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Related Experiment Video

Updated: Jun 15, 2026

Measurement of the Potential Rates of Dissimilatory Nitrate Reduction to Ammonium Based on 14NH4+/15NH4+ Analyses via Sequential Conversion to N2O

Measurement of the Potential Rates of Dissimilatory Nitrate Reduction to Ammonium Based on ¹⁴NH₄⁺/¹⁵NH₄⁺ Analyses via Sequential Conversion to N₂O

Published on: October 7, 2020

Mimicking nitrogenase.

¹School of Chemistry, University of New South Wales, Sydney, 2052, Australia. i.dance@unsw.edu.au

Dalton Transactions (Cambridge, England : 2003)

|March 12, 2010

Summary

This study theoretically assesses metal sulfide clusters as models for nitrogenase, the enzyme catalyzing ammonia production from nitrogen. Promising M1 clusters show potential for mimicking nitrogenase intermediates, aiding in the design of artificial nitrogen fixation catalysts.

Area of Science:

Bioinorganic Chemistry
Computational Chemistry
Catalysis

Background:

The enzyme nitrogenase catalyzes the conversion of atmospheric nitrogen (N(2)) to ammonia (NH(3)) under mild conditions.
The active site of nitrogenase, FeMo-co, contains a unique NFe(7)MoS(9) core.
Understanding nitrogenase's mechanism is crucial for developing artificial nitrogen fixation catalysts.

Purpose of the Study:

To theoretically evaluate metal sulfide clusters as functional models of the nitrogenase active site (FeMo-co).
To assess the ability of these models to mimic intermediates in the proposed nitrogenase mechanism.
To identify promising cluster designs for artificial nitrogen fixation.

Main Methods:

Theoretical assessment using density functional simulations.

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Last Updated: Jun 15, 2026

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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Published on: October 7, 2020

Synthesis and Performance Characterizations of Transition Metal Single Atom Catalyst for Electrochemical CO2 Reduction

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Ammonia Synthesis at Low Pressure

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Published on: August 23, 2017

Focus on metal sulfide clusters with an X(c)Fe(4)S(4) face, mimicking FeMo-co's active site.

Evaluation of M1 clusters, {(tpb)Mo(mu(3)-S)(3)Fe(2)(Fe-L)S(c)(mu-S)(2)(Fe-L)Fe(2)(mu(3)-S)(3)Mo(tpb)}, for their mechanistic mimicry.

Main Results:

M1 clusters, with well-developed syntheses, show promise as functional models.
Simulations indicate M1 clusters can mimic key intermediates in the nitrogenase mechanism.
Elaborations of M1, including ligand modification, are proposed to enhance FeMo-co mimicry.

Conclusions:

Metal sulfide clusters, particularly elaborated M1 systems, are viable models for studying nitrogenase's FeMo-co active site.
Ligand modification of M1 clusters can tune their properties for proton relay and prevent unwanted side reactions.
The P-cluster of nitrogenase may have evolved from a relic catalytic site for N(2) reduction.