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The Spectroscopy of Nitrogenases.

Authors :
Van Stappen, Casey
Decamps, Laure
Cutsail III, George E.
Bjornsson, Ragnar
Henthorn, Justin T.
Birrell, James A.
DeBeer, Serena
Source :
Chemical Reviews. 6/24/2020, Vol. 120 Issue 12, p5005-5081. 77p.
Publication Year :
2020

Abstract

Nitrogenases are responsible for biological nitrogen fixation, a crucial step in the biogeochemical nitrogen cycle. These enzymes utilize a two-component protein system and a series of iron-sulfur clusters to perform this reaction, culminating at the FeMco active site (M = Mo, V, Fe), which is capable of binding and reducing N2 to 2NH3. In this review, we summarize how different spectroscopic approaches have shed light on various aspects of these enzymes, including their structure, mechanism, alternative reactivity, and maturation. Synthetic model chemistry and theory have also played significant roles in developing our present understanding of these systems and are discussed in the context of their contributions to interpreting the nature of nitrogenases. Despite years of significant progress, there is still much to be learned from these enzymes through spectroscopic means, and we highlight where further spectroscopic investigations are needed. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
00092665
Volume :
120
Issue :
12
Database :
Academic Search Index
Journal :
Chemical Reviews
Publication Type :
Academic Journal
Accession number :
144258749
Full Text :
https://doi.org/10.1021/acs.chemrev.9b00650