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Cofactors and Coenzymes01:24

Cofactors and Coenzymes

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Enzymes are proteins made of amino acids. The functional group of each constituent amino acid catalyzes a wide variety of chemical reactions via ionic interactions or acid-base reactions. However, amino acids cannot catalyze oxidation-reduction and group transfer reactions and need to be aided by non-protein components called cofactors. Cofactors are also referred to as the chemical teeth of an enzyme.
Cofactors can be metallic ions or organic molecules called coenzymes. These types of helper...
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Nitrosation of Enols01:19

Nitrosation of Enols

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The nitrosation reaction is one of the methods of preparing 1,2-diketones. The enol tautomer of the starting ketone reacts with sodium nitrite in hydrochloric acid, generating the 1,2-diketone after hydrolysis.
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Overview of Nitrogen Metabolism01:20

Overview of Nitrogen Metabolism

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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...
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2° Amines to N-Nitrosamines: Reaction with NaNO201:20

2° Amines to N-Nitrosamines: Reaction with NaNO2

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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.
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Role of Reduced Coenzymes NADH and FADH₂01:29

Role of Reduced Coenzymes NADH and FADH₂

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The energy released from the breakdown of the chemical bonds within nutrients can be stored either through the reduction of electron carriers or in the bonds of adenosine triphosphate (ATP). In living systems, a small class of compounds functions as mobile electron carriers, molecules that bind to and shuttle high-energy electrons between compounds in pathways. The principal electron carriers that will be considered originate from the B vitamin group and are derivatives of nucleotides; they are...
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Preparation of 1° Amines: Hofmann and Curtius Rearrangement Mechanism01:26

Preparation of 1° Amines: Hofmann and Curtius Rearrangement Mechanism

3.5K
The Hofmann and Curtius rearrangement reactions can be applied to synthesize primary amines from carboxylic acid derivatives such as amides and acyl azides. In the Hofmann rearrangement, a primary amide undergoes deprotonation in the presence of a base, followed by halogenation to generate an N-haloamide. A second proton abstraction produces a stabilized anionic species, which rearranges to an isocyanate intermediate via an alkyl group migration from the carbonyl carbon to the neighboring...
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Mutagenic Survey of Key Residues of NifB Involved in Radical SAM-Dependent Nitrogenase Cofactor Assembly.

Chembiochem : a European journal of chemical biology·2026
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Minimal ATP-Independent N<sub>2</sub>-Reducing Systems Defined by L-Cluster-Bound Nitrogenase Assembly Platforms.

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Structural insights into metallocluster trafficking in the nitrogenase assembly scaffold NifEN.

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Dual-enzyme logic powers azetidine biosynthesis.

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Heterologous synthesis of a simplified nitrogenase analog in <i>Escherichia coli</i>.

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Updated: Jun 24, 2025

Measurement of the Potential Rates of Dissimilatory Nitrate Reduction to Ammonium Based on 14NH4+/15NH4+ Analyses via Sequential Conversion to N2O
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Measurement of the Potential Rates of Dissimilatory Nitrate Reduction to Ammonium Based on 14NH4+/15NH4+ Analyses via Sequential Conversion to N2O

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Cofactor maturase NifEN: A prototype ancient nitrogenase?

Chi Chung Lee1, Kamil Górecki1, Martin Stang2

  • 1Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697- 3900, USA.

Science Advances
|June 12, 2024
PubMed
Summary

Nitrogenase

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Area of Science:

  • Biochemistry
  • Evolutionary Biology
  • Microbiology

Background:

  • Nitrogenase is crucial for the global nitrogen cycle.
  • The evolutionary origins of nitrogenase, specifically the order of appearance of its components NifDK and NifEN, are not well understood.

Purpose of the Study:

  • To investigate the evolutionary history of nitrogenase.
  • To explore the functional relationship between NifEN and NifDK in nitrogen fixation.

Main Methods:

  • Biochemical assays to test nitrogen reduction capabilities.
  • Structural and functional analysis of nitrogenase components.

Main Results:

  • NifEN can reduce nitrogen (N₂) at its L-cluster, a homolog of NifDK's M-cluster.
  • NifDK with an L-cluster can also perform nitrogen reduction, mimicking NifEN.

Conclusions:

  • A NifEN-like protein with an L-cluster may represent an ancient form of nitrogenase.
  • This finding offers insights into the evolutionary origins of nitrogenase and related enzymes.