Identification of a Nitrogenase FeMo Cofactor Precursor on NifEN Complex

Overview

Journal Proc Natl Acad Sci U S A

Specialty Science

Date 2005 Feb 25

PMID 15728375

Citations 55

Authors

Yilin Hu

Aaron W Fay

Markus W Ribbe

Affiliations

Soon will be listed here.

Abstract

The biosynthesis of the FeMo cofactor (FeMoco) of Azotobacter vinelandii nitrogenase presumably starts with the production of its Fe/S core by NifB (the nifB gene product). This core is subsequently processed on the alpha2beta2 tetrameric NifEN complex (formed by the nifE and nifN gene products). In this article, we identify a NifEN-bound FeMoco precursor form that can be converted to fully assembled FeMoco in a so-called FeMoco-maturation assay containing only purified components. We also establish that only molybdate, homocitrate, MgATP, and Fe protein are essential for FeMoco maturation. The FeMoco-maturation assay described here will further address the remaining questions related to the assembly mechanism of the ever-intriguing FeMoco.

Citing Articles

Ammonia synthesis via an engineered nitrogenase assembly pathway in .

Solomon J, Lee C, Liu Y, Duffin C, Ribbe M, Hu Y Nat Catal. 2024; 7(10):1130-1141.

PMID: 39713742 PMC: 11661828. DOI: 10.1038/s41929-024-01229-x.

NifEN: a versatile player in nitrogenase assembly, catalysis and evolution.

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PMID: 39663240 DOI: 10.1007/s00775-024-02086-6.

Cofactor maturase NifEN: A prototype ancient nitrogenase?.

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