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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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Cluster assembly in nitrogenase.

Nathaniel S Sickerman1, Lee A Rettberg1, Chi Chung Lee1

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

Essays in Biochemistry
|May 11, 2017
PubMed
Summary
This summary is machine-generated.

Nitrogenase enzymes use complex iron-sulfur clusters, P-cluster and M-cluster, for nitrogen (N₂) reduction. Their biosynthesis involves intricate steps, including cluster assembly and cofactor insertion, crucial for enzyme function.

Keywords:
M-clusterNifDKNifENNitrogenaseP-cluster

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Area of Science:

  • Biochemistry
  • Enzymology
  • Bioinorganic Chemistry

Background:

  • Nitrogenase is essential for biological nitrogen fixation, converting atmospheric nitrogen (N₂) into ammonia.
  • The enzyme utilizes complex iron-sulfur metalloclusters, P-cluster and M-cluster, for catalysis.
  • Understanding the biosynthesis of these metalloclusters is key to comprehending nitrogenase function.

Purpose of the Study:

  • To elucidate the intricate biosynthetic pathways of the P-cluster and M-cluster metalloclusters in nitrogenase.
  • To detail the roles of accessory proteins and specific chemical processes in cofactor maturation.
  • To provide mechanistic insights into the assembly and transfer of these critical cofactors.

Main Methods:

  • The study describes the origin of metalloclusters from [Fe₄S₄] precursors.
  • It details the involvement of accessory proteins like NifS, NifU, NifZ, NifB, and NifEN.
  • Mechanistic steps including reductive coupling, radical-SAM dependent processes, and cofactor transfer are outlined.

Main Results:

  • P-cluster assembly involves the fusion of [Fe₄S₄] clusters on NifDK, facilitated by NifZ and NifH.
  • M-cluster biosynthesis proceeds via an L-cluster intermediate on NifB, followed by maturation with Mo and homocitrate on NifEN.
  • Mature M-cluster is transferred from NifEN to NifDK, undergoing a conformational change for activation.

Conclusions:

  • The biosynthesis of nitrogenase metalloclusters is a complex, multi-step process involving precise coordination of proteins and chemical reactions.
  • These findings provide critical mechanistic insights into how nitrogenase achieves the challenging reduction of N₂.
  • The study highlights the essential roles of various accessory proteins in generating and delivering the catalytic cofactors.