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P-cluster maturation on nitrogenase MoFe protein.

Yilin Hu¹, Aaron W Fay, Chi Chung Lee

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

Proceedings of the National Academy of Sciences of the United States of America

|June 15, 2007

Summary

The biosynthesis of nitrogenase P-cluster involves a stepwise assembly on the MoFe protein. This study reveals that NifZ protein acts as a chaperone, facilitating the maturation of the second P-cluster.

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Area of Science:

Biochemistry
Bioinorganic Chemistry
Enzymology

Background:

Nitrogenase P-cluster biosynthesis is crucial and chemically unique.
Previous research indicates a stepwise assembly of the P-cluster on the MoFe protein from precursor [4Fe-4S]-like clusters.

Purpose of the Study:

To elucidate the specific mechanism and requirements for the assembly of the second nitrogenase P-cluster.
To investigate the role of NifZ protein in P-cluster maturation.

Main Methods:

Utilized a P-cluster maturation assay with purified components.
Employed combined biochemical and spectroscopic approaches.
Investigated the sequential action of NifZ, Fe protein, and MgATP.

Main Results:

Demonstrated that NifZ protein is required before Fe protein/MgATP for the second P-cluster's maturation.
Spectroscopic evidence confirmed the conversion of [4Fe-4S] cluster-like fragments to P-clusters.
Identified NifZ as a potential chaperone facilitating subsequent steps.

Conclusions:

The maturation of the second P-cluster is a concerted process involving NifZ, Fe protein, and MgATP.
NifZ protein likely functions as a chaperone, preceding the action of Fe protein/MgATP.
Confirmed the physiological relevance of the [4Fe-4S] cluster-like precursor in P-cluster biosynthesis.