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Nitrogenase Cofactor Assembly: An Elemental Inventory.

Nathaniel S Sickerman1, Markus W Ribbe1,2, Yilin Hu1

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Researchers elucidated the assembly of the complex nitrogenase M-cluster, revealing how iron, sulfur, carbon, and molybdenum atoms combine. This work provides a framework for understanding nitrogenase cofactor biosynthesis and function.

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Area of Science:

  • Biochemistry
  • Bioinorganic Chemistry
  • Enzymology

Background:

  • Nitrogenase catalyzes N2 reduction to NH3 and C1 substrate conversion under ambient conditions.
  • The M-cluster, a complex [MoFe7S9C(R-homocitrate)] metallocofactor, is the active site in Mo-nitrogenase.
  • Understanding M-cluster biosynthesis is crucial for mechanistic insights and chemical synthesis.

Purpose of the Study:

  • To investigate the key biosynthetic steps involved in assembling the nitrogenase M-cluster.
  • To elucidate the roles of individual components (Fe, S, C, Mo, homocitrate) in cofactor formation.
  • To develop a working model for M-cluster assembly and maturation.

Main Methods:

  • Combined biochemical, spectroscopic, and structural studies.
  • Analysis of sequential synthesis of [Fe2S2] and [Fe4S4] units by NifS/U.
  • Investigation of cluster coupling, carbide insertion, and Mo-homocitrate substitution on NifB and NifEN.

Main Results:

  • A model for M-cluster assembly starting with FeS units, followed by coupling to form an [Fe8S9C] core.
  • Identification of a radical SAM-dependent mechanism for interstitial carbide insertion.
  • Characterization of an ATPase-dependent mechanism for Mo-homocitrate insertion into the [Fe8S9C] core.

Conclusions:

  • The M-cluster is assembled through a stepwise process involving modular FeS units, carbide insertion, and Mo-homocitrate substitution.
  • Novel mechanisms involving radical SAM and ATPase activities are critical for cofactor functionalization.
  • This research provides a framework for further understanding nitrogenase cofactor assembly and function.