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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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Chemolithotrophs are microorganisms that obtain energy by oxidizing inorganic molecules such as hydrogen gas (H₂), ammonia (NH₃), reduced sulfur compounds (H₂S, S²⁻), and ferrous iron (Fe²⁺). Unlike heterotrophic organisms that rely on organic carbon, chemolithotrophs transfer electrons from these inorganic donors to the electron transport chain (ETC), generating a proton motive force (PMF) that drives ATP synthesis through oxidative phosphorylation.
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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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The hemoglobin in the blood, the chlorophyll in green plants, vitamin B-12, and the catalyst used in the manufacture of polyethylene all contain coordination compounds. Ions of the metals, especially the transition metals, are likely to form complexes.
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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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Structural evidence for a dynamic metallocofactor during N2 reduction by Mo-nitrogenase.

Wonchull Kang1, Chi Chung Lee1, Andrew J Jasniewski1

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

Science (New York, N.Y.)
|June 20, 2020
PubMed
Summary
This summary is machine-generated.

Nitrogenase enzyme

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • Nitrogenase is crucial for converting atmospheric nitrogen to ammonia.
  • The precise mechanism of nitrogenase catalysis remains incompletely understood.
  • Metallocofactors are essential for nitrogenase's dinitrogen reduction activity.

Purpose of the Study:

  • To elucidate the mechanistic details of nitrogenase function.
  • To capture and analyze the structure of the MoFe protein during N2 turnover.
  • To investigate the role of cofactor dynamics in nitrogen fixation.

Main Methods:

  • X-ray crystallography
  • Determination of a high-resolution (1.83 Å) crystal structure of the MoFe protein.
  • Analysis of cofactor structural changes under physiological N2 turnover conditions.

Main Results:

  • Observed asymmetric displacements of cofactor belt sulfurs (S2B, S3A, S5A).
  • Identified distinct dinitrogen species within the two alpha-beta dimers.
  • Revealed differences in proton donation and Mo-homocitrate ligation (bidentate to monodentate switching).

Conclusions:

  • The nitrogenase cofactor exhibits dynamic behavior during catalysis.
  • All identified belt-sulfur sites appear to participate in the nitrogen fixation process.
  • The findings provide critical insights into the mechanism of biological nitrogen fixation.