Enzymatic catalysis has fueled considerable interest from chemists due to its high efficiency
and selectivity. However, the structural complexity and vulnerability hamper the application …

The electrochemical method of combining N2 and H2O to produce ammonia (ie, the
electrochemical nitrogen reduction reaction [E‐NRR]) continues to draw attention as it is …

Gases like H2, N2, CO2, and CO are increasingly recognized as critical feedstock in “green”
energy conversion and as sources of nitrogen and carbon for the agricultural and chemical …

The production of synthetic ammonia remains dependent on the energy-and capital-
intensive Haber–Bosch process. Extensive research in molecular catalysis has …

The reduction of dinitrogen to ammonia by nitrogenase reflects a complex choreography
involving two component proteins, MgATP and reductant. At center stage of this process …

Reduction of N2 by nitrogenases occurs at an organometallic iron cofactor that commonly
also contains either molybdenum or vanadium. The well-characterized resting state of the …

Nitrogenase is the only enzyme capable of reducing N2 to NH3. This challenging reaction
requires the coordinated transfer of multiple electrons from the reductase, Fe-protein, to the …

Nitrogenases are responsible for biological nitrogen fixation, a crucial step in the
biogeochemical nitrogen cycle. These enzymes utilize a two-component protein system and …

Biological nitrogen fixation is catalyzed by the enzyme nitrogenase, which facilitates the
cleavage of the relatively inert triple bond of N2. Nitrogenase is most commonly associated …

Numerous reports claim that quantum advantage, which should emerge as a direct
consequence of the advent of quantum computers, will herald a new era of chemical …