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 …

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 …

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 …

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

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

The reaction catalyzed by the nitrogenase enzyme involves breaking the stable triple bond
of the dinitrogen molecule and is consequently considered among the most challenging …

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

Conspectus Metal ions and metallocofactors play important roles in a broad range of
biochemical reactions. Accordingly, it has been estimated that as much as 25–50% of the …

Enzymes with iron-containing active sites play crucial roles in catalysing a myriad of
oxidative reactions essential to aerobic life. Defining the three-dimensional structures of iron …

AlphaFold2 has revolutionized structural biology by offering unparalleled accuracy in
predicting protein structures. Traditional methods for determining protein structures, such as …