2020/03/16 by Lance C. Seefeldt, Zhi‐Yong Yang, Dmitriy Lukoyanov +4 · 4 citations
Chemical Engineering · Energy · Materials Science · #Ammonia Synthesis and Nitrogen Reduction #Metalloenzymes and iron-sulfur proteins #Hydrogen Storage and Materials
paper · doi:10.1021/acs.chemrev.9b00556
openalex publication_date 2020/03/16 · openalex created_date 2025/10/10 · openalex updated_date 2026/07/31
Nitrogenase is the enzyme that catalyzes biological N 2 reduction to NH 3 . This enzyme achieves an impressive rate enhancement over the uncatalyzed reaction. Given the high demand for N 2 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 N 2 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 CO 2, is also discussed, and remaining challenges in understanding nitrogenase substrate reduction are considered.