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Related Concept Videos

Inorganic Nitrogen Assimilation01:22

Inorganic Nitrogen Assimilation

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 nitrate reductase...
Structure of Amines01:19

Structure of Amines

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 illustrated in Figure...
Overview of Nitrogen Metabolism01:20

Overview of Nitrogen Metabolism

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 nitrogen...
Structural Isomerism02:34

Structural Isomerism

Isomerism in Complexes
Isomers are different chemical species that have the same chemical formula. Structural isomerism of coordination compounds can be divided into two subcategories, the linkage isomers and coordination-sphere isomers.
Linkage isomers occur when the coordination compound contains a ligand that can bind to the transition metal center through two different atoms. For example, the CN− ligand can bind through the carbon atom or through the nitrogen atom. Similarly, SCN− can be...
Microbes and the Nitrogen Cycle01:26

Microbes and the Nitrogen Cycle

The nitrogen cycle is a complex biogeochemical process critical to maintaining the balance of nitrogenous compounds in ecosystems. This cycle involves multiple microbial-mediated transformations through which nitrogen changes oxidation states, supporting essential ecological functions and contributing to plant and microbial growth.Nitrogen Fixation and AmmonificationNitrogen fixation initiates the cycle by converting inert atmospheric nitrogen (N₂) into bioavailable ammonia (NH₃), a process...
Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...

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Related Experiment Video

Updated: Jul 3, 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

Structural and Functional Characterization of Heterologous Nitrogenase Complexes.

Yizhou Li1,2, Sarah M Narehood1,2, Brian D Cook2

  • 1Department of Chemistry, University of California, La Jolla, San Diego, California 92093, United States.

Biochemistry
|July 2, 2026
PubMed
Summary
This summary is machine-generated.

Nitrogenase enzyme function is conserved across diverse bacteria. Researchers found that different nitrogenase components (iron protein and molybdenum-iron protein) from distinct species can still work together, retaining significant catalytic activity.

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Last Updated: Jul 3, 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

Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry
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Analyzing Protein Architectures and Protein-Ligand Complexes by Integrative Structural Mass Spectrometry

Published on: October 15, 2018

Determining Surface Areas and Pore Volumes of Metal-Organic Frameworks
06:45

Determining Surface Areas and Pore Volumes of Metal-Organic Frameworks

Published on: March 8, 2024

Area of Science:

  • Biochemistry
  • Structural Biology
  • Microbiology

Background:

  • Nitrogenase catalyzes essential dinitrogen to ammonia conversion.
  • Molybdenum nitrogenase consists of iron protein (FeP) and molybdenum-iron protein (MoFeP).
  • Sequence variability exists in FeP and MoFeP across different diazotrophs, questioning functional compatibility.

Purpose of the Study:

  • To investigate the functional and structural compatibility of nitrogenase components from distinct species, Azotobacter vinelandii (Av) and Gluconacetobacter diazotrophicus (Gd).
  • To understand the structural basis for functional complementation between heterologous nitrogenase pairs.

Main Methods:

  • Determined ADP·BeFx-trapped structure of homologous GdFeP-GdMoFeP complex using cryogenic electron microscopy (cryoEM).
  • Measured catalytic activities of homologous and heterologous FeP-MoFeP combinations (Gd/Av and Av/Gd).
  • Obtained high-resolution cryoEM structures of heterologous GdFeP-AvMoFeP and AvFeP-GdMoFeP complexes.

Main Results:

  • Homologous GdFeP-GdMoFeP complex structure is geometrically similar to its Av counterpart.
  • Heterologous Gd/Av nitrogenase combinations retained 60-80% of homologous catalytic activities.
  • CryoEM structures revealed that functional complementation tolerates significant sequence variation.

Conclusions:

  • Nitrogenase functional compatibility is conserved across phylogenetically distinct species.
  • Structural conservation of key elements for ATP hydrolysis, electron transfer, and substrate reduction underlies functional complementation.
  • This study provides structural insights into the chemomechanical coupling mechanism of nitrogenase.