BiologyEnvironmental ScienceChemistry

Ana Lago-Maciel, Marcello Herzog, J. Rebelein

2026.1.1TRENDS IN BIOCHEMICAL SCIENCES

DOI: 10.1016/j.tibs.2025.11.009

tlooto Summary

The structural and functional diversity of the nitrogen fixation-like enzyme superfamily is explored and its potential for the production of chemical building blocks beyond ammonia formation is explored.

Abstract

Nitrogenases are the only enzymes capable of converting atmospheric nitrogen into bioavailable ammonia, an essential process for all life on Earth. Early ancestors of bona fide nitrogenases and their maturases gave rise to several structural homologues with diverse functions. The nitrogen fixation-like enzyme superfamily comprises ancient metalloproteins involved in elemental processes that range from the biosynthesis of bacteriochlorophyll in bacterial photosynthesis to the biosynthesis of cofactor F430 in archaeal methanogenesis. Recently, new functions of nitrogenase-like enzymes in sulfur scavenging were discovered and have spurred interest due to the simultaneous production of small hydrocarbons. Here we explore the structural and functional diversity of the nitrogen fixation-like enzyme superfamily and its potential for the production of chemical building blocks beyond ammonia formation.

Citation format

LAGO-MACIEL, Ana; HERZOG, Marcello; REBELEIN, J. Functional insights into the nitrogenase-like enzyme superfamily. TRENDS IN BIOCHEMICAL SCIENCES, 2026, 51(2): 187–202.