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Review
. 1994;14(3):225-49.
doi: 10.3109/07388554409079834.

Biosynthesis of the iron-molybdenum cofactor of nitrogenase

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Review

Biosynthesis of the iron-molybdenum cofactor of nitrogenase

R M Allen et al. Crit Rev Biotechnol. 1994.

Erratum in

  • Crit Rev Biotechnol 1995;15(1):104

Abstract

The iron-molybdenum cofactor (FeMo-co) of nitrogenase is a unique molybdenum-containing prosthetic group that has been proposed to form an integral part of the active site of dinitrogenase. In Klebsiella pneumoniae, at least six nif (nitrogen fixation) gene products are required for the biosynthesis of FeMo-co, including NIFB, NIFNE, NIFH, NIFQ, and NIFV. An in vitro system for the synthesis of FeMo-co, which requires MgATP, molybdate, homocitrate, and at least the products of nifN, E, B, and H, has provided an enzymatic assay for the purification of many of the gene products required for FeMo-co biosynthesis. Although the structure of the cofactor has been solved recently, much about the biosynthetic pathway remains unknown. This article reviews what is known about the various components required for FeMo-co biosynthesis.

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