Nitrogenases

Nathaniel S Sickerman; Yilin Hu; Markus W Ribbe

doi:10.1007/978-1-4939-8864-8_1

Nitrogenases

Methods Mol Biol. 2019:1876:3-24. doi: 10.1007/978-1-4939-8864-8_1.

Authors

Nathaniel S Sickerman¹, Yilin Hu², Markus W Ribbe^{3

4}

Affiliations

¹ Department of Molecular Biology and Biochemistry, University of California, Irvine, Irvine, CA, USA.
² Department of Molecular Biology and Biochemistry, University of California, Irvine, Irvine, CA, USA. yilinh@uci.edu.
³ Department of Molecular Biology and Biochemistry, University of California, Irvine, Irvine, CA, USA. mribbe@uci.edu.
⁴ Department of Chemistry, University of California, Irvine, Irvine, CA, USA. mribbe@uci.edu.

PMID: 30317471
DOI: 10.1007/978-1-4939-8864-8_1

Abstract

Biological nitrogen fixation, the conversion of dinitrogen (N₂) into ammonia (NH₃), stands as a particularly challenging chemical process. As the entry point into a bioavailable form of nitrogen, biological nitrogen fixation is a critical step in the global nitrogen cycle. In Nature, only one enzyme, nitrogenase, is competent in performing this reaction. Study of this complex metalloenzyme has revealed a potent substrate reduction system that utilizes some of the most sophisticated metalloclusters known. This chapter discusses the structure and function of nitrogenase, covers methods that have proven useful in the elucidation of enzyme properties, and provides an overview of the three known nitrogenase variants.

Keywords: Biological nitrogen fixation; Fe protein; M-cluster; MoFe protein; Nitrogenase; P-cluster.

Publication types

Research Support, N.I.H., Extramural

MeSH terms

Ammonia
Models, Molecular
Nitrogen
Nitrogen Fixation*
Nitrogenase / chemistry*
Nitrogenase / metabolism*
Oxidation-Reduction
Protein Conformation

Substances

Ammonia
Nitrogenase
Nitrogen