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 …

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 …

Nitrogenases catalyze the reduction of dinitrogen (N2) gas to ammonium at a complex
heterometallic cofactor. This most commonly occurs at the FeMo cofactor (FeMoco), a [Mo …

Abstract The [Mo: 7Fe: 9S: C] iron-molybdenum cofactor (FeMoco) of nitrogenase is the
largest known metal cluster and catalyses the 6-electron reduction of dinitrogen to …

Rock–water–carbon interactions germane to serpentinization in hydrothermal vents have
occurred for over 4 billion years, ever since there was liquid water on Earth. Serpentinization …

Understanding the electronic structures of high‐valent metal complexes aids the
advancement of metal‐catalyzed cross coupling methodologies. A prototypical complex with …

Nitrogenase is one of the most fascinating enzymes in nature, being responsible for all
biological nitrogen reduction. Despite decades of research, it is among the enzymes in …

Studies of multinuclear metal complexes are greatly enhanced by resonant diffraction
measurements, which probe X-ray absorption profiles of crystallographically independent …

Anomalous X-ray diffraction (AXD) and neutron diffraction can be used to
crystallographically distinguish between metals of similar electron density. Despite the use …