1m1n
Nitrogenase MoFe protein from Azotobacter vinelandii
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OverviewOverview
A high-resolution crystallographic analysis of the nitrogenase MoFe-protein reveals a previously unrecognized ligand coordinated to six iron atoms in the center of the catalytically essential FeMo-cofactor. The electron density for this ligand is masked in structures with resolutions lower than 1.55 angstroms, owing to Fourier series termination ripples from the surrounding iron and sulfur atoms in the cofactor. The central atom completes an approximate tetrahedral coordination for the six iron atoms, instead of the trigonal coordination proposed on the basis of lower resolution structures. The crystallographic refinement at 1.16 angstrom resolution is consistent with this newly detected component being a light element, most plausibly nitrogen. The presence of a nitrogen atom in the cofactor would have important implications for the mechanism of dinitrogen reduction by nitrogenase.
About this StructureAbout this Structure
1M1N is a Protein complex structure of sequences from Azotobacter vinelandii with , , and as ligands. Active as Nitrogenase, with EC number 1.18.6.1 Full crystallographic information is available from OCA.
ReferenceReference
Nitrogenase MoFe-protein at 1.16 A resolution: a central ligand in the FeMo-cofactor., Einsle O, Tezcan FA, Andrade SL, Schmid B, Yoshida M, Howard JB, Rees DC, Science. 2002 Sep 6;297(5587):1696-700. PMID:12215645
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