Reduction of Substrates by Nitrogenases

• Published in: Chemical reviews 2020-06, Vol.120 (12), p.5082-5106
• Main Authors: Seefeldt, Lance C, Yang, Zhi-Yong, Lukoyanov, Dmitriy A, Harris, Derek F, Dean, Dennis R, Raugei, Simone, Hoffman, Brian M
• Format: Article
• Language: English
• Subjects: Ammonia; Carbon dioxide; Catalysts; Enzymes; Food production; Fossil fuels; Nitrogen fixation; Nitrogenation; Reduction; Substrates
• ISSN: 0009-2665; 1520-6890
• DOI: 10.1021/acs.chemrev.9b00556

Nitrogenase is the enzyme that catalyzes biological N2 reduction to NH3. This enzyme achieves an impressive rate enhancement over the uncatalyzed reaction. Given the high demand for N2 fixation to support food and chemical production and the heavy reliance of the industrial Haber–Bosch nitrogen fixation reaction on fossil fuels, there is a strong need to elucidate how nitrogenase achieves this difficult reaction under benign conditions as a means of informing the design of next generation synthetic catalysts. This Review summarizes recent progress in addressing how nitrogenase catalyzes the reduction of an array of substrates. New insights into the mechanism of N2 and proton reduction are first considered. This is followed by a summary of recent gains in understanding the reduction of a number of other nitrogenous compounds not considered to be physiological substrates. Progress in understanding the reduction of a wide range of C-based substrates, including CO and CO2, is also discussed, and remaining challenges in understanding nitrogenase substrate reduction are considered.