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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...
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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...

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Catalizadores autoadaptables: configuración de ligando dependiente del sustrato y dependiente del sustrato.

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
Resumen
Este resumen es generado por máquina.

Los complejos de paladio con un ligando flexible adaptan su estructura a diferentes sustratos durante las reacciones de alquilación alílica. Esta adaptabilidad estructural explica los diferentes comportamientos catalíticos observados con diferentes sistemas de alelos.

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Área de la Ciencia:

  • Química organometálica Química orgánica de los metales.
  • La catálisis de la catálisis.
  • Síntesis orgánica La síntesis orgánica.

Sus antecedentes:

  • La alquilación alilica catalizada por paladio es una reacción crucial en la síntesis orgánica.
  • Comprender la estructura de los intermediarios catalíticos es clave para optimizar los resultados de las reacciones.
  • La conformación del ligando influye significativamente en las vías estereoquímicas de las reacciones catalíticas.

Objetivo del estudio:

  • Para investigar el comportamiento conformacional de un ligando configuradamente lábil en complejos de paladio.
  • Para modelar los intermediarios en las alquilaciones alilicas catalizadas por el paladio.
  • Para correlacionar la estructura del ligando con la actividad catalítica y la selectividad.

Principales métodos:

  • La espectroscopia de resonancia magnética nuclear (RMN) también se conoce como espectroscopia de resonancia magnética nuclear.
  • Cálculos de la Teoría Funcional de la Densidad (DFT, por sus siglas en inglés)
  • Cristalografía de rayos X con rayos X.

Principales resultados:

  • El ligando adopta una conformación C(s) en los complejos Pd(II) de alelo.
  • El ligando exhibe diferentes conformaciones en los complejos de olefinas Pd(0) dependiendo del sistema de alelos.
  • Se confirmó la adaptabilidad estructural del complejo de paladio a sustratos tanto en estado sólido como en estado disuelto.
  • Las preferencias estructurales observadas se correlacionan con la reactividad de los diferentes acetatos de alilo en las alquilaciones alilicas catalizadas por el paladio.

Conclusiones:

  • El ligando configuradamente labile demuestra una flexibilidad conformacional significativa.
  • Los complejos de paladio pueden ajustar su estructura para acomodar varios sustratos, influyendo en los resultados catalíticos.
  • Este estudio proporciona información sobre el mecanismo de las alquilaciones alilicas catalizadas por el paladio y el papel del diseño del ligando.