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Nitrogenase MoFe-Protein at 1.16 Å Resolution: A Central Ligand in the FeMo-Cofactor

Einsle, Oliver, Tezcan, F. Akif, Andrade, Susana L. A., Schmid, Benedikt, Yoshida, Mika, Howard, James B., Rees, Douglas C.·2002·Science

Abstract

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.

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Metadata

Authors
Einsle, O., Tezcan, F. A., Andrade, S. L. A., Schmid, B., Yoshida, M., Howard, J. B., & Rees, D. C.
Venue
Science
Published
2002-09-06
Volume
297
Issue
5587
Pages
1696-1700
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W1986546695
Cited by
1,093
References
0
FWCI
61.46
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Nitrogenase MoFe-Protein at 1.16 Å Resolution: A Central Ligand in the FeMo-Cofactor. https://app.cochat.ai/papers/10.1126/science.1073877
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Einsle, O., Tezcan, F. A., Andrade, S. L. A., Schmid, B., Yoshida, M., Howard, J. B., & Rees, D. C. (2002). Nitrogenase MoFe-Protein at 1.16 Å Resolution: A Central Ligand in the FeMo-Cofactor. Science. https://doi.org/10.1126/science.1073877

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