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Literature summary extracted from

  • Wiig, J.A.; Hu, Y.; Ribbe, M.W.
    NifEN-B complex of Azotobacter vinelandii is fully functional in nitrogenase FeMo cofactor assembly (2011), Proc. Natl. Acad. Sci. USA, 108, 8623-8627.
    View publication on PubMedView publication on EuropePMC

Organism

EC Number Organism UniProt Comment Textmining
1.18.6.1 Azotobacter vinelandii
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Cofactor

EC Number Cofactor Comment Organism Structure
1.18.6.1 [4Fe-4S]-center NifB and NifEN are two essential elements immediately adjacent to each other along the biosynthetic pathway of FeMoco. The 8Fe-precursor is present in the NifEN entity of a synthetic NifEN-B fusion protein, and additional [Fe4S4]-type cluster species are present in the NifB entity of NifEN-B. The cluster species in NifEN-B consist of both SAM-motif- and non-SAM-motif-bound [Fe4S4]-type clusters. The non-SAM-motif [Fe4S4]-cluster is a NifB-bound intermediate of FeMoco assembly, which could be converted to the 8Fe-precursor in a SAM-dependent mechanism Azotobacter vinelandii

General Information

EC Number General Information Comment Organism
1.18.6.1 metabolism NifB and NifEN are two essential elements immediately adjacent to each other along the biosynthetic pathway of FeMoco. The 8Fe-precursor is present in the NifEN entity of a synthetic NifEN-B fusion protein, and additional [Fe4S4]-type cluster species are present in the NifB entity of NifEN-B. The cluster species in NifEN-B consist of both SAM-motif- and non-SAM-motif-bound [Fe4S4]-type clusters. The non-SAM-motif [Fe4S4]-cluster is a NifB-bound intermediate of FeMoco assembly, which could be converted to the 8Fe-precursor in a SAM-dependent mechanism Azotobacter vinelandii