Nitrogenase is the enzyme that catalyzes biological N2 reduction to NH3. This enzyme
achieves an impressive rate enhancement over the uncatalyzed reaction. Given the high …

The multiscaling quantum mechanics/molecular mechanics (QM/MM) approach was
introduced in 1976, while the extensive acceptance of this methodology started in the 1990s …

Metallic conductive 1T phase molybdenum sulfide (MoS2) has been identified as promising
anode for sodium ion (Na+) batteries, but its metastable feature makes it difficult to obtain …

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 …

X-ray spectroscopy has had a significant and continually growing impact on catalysis
research for nearly 50 years. In particular, the ability to obtain element selective electronic …

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

Hybrid quantum mechanical/molecular mechanical (QM/MM) methods are a powerful
computational tool for the investigation of all forms of catalysis, as they allow for an accurate …

In providing bioavailable nitrogen as building blocks for all classes of biomacromolecules,
biological nitrogen fixation is an essential process for all organismic life. Only a single …

The FeMo cofactor (FeMoco) of Mo nitrogenase is responsible for reducing dinitrogen to
ammonia, but it requires the addition of 3–4 e–/H+ pairs before N2 even binds. A binding …

The open-shell electronic structure of iron–sulfur clusters presents considerable challenges
to quantum chemistry, with the complex iron–molybdenum cofactor (FeMoco) of nitrogenase …