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Response to Comment on "Structural evidence for a dynamic metallocofactor during N₂ reduction by Mo-nitrogenase".

Wonchull Kang¹, Chi Chung Lee¹, Andrew J Jasniewski¹

¹Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697, USA.

Science (New York, N.Y.)

|February 12, 2021

Summary

This study refutes claims that nitrogenase metallocofactor structure contradicts our findings. Biochemical and structural data confirm dinitrogen binding during nitrogen fixation.

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Area of Science:

Biochemistry
Structural Biology
Enzymology

Background:

Nitrogenase is crucial for biological nitrogen fixation.
Understanding the nitrogenase metallocofactor's dynamic structure is key to its mechanism.
Previous reports suggested alternative interpretations of the metallocofactor structure.

Purpose of the Study:

To address and refute claims by Peters et al. regarding the dynamic structure of the nitrogenase metallocofactor.
To reaffirm the binding of dinitrogen species to the nitrogenase cofactor during N2 reduction.

Main Methods:

Independent structural refinement of the nitrogenase metallocofactor.
Consideration of biochemical data related to nitrogenase activity.
Comparative analysis of structural and biochemical evidence.

Main Results:

The structural refinement by Peters et al. does not contradict the original findings.
Biochemical data strongly supports the proposed dynamic structure.
Evidence conclusively indicates dinitrogen species binding to the nitrogenase cofactor.

Conclusions:

The dynamic structure of the nitrogenase metallocofactor during N2 reduction is accurately represented.
Dinitrogen binding to the nitrogenase cofactor is confirmed by integrated biochemical and structural data.
The interpretation by Peters et al. is refuted by the presented evidence.