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The mechanism for nitrogenase including all steps.

Per E M Siegbahn¹

¹Department of Organic Chemistry, Arrhenius Laboratory, Stockholm University, SE-106 91, Stockholm, Sweden. per.siegbahn@su.se.

Physical Chemistry Chemical Physics : PCCP

|July 6, 2019

Summary

Nitrogenase

Area of Science:

Biochemistry
Bioinorganic Chemistry
Enzyme Mechanisms

Background:

Nitrogenase catalyzes nitrogen fixation, a vital process for life.
The enzyme's active site contains a complex iron-molybdenum cofactor (FeMoco).
Previous studies suggested roles for a central carbide and a homocitrate ligand in proton transfer and substrate binding.

Purpose of the Study:

To reinvestigate the carbide protonation steps in nitrogenase catalysis.
To elucidate the mechanism of N2 activation and cofactor modification.
To propose a mechanism for deprotonating the carbide after catalysis.

Main Methods:

Computational studies and theoretical investigations.
Reinvestigation of experimental findings on carbide protonation.

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Analysis of cofactor structural dynamics during the catalytic cycle.

Main Results:

Protonation of the homocitrate ligand facilitates its rotation, releasing a molybdenum bond.
This rotation allows for the binding and activation of N2.
A mechanism for deprotonating the central carbide is proposed to reconcile experimental observations.

Conclusions:

The homocitrate ligand plays a dynamic role in N2 activation by modulating cofactor structure.
A proton transfer mechanism involving homocitrate rotation is essential for nitrogenase function.
A novel deprotonation pathway for the central carbide is suggested to complete the catalytic cycle.