Metal–Sulfur Compounds in N2 Reduction and Nitrogenase-Related Chemistry
- 28 May 2020
- journal article
- review article
- Published by American Chemical Society (ACS) in Chemical Reviews
- Vol. 120 (12), 5194-5251
- https://doi.org/10.1021/acs.chemrev.9b00544
Abstract
Transition metal–sulfur (M–S) compounds are an indispensable means for biological systems to convert N2 into NH3 (biological N2 fixation), and these may have emerged by chemical evolution from a prebiotic N2 fixation system. With a main focus on synthetic species, this article provides a comprehensive review of the chemistry of M–S compounds related to the conversion of N2 and the structures/functions of the nitrogenase cofactors. Three classes of M–S compounds are highlighted here: multinuclear M–S clusters structurally or functionally relevant to the nitrogenase cofactors, mono- and dinuclear transition metal complexes supported by sulfur-containing ligands in N2 and N2Hx (x = 2, 4) chemistry, and metal sulfide-based solid materials employed in the reduction of N2. Fair assessments on these classes of compounds revealed that our understanding is still limited in N2 reduction and related substrate reductions. Our aims of this review are to compile a collection of studies performed at atomic to mesoscopic scales and to present potential opportunities for elucidating the roles of metal and sulfur atoms in the biological N2 fixation that might be helpful for the development of functional materials.Funding Information
- Takeda Science Foundation
- Ministry of Education, Culture, Sports, Science and Technology (18H04246, 19H02733)
- Yazaki Memorial Foundation for Science and Technology
This publication has 401 references indexed in Scilit:
- Selenium as a Structural Surrogate of Sulfur: Template-Assisted Assembly of Five Types of Tungsten–Iron–Sulfur/Selenium Clusters and the Structural Fate of Chalcogenide ReactantsJournal of the American Chemical Society, 2012
- ATP‐Independent Formation of Hydrocarbons Catalyzed by Isolated Nitrogenase CofactorsAngewandte Chemie International Edition, 2012
- Specific Incorporation of Chalcogenide Bridge Atoms in Molybdenum/Tungsten-Iron-Sulfur Single Cubane ClustersInorganic Chemistry, 2011
- Electron Transfer within Nitrogenase: Evidence for a Deficit-Spending MechanismBiochemistry, 2011
- Spectroscopic Characterization of the Isolated Iron–Molybdenum Cofactor (FeMoco) Precursor from the Protein NifENAngewandte Chemie International Edition, 2011
- Uncoupling Nitrogenase: Catalytic Reduction of Hydrazine to Ammonia by a MoFe Protein in the Absence of Fe Protein-ATPJournal of the American Chemical Society, 2010
- Characterization of Isolated Nitrogenase FeVcoJournal of the American Chemical Society, 2010
- Hydroxide-Promoted Core Conversions of Molybdenum−Iron−Sulfur Edge-Bridged Double Cubanes: Oxygen-Ligated Topological PN ClustersInorganic Chemistry, 2007
- Diazene (HNNH) Is a Substrate for Nitrogenase: Insights into the Pathway of N2 ReductionBiochemistry, 2007
- Stabilization of Reduced Molybdenum−Iron−Sulfur Single- and Double-Cubane Clusters by Cyanide LigationInorganic Chemistry, 2006