Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
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Journal
IF	>30 >20 >10 >5 all

Title	Structural and Functional Characterization of Heterologous Nitrogenase Complexes.
Journal, issue, pages	Biochemistry, Year 2026
Publish date	Jul 2, 2026
Authors	Yizhou Li / Sarah M Narehood / Brian D Cook / Kelly L McGuire / Mark A Herzik / F Akif Tezcan /
PubMed Abstract	Nitrogenase is the only known enzyme that catalyzes the reduction of dinitrogen to ammonia. The most prevalent isozyme, molybdenum nitrogenase, comprises the catalytic molybdenum-iron protein (MoFeP) ...Nitrogenase is the only known enzyme that catalyzes the reduction of dinitrogen to ammonia. The most prevalent isozyme, molybdenum nitrogenase, comprises the catalytic molybdenum-iron protein (MoFeP) and the ATP-dependent reductase iron protein (FeP). Although Mo-nitrogenases are widespread across bacteria and archaea and appear to share conserved mechanistic and structural features, FeP and MoFeP show considerable sequence variability across diazotrophs. This raises questions about the conservation of chemomechanical mechanisms coupling FeP-dependent ATP hydrolysis and electron transfer to MoFeP, and about the functional compatibility of nitrogenase components from divergent species. Previous studies showed that some heterologous FeP-MoFeP pairs can functionally complement each other, whereas other pairs lack catalytic activity, but the absence of structural information on such heterologous pairs has limited mechanistic understanding. To this end, we investigated the functional and structural compatibility of FeP and MoFeP from () and (), two phylogenetically and ecologically distinct species. Building on our prior work with -nitrogenase and recently developed cryogenic electron microscopy (cryoEM) protocols, we determined the ADP·BeF-trapped structure of the homologous FeP-MoFeP complex and showed that it adopted the same geometry as its counterpart. Activity measurements showed that heterologous combinations retained 60-80% of homologous catalytic activities despite 30-50% sequence divergence in FeP and MoFeP. High-resolution cryoEM structures of FeP-MoFeP and FeP-MoFeP corroborated these activities and revealed that functional complementation tolerates substantial sequence variation when the core structural elements supporting ATP binding/hydrolysis, protein-protein interaction, electron transfer, and substrate reduction are conserved.
External links	Biochemistry / PubMed:42390130
Methods	EM (single particle)
Resolution	2.15 - 2.92 Å
Structure data	75566 10zk EMDB-75566, PDB-10zk: CryoEM structure of Gluconacetobacter diazotrophicus nitrogenase complex (2:1 FeP:MoFeP) inhibited by BeFx (C2 symmetry) Method: EM (single particle) / Resolution: 2.73 Å 75567 10zl EMDB-75567, PDB-10zl: CryoEM structure of Gluconacetobacter diazotrophicus MoFeP (C2 symmetry) Method: EM (single particle) / Resolution: 2.15 Å 75568 10zm EMDB-75568, PDB-10zm: CryoEM structure of heterologous nitrogenase complex (2:1 G. diazotrophicus-FeP:A. vinelandii-MoFeP) inhibited by BeFx (C2 symmetry) Method: EM (single particle) / Resolution: 2.22 Å 75569 10zn EMDB-75569, PDB-10zn: CryoEM structure of Heterologous nitrogenase complex (2:1 A. vinelandii-FeP:G. diazotrophicus-MoFeP) inhibited by BeFx (C2 symmetry) Method: EM (single particle) / Resolution: 2.92 Å
Chemicals	ChemComp-HCA: 3-HYDROXY-3-CARBOXY-ADIPIC ACID ChemComp-ICS: iron-sulfur-molybdenum cluster with interstitial carbon ChemComp-CLF: FE(8)-S(7) CLUSTER ChemComp-FE: Unknown entry ChemComp-SF4: IRON/SULFUR CLUSTER ChemComp-MG: Unknown entry ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying moleculeYM ChemComp-0BE: BERYLLIUM ChemComp-HOH*: WATER
Source	gluconacetobacter diazotrophicus pa1 5 (bacteria) azotobacter vinelandii dj (bacteria)
Keywords	OXIDOREDUCTASE / Nitrogenase / Nitrogenase complex / Gluconacetobacter diazotrophicus / molybdenum-iron protein / Iron protein / MoFeP / FeP / FeP-MoFeP / Heterologous Nitrogenase complex / Azotobacter vinelandii