.

Journal of the American Chemical Society·2026
Same journal

Pressure-Induced Superconductivity at 15 K in van-der-Waals Ferroelectric CuInP<sub>2</sub>S<sub>6</sub>.

Journal of the American Chemical Society·2026
Same journal

Carbene Analogues of Group 15: Reduction of s-Hydrindacene-Based Chloropnictogenium Ions To Access an Antimony Hydride Monocation and a Trinuclear Bismuth Dication.

Journal of the American Chemical Society·2026
Same journal

Chiral-Ligand-Modulated Nickel-Catalyzed Stereoselective Radical Migratory C2-Arylation of Carbohydrates.

Journal of the American Chemical Society·2026
Same journal

Coordination-Constraint-Driven Enhanced Chirality Induction in Perovskite Quantum Dot Solids.

Journal of the American Chemical Society·2026
See all related articles

Related Experiment Video

Updated: May 29, 2026

Genome-wide Protein-protein Interaction Screening by Protein-fragment Complementation Assay (PCA) in Living Cells
08:38

Genome-wide Protein-protein Interaction Screening by Protein-fragment Complementation Assay (PCA) in Living Cells

Published on: March 3, 2015

Efficient electron transfer in a protein network lacking specific interactions.

Francesca Meschi1, Frank Wiertz, Linda Klauss

  • 1Department of Biochemistry and Molecular Biology, University of Parma, 43100 Parma, Italy.

Journal of the American Chemical Society
|September 16, 2011
PubMed
Summary
This summary is machine-generated.

This study reveals that Paracoccus denitrificans uses weak, electrostatic interactions for efficient electron transfer, challenging the need for specific protein binding in biochemical processes. This flexibility may aid in integrating new metabolic pathways.

More Related Videos

Investigating Protein-protein Interactions in Live Cells Using Bioluminescence Resonance Energy Transfer
11:46

Investigating Protein-protein Interactions in Live Cells Using Bioluminescence Resonance Energy Transfer

Published on: May 26, 2014

Quantification of Protein Interaction Network Dynamics using Multiplexed Co-Immunoprecipitation
07:57

Quantification of Protein Interaction Network Dynamics using Multiplexed Co-Immunoprecipitation

Published on: August 21, 2019

Related Experiment Videos

Last Updated: May 29, 2026

Genome-wide Protein-protein Interaction Screening by Protein-fragment Complementation Assay (PCA) in Living Cells
08:38

Genome-wide Protein-protein Interaction Screening by Protein-fragment Complementation Assay (PCA) in Living Cells

Published on: March 3, 2015

Investigating Protein-protein Interactions in Live Cells Using Bioluminescence Resonance Energy Transfer
11:46

Investigating Protein-protein Interactions in Live Cells Using Bioluminescence Resonance Energy Transfer

Published on: May 26, 2014

Quantification of Protein Interaction Network Dynamics using Multiplexed Co-Immunoprecipitation
07:57

Quantification of Protein Interaction Network Dynamics using Multiplexed Co-Immunoprecipitation

Published on: August 21, 2019

Area of Science:

  • Biochemistry
  • Microbiology
  • Protein Interactions

Background:

  • Proteins typically require specific, well-defined interactions for partner selection in biochemical processes.
  • The soil bacterium Paracoccus denitrificans is involved in metabolic electron transfer, oxidizing compounds and channeling electrons to reduce oxygen.

Purpose of the Study:

  • To investigate the nature of protein interactions in the electron transfer network of Paracoccus denitrificans.
  • To determine if specific molecular interactions are essential for efficient electron transfer in this bacterium.

Main Methods:

  • Utilized steady-state kinetic measurements.
  • Employed Nuclear Magnetic Resonance (NMR) experiments to analyze protein interactions.

Main Results:

  • Identified a protein network involving amicyanin and four c-type cytochromes for electron transfer.
  • Demonstrated that interactions are governed primarily by the electrostatic properties of the proteins.
  • Observed a high degree of flexibility in electron transfer pathways due to weak, ill-defined interactions.

Conclusions:

  • Paracoccus denitrificans employs a pool of cytochromes with weak, non-specific interactions for efficient electron transfer.
  • This contrasts with the prevailing view that specific molecular interactions are necessary for functional biochemical processes.
  • The lack of stringent specificity may facilitate the integration of novel metabolic pathways within the bacterium.