Reduction of Substrates by Nitrogenases

Lance C. Seefeldt, Zhi Yong Yang, Dmitriy A. Lukoyanov, Derek F. Harris, Dennis R. Dean, Simone Raugei, Brian M. Hoffman

Research output: Contribution to journalReview articlepeer-review

22 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)5082-5106
Number of pages25
JournalChemical reviews
Issue number12
Publication statusPublished - Jun 24 2020

ASJC Scopus subject areas

  • Chemistry(all)

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