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Articles linked to this work by shared authors, journal, and citation graph.

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Deserts, Rivers, Pools, and Billabongs: Water Features of the Nitrogenase Proteins, and their Functions.

Chembiochem : a European journal of chemical biology·2025
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The mechanism of nitrogenase: formation and release of the second NH<sub>3</sub> and completion of the cycle.

Dalton transactions (Cambridge, England : 2003)·2025
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Understanding non-reducible N<sub>2</sub> in the mechanism of Mo-nitrogenase.

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The mechanism of Mo-nitrogenase: from N<sub>2</sub> capture to first release of NH<sub>3</sub>.

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The activating capture of N<sub>2</sub> at the active site of Mo-nitrogenase.

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What triggers the coupling of proton transfer and electron transfer at the active site of nitrogenase?

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S 2B or not 2B?

Ian Dance1

  • 1School of Chemistry, UNSW Sydney, NSW 2052, Australia. i.dance@unsw.edu.au.

Dalton Transactions (Cambridge, England : 2003)
|November 27, 2025
PubMed
Summary

The enzyme nitrogenase

Area of Science:

  • Biochemistry
  • Enzymology
  • Computational Chemistry

Background:

  • The nitrogenase enzyme complex catalyzes nitrogen fixation.
  • The iron-molybdenum cofactor (FeMo-co) is central to nitrogenase activity.
  • A key debate exists regarding the role of the S2B atom within the FeMo-co during catalysis.

Purpose of the Study:

  • To resolve the mechanistic dilemma concerning the S2B atom's position in the FeMo-co during nitrogenase catalysis.
  • To evaluate evidence for a disruptive versus a conservative enzyme mechanism.

Main Methods:

  • Review and synthesis of existing experimental data.
  • Analysis of computational investigations into the nitrogenase mechanism.

Main Results:

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  • Experimental data suggests the S2B atom may be displaced to allow substrate binding.
  • Computational studies propose a mechanism where S2B is retained and essential.
  • A conflict exists between proposed disruptive and conservative mechanisms.

Conclusions:

  • The role of the S2B atom in the FeMo-co remains a critical question in nitrogenase research.
  • Further investigation is needed to definitively determine if S2B is displaced or retained during the enzyme's function.