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Precursor-Bound NifEN: Insights into Nitrogenase Cofactor Assembly

  1. Jared A. Wiig,
  2. Chi Chung Lee,
  3. Yilin Hu,
  4. Markus W. Ribbe

Published Online: 15 SEP 2012

DOI: 10.1002/9781119951438.eibc2075

Encyclopedia of Inorganic and Bioinorganic Chemistry

Encyclopedia of Inorganic and Bioinorganic Chemistry

How to Cite

Wiig, J. A., Lee, C. C., Hu, Y. and Ribbe, M. W. 2012. Precursor-Bound NifEN: Insights into Nitrogenase Cofactor Assembly. Encyclopedia of Inorganic and Bioinorganic Chemistry. .

Author Information

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

Publication History

  1. Published Online: 15 SEP 2012

Abstract

The biosynthesis of the iron–molybdenum cofactor (FeMoco) of nitrogenase is one of the most complicated processes in metalloprotein biochemistry. Here we review the recent progress on the investigation of NifEN, an important scaffold protein for the maturation of an iron-only precursor to a molybdenum- and homocitrate-containing FeMoco. The recently solved crystal structure of the precursor-bound form of NifEN is discussed in detail, which provides important insights into the biosynthetic mechanism of nitrogenase. In addition, the functional and spectroscopic features of NifEN are discussed.

3D Structure

Keywords:

  • Mo nitrogenase;
  • NifEN;
  • FeMoco;
  • precursor;
  • L-cluster;
  • MoFe protein;
  • Fe protein;
  • biosynthesis;
  • Azotobacter vinelandii