In this study, we set out to scrutinize the role electrostatics play in the biological nitrogen fixation mechanism catalyzed by nitrogenase. We hypothesize that, just like in any other enzyme, the active site of nitrogenases is surrounded by an exquisitely tailored protein matrix that significantly affects catalysis, without direct interaction with the M-cofactor or its substrates. Collectively, these (partial) charges exert strong local electric fieldsexperimental estimates indicate that field strengths of several VÅ -1 are not uncommon. Such field strengths exert a marked influence on catalysis, whereby both kinetic and thermodynamic aspects can be affected, even for apolar substrates as local electric fields tend to wake-up dormant ionicity/charge separation in molecules. Many examples of electrostatic catalysis have been reported in recent years. Interestingly, simulations by Shaik and co-workers recently indicated that despite its limited polarizability in the gas-phase, the energy barrier to N2-activation in Frustrated Lewis Pairs can be modulated by dozens of kcal/mol through the application of electric fields of a mere 0.2-0.3 VÅ -1 . Considering this field strength is rather modest, compared to what is often computed around the active site of enzymes, we surmised that nitrogenases may also take advantage of electrostatics to lower the barrier to N2 activation, and ultimately reduce it. To explore this hypothesis, we set out to quantify the electric field exerted by the protein matrix, based on the crystal structure of a variety of nitrogenases. We observe clear patterns in the electric fields surrounding -as well as in between -the metal sites of the M-clusters, and the observed trends persist across the entire family of FeMoco, FeVco and FeFeco nitrogenases. Interestingly, we are able to connect these findings to mechanistic results reported by Bjornsson et al. as well as Head-Gordon et al., and others, which indicates that electrostatics may indeed play a vital role in nitrogenase activity.