ArticleChemistry (Weinheim an der Bergstrasse, Germany)2025
What Can be Learned From the Electrostatic Environments Within Nitrogenase Enzymes?
Article in Chemistry (Weinheim an der Bergstrasse, Germany), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Nitrogen fixation is a fundamental, and yet challenging, chemical transformation due to the intrinsic inertness of dinitrogen. Whereas industrial ammonia synthesis relies on the energy-intensive Haber-Bosch process, nitrogenase enzymes achieve this transformation under ambient conditions-yet at the expense of a remarkably high ATP demand. Understanding their mode of operation could inspire the development of more efficient synthetic catalysts. In this study, we scrutinize the electrostatic environment surrounding nitrogenase's active site, the so-called M-cluster. Strikingly, we observe that all types of M-clusters exhibit similar trends, with distinct patterns around the individual metal sites that have been proposed as potential N
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