Function, Structure, and Regulation of Nitrogen Fixation-like Metalloproteins for Nitrogen, Energy, Carbon, and Sulfur Metabolism

Description

North and Shafaat review a family of metal loaded enzymes that look like nitrogen fixers but do other jobs. They run pieces of the nitrogen, carbon, sulfur, and energy cycles. Nitrogenases turn nitrogen into ammonia, yet their cousins were filed as oddities. Their 2026 review gathers discoveries across bacteria, archaea, algae, and plants, comparing structures, cofactors, chemistry, and regulation against the nitrogenase template.

The family spans iron clusters to cofactors once thought unique to nitrogenase. Named members include the enzymes that finish chlorophyll in the dark for photosynthetic cells, and the pair that builds the F430 cofactor methane making archaea depend on. A reductase that cleaves sulfur compounds in bacteria is another. Spectroscopy tools borrowed from nitrogenase research reveal how each variant's metal core enforces its reaction. The gaps the authors flag, what sets one system's specificity apart and how cells switch them, define the next experiments.

Catalog record

Source: https://europepmc.org/article/MED/PMC13474568