The nitrogenase enzyme complex can be separated into two components – the Fe protein and the MoFe protein – neither of which has catalytic activity by itself (Figure 13.13):
The Fe protein is the smaller of the two components and has two identical subunits that vary in mass from 30 to 72 kDa each, depending on the bacterial species. Each subunit contains an iron-sulfur cluster (4 Fe and 4 S²-), which participates in the redox reactions that convert N2 to NH3. The Fe protein is irreversibly inactivated by O2 with typical half-decay times of 30 to 45 seconds.
The MoFe protein has four subunits, with a total molecular mass of 180 to 235 kDa, depending on the bacterial species. Each subunit has two Mo–Fe–S clusters. The MoFe protein is also inactivated by O2, with a half-decay time in air of 10 minutes.
In the overall nitrogen reduction reaction (see Figure 13.13), ferredoxin serves as an electron donor to the Fe protein, which in turn hydrolyzes ATP and reduces the MoFe protein.
"Plant Physiology and Development" int'l 6e - Taiz, L., Zeiger, E., Møller, I.M., Murphy, A.