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 …

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 …

Nitrogenases catalyze the reduction of dinitrogen (N 2) gas to ammonium at a complex
heterometallic cofactor. This most commonly occurs at the FeMo cofactor (FeMoco), a [Mo …

Biological nitrogen fixation, the conversion of atmospheric N2 to a form utilizable by higher
organisms, is catalyzed by the enzyme nitrogenase. This enzyme is found in relatively few …

Three genetically distinct, but structurally similar, isozymes of nitrogenase catalyze
biological N2 reduction to 2NH3: Mo-, V-, and Fe-nitrogenase, named respectively for the …

Vanadium is a trace element that plays an important, perhaps essential and general role in
the regulation of enzymatic phosphorylations. Several forms of life, including the fly agaric …

Nitrogenase is the catalytic component of the biological nitrogen-fixation system which
reduces atmospheric N2 to ammonia. As shown in Figure 1 the en-zyme is actually …

V-nitrogenase is both genetically and biochemically similar to the more intensively studied
Mo-nitrogenase. The VFe protein contains P cluster redox centres and a catalytic FeVco …

In sharp contrast to most of the first row transition metal ions, the biochemistry of vanadium
has been relatively uninvestigated until recently. Sporadic reports dealing with the …