Nitrogenase MoFe-protein at 1.16 A resolution: a central ligand in the FeMo-cofactor.

  title={Nitrogenase MoFe-protein at 1.16 A resolution: a central ligand in the FeMo-cofactor.},
  author={Oliver Einsle and F Akif Tezcan and Susana L A Andrade and Benedikt Schmid and Mika Yoshida and James W. Howard and Douglas C Rees},
  volume={297 5587},
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… CONTINUE READING
Related Discussions
This paper has been referenced on Twitter 1 time. VIEW TWEETS

From This Paper

Topics from this paper.


Publications citing this paper.
Showing 1-10 of 79 extracted citations

Fe-N2/CO complexes that model a possible role for the interstitial C atom of FeMo-cofactor (FeMoco).

Proceedings of the National Academy of Sciences of the United States of America • 2013
View 5 Excerpts
Highly Influenced

Biosynthesis of the metalloclusters of molybdenum nitrogenase.

Microbiology and molecular biology reviews : MMBR • 2011
View 4 Excerpts
Highly Influenced

Surprising cofactors in metalloenzymes.

Current opinion in structural biology • 2003
View 4 Excerpts
Highly Influenced

Similar Papers

Loading similar papers…