Journal
JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY
Volume 23, Issue 7, Pages 1049-1056Publisher
SPRINGER
DOI: 10.1007/s00775-018-1602-4
Keywords
Biological nitrogen fixation; Vanadium nitrogenase; Fe protein; Dinitrogenase reductase; X-ray crystallography
Funding
- Deutsche Forschungsgemeinschaft [RTG 1976, PP 1927]
- European Research Council [310656]
- European Research Council (ERC) [310656] Funding Source: European Research Council (ERC)
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Nitrogenases catalyze the biological fixation of inert N-2 into bioavailable ammonium. They are bipartite systems consisting of the catalytic dinitrogenase and a complementary reductase, the Fe protein that is also the site where ATP is hydrolyzed to drive the reaction forward. Three different subclasses of dinitrogenases are known, employing either molybdenum, vanadium or only iron at their active site cofactor. Although in all these classes the mode and mechanism of interaction with Fe protein is conserved, each one encodes its own orthologue of the reductase in the corresponding gene cluster. Here we present the 2.2 angstrom resolution structure of VnfH from Azotobacter vinelandii, the Fe protein of the alternative, vanadium-dependent nitrogenase system, in its ADP-bound state. VnfH adopts the same conformation that was observed for NifH, the Fe protein of molybdenum nitrogenase, in complex with ADP, representing a state of the functional cycle that is ready for reduction and subsequent nucleotide exchange. The overall similarity of NifH and VnfH confirms the experimentally determined cross-reactivity of both ATP-hydrolyzing reductases.
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