Bioinorganic & Materials Chemistry

nitrogenase and the molybdenum-iron cofactor

/ ny-TROJ-uh-nayss /

The air is nearly four-fifths nitrogen gas, yet no plant or animal can use it directly, because N2 is one of the most stubborn molecules in nature — its two nitrogen atoms are locked together by a triple bond so strong it is almost inert. To make the nitrogen that builds proteins and DNA, that bond must be broken open. Industry does this in giant high-pressure reactors at hundreds of degrees (the Haber-Bosch process), but certain humble soil and root bacteria do the same thing at ordinary temperature and pressure, using an enzyme called nitrogenase. Reproducing what nitrogenase does so gently is one of the great unsolved goals of inorganic chemistry.

Nitrogenase carries one of the most remarkable metal clusters known in biology, the iron-molybdenum cofactor, usually written FeMo-co. It is a cage of seven iron atoms and one molybdenum, bridged by sulfur atoms, with a single carbon atom hidden in the exact center — a carbon discovered only recently, sitting inside a cluster of metals, a striking reminder that inorganic chemistry includes carbon too. The N2 molecule is thought to bind across the iron face of this cluster, where a stream of electrons (delivered by iron-sulfur clusters) and protons is fed in to add hydrogen atoms one at a time, gradually weakening and finally cleaving the triple bond to produce two ammonia molecules. The whole conversion is energetically expensive, and the cell pays for it by burning a large amount of its energy currency, ATP, for every nitrogen fixed.

This matters because biological nitrogen fixation, together with Haber-Bosch, feeds the world — roughly half the nitrogen atoms in your body passed through one of these two routes. The contrast is humbling: the industrial process needs extreme heat and pressure, while the enzyme works in cool soil, and chemists still cannot build a catalyst that matches it. An honest caveat: despite decades of study and a now-known structure, the exact step-by-step mechanism by which FeMo-co tames N2 is still debated, including just where and how the N2 binds and what the central carbon does. It stands as a frank example of biology solving a chemistry problem we have not yet fully cracked.

Bacteria living in the root nodules of clover and beans run nitrogenase to turn N2 from the air into ammonia, fertilizing the plant from within — which is why farmers rotate legumes into a field to restore its nitrogen.

Nitrogenase fixes nitrogen at ordinary temperature; industry needs extreme heat and pressure to do the same.

Despite a solved structure, the detailed mechanism of N2 cleavage by FeMo-co is still actively debated — and the central carbon atom sitting inside the metal cluster was a genuine surprise found only in 2011.

Also called
FeMo-coMoFe cofactor钼铁辅因子鉬鐵輔因子nitrogen-fixing enzyme