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| Title | Trafficking of a nitrogenase FeMo-cofactor assembly intermediate. |
|---|---|
| Journal, issue, pages | Nat Chem Biol, Vol. 22, Issue 5, Page 822-828, Year 2026 |
| Publish date | Mar 23, 2026 |
 Authors | Florian F Schneider / Julia S Martin Del Campo / Lin Zhang / Dennis R Dean / Oliver Einsle /    |
| PubMed Abstract | The maturation of the unique FeMo-cofactor of molybdenum nitrogenase is a multistep process requiring the sequential action of a series of maturase complexes. As a final step, the NifEN complex forms ...The maturation of the unique FeMo-cofactor of molybdenum nitrogenase is a multistep process requiring the sequential action of a series of maturase complexes. As a final step, the NifEN complex forms FeMo-cofactor from the precursor NifB-co, also called L-cluster, through replacement of an apical iron ion by molybdenum and the attachment of an organic homocitrate ligand. NifB-co is delivered by a small cofactor chaperone, NifX, and initially bound near the surface of the maturase NifEN. Here, we report high-resolution cryo-electron microscopy structures of NifEN in complex with NifX, showing NifB-co binding to NifEN in full detail, capturing both interacting partners in the act of cluster transfer. In a dynamic transfer complex, the large metal cluster is coordinated by single residues from both NifEN and NifX. In silico studies concur with these structures but suggest a third, internal conversion site where cluster maturation likely takes place. |
 External links | Nat Chem Biol / PubMed:41872497 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 2.14 - 2.16 Å |
| Structure data | EMDB-52782, PDB-9ian: EMDB-52783, PDB-9iao: |
| Chemicals |  ChemComp-S5Q:  ChemComp-SF4:  ChemComp-MG:  ChemComp-HOH: |
| Source |
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 Keywords | METAL BINDING PROTEIN / nitrogenase cofactor maturase |
azotobacter vinelandii dj (bacteria)