Excessive nitrate has been a critical issue in the water environment, originating from the
burning of fossil fuels, inefficient use of nitrogen fertilizers, and discharge of domestic and …

Nitrogenases uniquely reduce atmospheric N2 to bioavailable ammonium. They group into
three isoforms that primarily differ in the architecture of their active-site cofactors. A …

Nitrogenases are best known for catalyzing the reduction of dinitrogen to ammonia at a
complex metallic cofactor. Recently, nitrogenases were shown to reduce carbon dioxide …

From the perspectives of environmental protection and resource reclamation, the
electrocatalytic reduction of nitrate not only removes nitrate but also converts it into value …

Molybdenum nitrogenase plays a crucial role in the biological nitrogen cycle by catalyzing
the reduction of dinitrogen (N2) to ammonia (NH3) under ambient conditions. However, the …

Dangler sites protruding from a core metallocluster were introduced into the bioinorganic
lexicon in 2000 by RD Britt and co-workers in an analysis of the tetramanganese oxygen …

Metal clusters featuring carbon and sulfur donors have coordination environments
comparable to the active site of nitrogenase enzymes. Here, we report a series of di-iron …

The biological conversion of N2 to NH3 is accomplished by the nitrogenase family, which is
collectively comprised of three closely related but unique metalloenzymes. In the present …

The catalytic moiety of nitrogenases contains two complex metalloclusters: The M‐cluster
(also called cofactor), where the catalytic reduction of substrates takes place, and the …

Acknowledging the crucial role of stereochemistry in fields as diverse as total synthesis,
synthetic methodology, spectroscopy, and the study of the origin of life, the 56 th SCS …