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• W2898382642 abstract "Significance This report critically evaluates the mechanism by which nitrogenase cleaves the N≡N triple bond. It assesses the thermodynamic driving force provided by the accompanying, apparently “wasteful,” reductive elimination of an H 2 , and explains how the enzyme mechanistically couples exothermic H 2 formation to endothermic triple-bond cleavage in a nearly thermoneutral equilibrium process, thereby preventing the “futile” generation of two H 2 without N 2 reduction. This evaluation rests on a critical assessment of the density functional theory flavors needed to properly treat nitrogenase, and a demonstration that to prevent spurious disruption of FeMo-co upon 4[ e − /H + ] accumulation, one must employ a nitrogenase structural model that includes all residues interacting directly with FeMo-co, either via specific H-bond interactions, nonspecific electrostatic interactions, or steric confinement." @default.
• W2898382642 created "2018-11-02" @default.
• W2898382642 creator A5078039482 @default.
• W2898382642 creator A5080373573 @default.
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• W2898382642 date "2018-10-24" @default.
• W2898382642 modified "2023-10-16" @default.
• W2898382642 title "Critical computational analysis illuminates the reductive-elimination mechanism that activates nitrogenase for N ₂ reduction" @default.
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• W2898382642 doi "https://doi.org/10.1073/pnas.1810211115" @default.
• W2898382642 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6233137" @default.
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