Functional insights into the nitrogenase-like enzyme superfamily
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 F<sub>430</sub> 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.
Authors
- Johannes G. Rebelein (ORCID: https://orcid.org/0000-0003-2560-716X)
- Marcello Herzog (ORCID: https://orcid.org/0009-0007-9817-8622)
- Ana Lago-Maciel
Institutions
- Loewe Center for Synthetic Microbiology (DE)
- Max Planck Institute for Terrestrial Microbiology (DE)
Publication Details
- Journal
- Trends in Biochemical Sciences
- Published
- 2026-01-02
- DOI
- https://doi.org/10.1016/j.tibs.2025.11.009
- Primary Topic
- Metalloenzymes and iron-sulfur proteins
- Type
- article
- Field-Weighted Citation Impact
- 0.00
Funders
- International Max Planck Research School for Environmental, Cellular and Molecular Microbiology
- Deutsche Forschungsgemeinschaft
- Max-Planck-Gesellschaft