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Reduction of Substrates by Nitrogenases.
Chemical Reviews ( IF 51.4 ) Pub Date : 2020-03-16 , DOI: 10.1021/acs.chemrev.9b00556
Lance C Seefeldt 1 , Zhi-Yong Yang 1 , Dmitriy A Lukoyanov 2 , Derek F Harris 1 , Dennis R Dean 3 , Simone Raugei 4 , Brian M Hoffman 2
Affiliation  

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.

中文翻译:

氮酶还原底物。

固氮酶是催化生物N 2还原为NH 3的酶。与未催化反应相比,该酶可实现令人印象深刻的速率增强。给定N的高需求2固定到支撑食品和化学品生产和对化石燃料的工业哈柏固氮反应的严重依赖,有强烈的需求,以阐明固氮如何实现良性条件的手段根据本难以反应告知下一代合成催化剂的设计。这篇综述总结了解决固氮酶如何催化一系列底物还原的最新进展。对N 2机理的新见解首先考虑质子还原。接下来是对最近了解减少许多其他非含氮化合物的生理学认识的总结。还讨论了在理解减少各种基于C的底物(包括CO和CO 2)方面的进展,并考虑了在理解固氮酶底物还原方面的剩余挑战。
更新日期:2020-03-16
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