Jove
Visualize
Contáctanos
JoVE
x logofacebook logolinkedin logoyoutube logo
ACERCA DE JoVE
Visión GeneralLiderazgoBlogCentro de Ayuda JoVE
AUTORES
Proceso de PublicaciónConsejo EditorialAlcance y PolíticasRevisión por ParesPreguntas FrecuentesEnviar
BIBLIOTECARIOS
TestimoniosSuscripcionesAccesoRecursosConsejo Asesor de BibliotecasPreguntas Frecuentes
INVESTIGACIÓN
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchivo
EDUCACIÓN
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualCentro de Recursos para ProfesoresSitio de Profesores
Términos y Condiciones de Uso
Política de Privacidad
Políticas

Videos de Conceptos Relacionados

Inorganic Nitrogen Assimilation01:22

Inorganic Nitrogen Assimilation

813
Nitrogen is an essential element in biological systems, forming a crucial component of proteins, nucleic acids, and other cellular constituents. Many bacteria and archaea acquire nitrogen in the form of nitrate (NO₃⁻) or ammonia (NH₃), which are then assimilated into biomolecules through specific enzymatic pathways.Assimilatory Nitrate ReductionWhen nitrate enters the cell, it undergoes a two-step reduction process known as assimilatory nitrate reduction. Initially, the enzyme...
813
Catalysis02:50

Catalysis

32.4K
The presence of a catalyst affects the rate of a chemical reaction. A catalyst is a substance that can increase the reaction rate without being consumed during the process. A basic comprehension of a catalysts’ role during chemical reactions can be understood from the concept of reaction mechanisms and energy diagrams.
32.4K
Introduction to Mechanisms of Enzyme Catalysis01:13

Introduction to Mechanisms of Enzyme Catalysis

10.3K
10.3K
Introduction to Mechanisms of Enzyme Catalysis01:13

Introduction to Mechanisms of Enzyme Catalysis

11.5K
For many years, scientists thought that enzyme-substrate binding took place in a simple "lock-and-key" fashion. This model stated that the enzyme and substrate fit together perfectly in one instantaneous step. However, current research supports a more refined view scientists call induced fit. The induced-fit model expands upon the lock-and-key model by describing a more dynamic interaction between enzyme and substrate. As the enzyme and substrate come together, their interaction causes...
11.5K
Overview of Nitrogen Metabolism01:20

Overview of Nitrogen Metabolism

12.5K
Nitrogen is a very important element for life because it is a major constituent of proteins and nucleic acids. It is a macronutrient, and in nature, it is recycled from organic compounds and stored in the form of  ammonia, ammonium ions, nitrate, nitrite, or  nitrogen gas by many metabolic processes. Many of these metabolic processes are carried out only by prokaryotes.
The largest pool of nitrogen available in the terrestrial ecosystem is gaseous nitrogen (N2) from the air, but this...
12.5K
2° Amines to N-Nitrosamines: Reaction with NaNO201:20

2° Amines to N-Nitrosamines: Reaction with NaNO2

5.8K
Secondary amines react with nitrous acid to form N-nitrosamines, as depicted in Figure 1. Nitrous acid, a weak and unstable acid, is formed in situ from an aqueous solution of sodium nitrite and strong acids, such as hydrochloric acid or sulfuric acid, in cold conditions. In the presence of an acid, the nitrous acid gets protonated. The subsequent loss of water results in the formation of the electrophile known as nitrosonium ion.
5.8K

También podría leer

Artículos Relacionados

Artículos vinculados a este trabajo por autores compartidos, revista y gráfico de citas.

Ordenar por
Same author

Structural and Functional Characterization of Heterologous Nitrogenase Complexes.

Biochemistry·2026
Same author

Role of Polymer-Protein Interactions in the Dynamics of Polymer-Integrated Protein Crystals.

Journal of the American Chemical Society·2026
Same author

Computational Design of a Highly Stable Dicopper Catechol Oxidase.

