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Related Concept Videos

Catalysis02:50

Catalysis

27.0K
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.
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Inorganic Nitrogen Assimilation01:22

Inorganic Nitrogen Assimilation

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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...
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Introduction to Mechanisms of Enzyme Catalysis01:13

Introduction to Mechanisms of Enzyme Catalysis

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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...
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Nitriles to Carboxylic Acids: Hydrolysis01:08

Nitriles to Carboxylic Acids: Hydrolysis

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Nitriles undergo acid-catalyzed hydrolysis or base-catalyzed hydrolysis to form a carboxylic acid. These reactions proceed via an amide intermediate.
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Structure of Amines01:19

Structure of Amines

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The hybridized nitrogen atom in amines possesses a lone pair of electrons and is bound to three substituents with a bond angle of around 108°, which is less than the tetrahedral angle of 109.5°. However, the C–N–H bond angle is slightly larger at 112°, with a carbon–nitrogen bond length of 147 pm. This carbon–nitrogen bond length of of amines is longer than the carbon–oxygen bond of alcohols (143 pm) but shorter than alkanes’...
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1° Amines to Diazonium or Aryldiazonium Salts: Diazotization with NaNO2 Mechanism01:37

1° Amines to Diazonium or Aryldiazonium Salts: Diazotization with NaNO2 Mechanism

3.8K
Nitrous acid is a relatively weak and unstable acid prepared in situ by the reaction of sodium nitrite and cold, dilute hydrochloric acid. In an acidic solution, the nitrous acid undergoes protonation when it loses water to form a nitrosonium ion—an electrophile. Nitrous acid reacts with primary amines to give diazonium salts. The reaction is called diazotization of primary amines.
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Related Experiment Video

Updated: Jul 14, 2025

Synthesis of Metal Nanoparticles Supported on Carbon Nanotube with Doped Co and N Atoms and its Catalytic Applications in Hydrogen Production
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Synthesis of Metal Nanoparticles Supported on Carbon Nanotube with Doped Co and N Atoms and its Catalytic Applications in Hydrogen Production

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Catalysis and structure of nitrogenases.

Oliver Einsle1

  • 1Institut für Biochemie, Albert-Ludwigs-Universität Freiburg, Albertstrasse 21, 79104 Freiburg im Breisgau, Germany.

Current Opinion in Structural Biology
|October 6, 2023
PubMed
Summary

Biological nitrogen fixation, essential for life, is performed by the nitrogenase enzyme. Recent structural studies reveal its plasticity and dynamic changes, supporting a new mechanism of alternating half-site reactivity.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Enzymology

Background:

  • Biological nitrogen fixation is crucial for synthesizing biomacromolecules.
  • Nitrogenase is the sole enzyme catalyzing nitrogen fixation under ambient conditions.
  • The enzyme's structure, assembly, and mechanism are areas of active research.

Purpose of the Study:

  • To investigate the structural plasticity of nitrogenase isoforms.
  • To elucidate the catalytic mechanism of nitrogenase.
  • To integrate recent structural findings into a mechanistic model.

Main Methods:

  • High-resolution cryo-electron microscopy (cryo-EM).
  • Structural analysis of nitrogenase isoforms.
  • Analysis of enzyme structures under turnover conditions.

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Main Results:

  • Identified structural plasticity in nitrogenase active site cofactors.
  • Proposed two distinct binding sites for substrates and intermediates.
  • Observed dynamic conformational changes using cryo-EM.
  • Structures under turnover support alternating half-site reactivity.

Conclusions:

  • A new mechanistic model integrating experimental data has been proposed.
  • Alternating half-site reactivity is supported by structural data under turnover conditions.
  • Cryo-EM reveals dynamic aspects crucial for understanding nitrogenase function.