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Related Concept Videos

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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Overview of Nitrogen Metabolism01:20

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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.
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The Nitrogen Cycle01:49

The Nitrogen Cycle

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Nitrogen atoms, present in all proteins and DNA, are recycled between abiotic and biotic components of the ecosystem. However, the primary form of nitrogen on Earth is nitrogen gas, which cannot be used by most animals and plants. Thus, nitrogen gas must first be converted into a usable form by nitrogen-fixing bacteria before it can be cycled through other living organisms. The use of nitrogen-containing fertilizers and animal waste products in human agriculture has greatly influenced the...
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Bacterial RNA Polymerase00:43

Bacterial RNA Polymerase

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Unlike eukaryotes, bacteria use a single RNA Polymerase (RNAP) to transcribe all genes. The different subunits of bacterial RNAPhave distinct functions. The multisubunit structure of the bacterial RNAP helps the enzyme to maintain catalytic function, facilitate assembly, interact with DNA and RNA, and self-regulate its activity.
In most genes, the transcription site is a single base present upstream of the coding sequence. Though RNAP is a catalytically efficient enzyme, it does not recognize...
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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’ carbon–carbon bond (154 pm). These aspects are...
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Bacterial Transcription

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RNA polymerase (RNAP) carries out DNA-dependent RNA synthesis in both bacteria and eukaryotes. Bacteria do not have a membrane-bound nucleus. So, transcription and translation occur simultaneously, on the same DNA template.
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Updated: Jan 18, 2026

Estimating Sediment Denitrification Rates Using Cores and N2O Microsensors
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Structural evolution of nitrogenase over 3 billion years.

Bruno Cuevas Zuviría1,2, Franka Detemple3, Kaustubh Amritkar1

  • 1Department of Bacteriology, University of Wisconsin-Madison, Madison, United States.

Elife
|September 11, 2025
PubMed
Summary
This summary is machine-generated.

Researchers resurrected ancient nitrogenases to study their evolution. This revealed how subtle changes and adaptations allowed nitrogenase to persist and evolve over billions of years, adapting to environmental shifts.

Keywords:
A. vinelandiiancient protein reconstructionevolutionary biologynitrogenaseprotein evolutionstructural reconstruction

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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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Area of Science:

  • Biochemistry
  • Evolutionary Biology
  • Structural Biology

Background:

  • The only known dinitrogen reduction mechanism is ancient, conserved from nitrogenase ancestors.
  • Previous work resurrected synthetic ancestral nitrogenases in *Azotobacter vinelandii*.

Purpose of the Study:

  • To investigate the structural evolution of nitrogenase over billions of years.
  • To combine phylogenetics, ancestral sequence reconstruction, protein crystallography, and deep-learning predictions.
  • To understand how nitrogenase adapted to major environmental transitions.

Main Methods:

  • Paleomolecular approach using phylogenetics and ancestral sequence reconstruction.
  • Protein crystallography to determine structures.
  • Deep-learning based predictions.
  • Resurrection and genomic integration of synthetic ancestral nitrogenases.

Main Results:

  • Nitrogenase maintained a conserved multimeric core throughout its evolution.
  • Novel modular features evolved in nitrogenase, correlating with environmental transitions.
  • Subtle distal changes and transient regulatory adaptations were crucial for nitrogenase persistence.
  • Protein evolution was shaped by environmental pressures over geologic time.

Conclusions:

  • Nitrogenase evolution is characterized by a conserved core and adaptable modular features.
  • Environmental transitions drove the evolution of nitrogenase structure and function.
  • The established framework aids in identifying structural constraints of ancient proteins.