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

Ligand Binding and Linkage00:49

Ligand Binding and Linkage

Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence the...
Ligand Binding and Linkage00:49

Ligand Binding and Linkage

Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence the...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Ligand Binding Sites02:40

Ligand Binding Sites

Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...

You might also read

Related Articles

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

Sort by
Same author

Age-Dependent z Scores and eGFR-Adjusted Reference Ranges for Neurofilament Light: A Practical Approach for Clinical Laboratories.

Clinical chemistry·2026
Same author

Indirect optical geometry measurement based on optical tweezers in transparent microchannels.

Optics express·2026
Same author

Correction: Intraperitoneal Oil Application Causes Local Inflammation with Depletion of Resident Peritoneal Macrophages.

Molecular cancer research : MCR·2026
Same author

Identification of serum biomarkers linking myocardial fibrosis, systolic dysfunction and outcomes in patients with severe aortic stenosis.

Cardiovascular research·2026
Same author

Molecular characterization of cell decay in inflammation and topological assignment of released cfDNA for integrative laboratory and radiological outcome assessment.

Frontiers in cellular and infection microbiology·2026
Same author

Perioperative laboratory profiles predict complications after extensive head and neck reconstruction: a proof-of-concept study.

Frontiers in oncology·2026

Related Experiment Video

Updated: Jul 8, 2026

Catalytic Reactions at Amine-Stabilized and Ligand-Free Platinum Nanoparticles Supported on Titania During Hydrogenation of Alkenes and Aldehydes
12:08

Catalytic Reactions at Amine-Stabilized and Ligand-Free Platinum Nanoparticles Supported on Titania During Hydrogenation of Alkenes and Aldehydes

Published on: June 24, 2022

Self-adaptable catalysts: substrate-dependent ligand configuration.

Raivis Zalubovskis1, Alexis Bouet, Ester Fjellander

  • 1KTH School of Chemical Science and Engineering, Department of Chemistry, Organic Chemistry, SE 100 44 Stockholm, Sweden.

Journal of the American Chemical Society
|January 18, 2008
PubMed
Summary
This summary is machine-generated.

Palladium complexes with a flexible ligand adapt their structure to different substrates during allylic alkylation reactions. This structural adaptability explains varying catalytic behaviors observed with different allyl systems.

More Related Videos

Defining Substrate Specificities for Lipase and Phospholipase Candidates
08:59

Defining Substrate Specificities for Lipase and Phospholipase Candidates

Published on: November 23, 2016

Structure-Guided Design and Development of Novel Cyclophilin A Inhibitors and Ganoderiol-F Derivatives: An In-Silico Approach
10:01

Structure-Guided Design and Development of Novel Cyclophilin A Inhibitors and Ganoderiol-F Derivatives: An In-Silico Approach

Published on: June 23, 2026

Related Experiment Videos

Last Updated: Jul 8, 2026

Catalytic Reactions at Amine-Stabilized and Ligand-Free Platinum Nanoparticles Supported on Titania During Hydrogenation of Alkenes and Aldehydes
12:08

Catalytic Reactions at Amine-Stabilized and Ligand-Free Platinum Nanoparticles Supported on Titania During Hydrogenation of Alkenes and Aldehydes

Published on: June 24, 2022

Defining Substrate Specificities for Lipase and Phospholipase Candidates
08:59

Defining Substrate Specificities for Lipase and Phospholipase Candidates

Published on: November 23, 2016

Structure-Guided Design and Development of Novel Cyclophilin A Inhibitors and Ganoderiol-F Derivatives: An In-Silico Approach
10:01

Structure-Guided Design and Development of Novel Cyclophilin A Inhibitors and Ganoderiol-F Derivatives: An In-Silico Approach

Published on: June 23, 2026

Area of Science:

  • Organometallic Chemistry
  • Catalysis
  • Organic Synthesis

Background:

  • Palladium-catalyzed allylic alkylation is a crucial reaction in organic synthesis.
  • Understanding the structure of catalytic intermediates is key to optimizing reaction outcomes.
  • Ligand conformation significantly influences the stereochemical pathways of catalytic reactions.

Purpose of the Study:

  • To investigate the conformational behavior of a configurationally labile ligand in palladium complexes.
  • To model intermediates in palladium-catalyzed allylic alkylations.
  • To correlate ligand structure with catalytic activity and selectivity.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) spectroscopy
  • Density Functional Theory (DFT) calculations
  • X-ray crystallography

Main Results:

  • The ligand adopts a C(s) conformation in Pd(II) allyl complexes.
  • The ligand exhibits different conformations in Pd(0) olefin complexes depending on the allyl system.
  • Structural adaptability of the palladium complex to substrates was confirmed in both solution and solid states.
  • Observed structural preferences correlate with the reactivity of different allyl acetates in palladium-catalyzed allylic alkylations.

Conclusions:

  • The configurationally labile ligand demonstrates significant conformational flexibility.
  • Palladium complexes can adjust their structure to accommodate various substrates, influencing catalytic outcomes.
  • This study provides insights into the mechanism of palladium-catalyzed allylic alkylations and the role of ligand design.