Journal of the American Chemical Society·2026
Same author

<i>De Novo</i> Design of a Metalloprotein with a Synthetically Inspired Dinuclear Paddlewheel Coordination Motif.

Journal of the American Chemical Society·2025
Same author

Design of a protein scaffold with a selective, Bi-containing heterodinuclear metal coordination motif.

Journal of inorganic biochemistry·2025
Same author

Design of light- and chemically responsive protein assemblies through host-guest interactions.

Chem·2025

Video Experimental Relacionado

Updated: Apr 4, 2026

Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase
10:01

Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase

Published on: December 4, 2017

12.8K

Pruebas de complejos de encuentro funcionalmente relevantes en la catálisis de la nitrogenasas

Cedric P Owens1, Faith E H Katz1, Cole H Carter1

  • 1Department of Chemistry and Biochemistry, University of California, San Diego , La Jolla, California 92039, United States.

Journal of the American Chemical Society
|September 12, 2015
PubMed
Resumen
Este resumen es generado por máquina.

Los complejos de encuentro entre la proteína de hierro (FeP) y la proteína de molibdeno-hierro (MoFeP) son cruciales para la catálisis de la nitrogenasa. Las mutaciones que interrumpen las interacciones electrostáticas en MoFeP reducen la actividad catalítica al impedir la asociación FeP-MoFeP.

Más Videos Relacionados

Synthesis and Performance Characterizations of Transition Metal Single Atom Catalyst for Electrochemical CO2 Reduction
10:57

Synthesis and Performance Characterizations of Transition Metal Single Atom Catalyst for Electrochemical CO2 Reduction

Published on: April 10, 2018

19.4K
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

4.2K

Videos de Experimentos Relacionados

Last Updated: Apr 4, 2026

Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase
10:01

Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase

Published on: December 4, 2017

12.8K
Synthesis and Performance Characterizations of Transition Metal Single Atom Catalyst for Electrochemical CO2 Reduction
10:57

Synthesis and Performance Characterizations of Transition Metal Single Atom Catalyst for Electrochemical CO2 Reduction

Published on: April 10, 2018

19.4K
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

4.2K

Área de la Ciencia:

  • La bioquímica
  • Enzimología
  • Fijación de nitrógeno

Sus antecedentes:

  • La nitrogenasa es esencial para la conversión del nitrógeno atmosférico (N2) en amoníaco (NH3).
  • Este proceso implica que la proteína MoFe (MoFeP) y la proteína Fe (FeP) interactúen de una manera dependiente del ATP para la transferencia de electrones.
  • Comprender las interacciones proteína-proteína es clave para optimizar la función de la nitrogenasa.

Objetivo del estudio:

  • Investigar el papel funcional de los complejos de encuentro en la catálisis de la nitrogenasa.
  • Identificar las interacciones específicas que estabilizan estos complejos.
  • Para aclarar el mecanismo de transferencia de electrones entre FeP y MoFeP.

Principales métodos:

  • Mutagénesis dirigida al sitio de Azotobacter vinelandii MoFeP para interrumpir las interacciones electrostáticas.
  • Evaluación de la actividad catalítica de las variantes de MoFeP.
  • Análisis cinético utilizando el modelo de Thorneley-Lowe para determinar las constantes de velocidad para la asociación y la transferencia de electrones.

Principales resultados:

  • Los complejos de encuentro se estabilizan mediante interacciones electrostáticas en la subunidad β de MoFeP.
  • Las mutaciones en esta región disminuyeron significativamente la actividad catalítica, con βLys400Glu mostrando el mayor efecto.
  • La mutación βK400E redujo la constante de tasa de asociación FeP-MoFeP cinco veces sin afectar el acoplamiento de transferencia de electrones por hidrólisis de ATP.

Conclusiones:

  • Los complejos de encuentro juegan un papel funcional en la catálisis de la nitrogenasa.
  • El FeP forma inicialmente complejos de encuentro en la superficie de la subunidad β del MoFeP.
  • Esta interacción es un requisito previo para la formación del complejo de transferencia de electrones activado por ATP en la interfaz αβ.