Journal Article

Partial synthetic models of FeMoco with sulfide and carbyne ligands

Le, Linh N. V., Agapie, Theodor, Bailey, Gwendolyn A., Scott, Anna G.

2021

Overview

Nitrogen-fixing organisms perform dinitrogen reduction to ammonia at an Fe-M (M = Mo, Fe, or V) cofactor (FeMco) of nitrogenase. FeMco displays eight metal centers bridged by sulfides and a carbide having the MFe₇S₈C cluster composition. The role of the carbide ligand, a unique motif in protein active sites, remains poorly understood. Toward addressing how the carbon bridge affects the physical and chemical properties of the cluster, we isolated synthetic models of subsite MFe₃S₃C displaying sulfides and a chelating carbyne ligand. We developed synthetic protocols for structurally related clusters, [Tp*M’Fe₃S₃X]n−, where M’ = Mo or W, the bridging ligand X = CR, N, NR, S, and Tp* = Tris(3,5-dimethyl-1-pyrazolyl)-hydroborate, to study the effects of the identity of the heterometal and the bridging X group on structure and electrochemistry. While the nature of M’ results in minor changes, the chelating, μ₃-bridging carbyne has a large impact on reduction potentials, being up to 1 V more reducing compared to nonchelating N and S analogs.

• Publisher: National Academy of Sciences
• Subject: Ammonia / Carbamates - chemistry / Carbamates - metabolism / Carbides / Carbon - metabolism / Carbyne / Catalytic Domain / Chelation / Chemical properties / Chemistry / Chromium / Clusters / Crystallography, X-Ray / Electrochemistry / Iron / Iron - chemistry / Iron - metabolism / Ligands / Models, Molecular / Molecular Structure / Molybdenum / Molybdenum - chemistry / Molybdenum - metabolism / Molybdoferredoxin - chemistry / Molybdoferredoxin - metabolism / Nitrogen / Nitrogen - metabolism / Nitrogen fixation / Nitrogen Fixation - physiology / Nitrogenase / Nitrogenase - metabolism / Nitrogenation / Oxidation-Reduction / Physical Sciences / Sulfides / Sulfides - chemistry / Sulfides - metabolism / Sulfur - metabolism