Nitrogenase iron-molybdenum cofactor binding site: Protein conformational changes associated with cofactor binding
Active nitrogenase MoFe-protein requires the assembly and insertion of an unusual molybdenum containing Fe:S cluster, the FeMoco.
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Cited by (12)
Sequential and differential interaction of assembly factors during nitrogenase MoFe protein maturation
2018, Journal of Biological ChemistryCitation Excerpt :In contrast to Strep-tagged MoFe protein produced by a ΔnifH strain, two different proteins co-purify with Strep-tagged MoFe protein produced by a ΔnifB strain (Fig. 5). These proteins, NafY and NifY, share primary structure similarity to each other and have been variously proposed to act as “molecular props” that assist FeMo-cofactor insertion or as FeMo-cofactor–trafficking proteins (33–39). These possibilities are not mutually exclusive, and indeed NafY has already been shown to co-purify with apo-MoFe protein produced by a NifB-deficient strain (33, 35).
A sterile α-motif domain in NafY targets apo-NifDK for iron-molybdenum cofactor delivery via a tethered domain
2011, Journal of Biological ChemistryCitation Excerpt :Because the surface of n-NafY displays a large negatively charged region (supplemental Fig. S3), it is possible that n-NafY would bind between the positively charged insertion funnel and the disordered region of apo-NifDK (NifD residues 381–407) that would act as a lid (29). Selective alkylation studies have shown that NafY-stabilized apo-NifDK has the side chain of α-Cys275 exposed to solvent (α-Cys275 serves as ligand to FeMo-co) (28). Fourth, it could also be possible that n-NafY increases the KD of the FeMo-co·apo-NifDK complex.
Comparison of iron-molybdenum cofactor-deficient nitrogenase MoFe proteins by x-ray absorption spectroscopy. Implications for P-cluster biosynthesis
2004, Journal of Biological ChemistryCitation Excerpt :This result helps define the role of the Fe protein (NifH) in MoFe biosynthesis. It is presumed that the Fe protein is involved in forming the open conformation of the MoFe protein that accepts preassembled FeMoco (67). The protein-protein interaction that leads to this conformational change could be driven by, or could drive, the condensation of two [Fe4S4] centers in “apoMoFe protein” to form the P-cluster.
Purification and Characterization of NafY (Apodinitrogenase γ Subunit) from Azotobacter vinelandii
2004, Journal of Biological ChemistryStructure, Function, and Biosynthesis of the Metallosulfur Clusters in Nitrogenases
1999, Advances in Inorganic ChemistryBiosynthesis of Nitrogenase Cofactors
2020, Chemical Reviews