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X-Ray Absorption Spectroscopy of Nitrogenase Mo-Fe Protein

Published online by Cambridge University Press:  15 February 2011

J. Chen ,
J. Christiansen ,
S. George ,
R. Tittsworth ,
B. Hales ,
N. Campobasso ,
J. Bolin  and
S. P. Cramer
J. Chen
Affiliation:
Department of Applied Science, University of California, Davis, CA 95616
J. Christiansen
Affiliation:
Department of Applied Science, University of California, Davis, CA 95616
S. George
Affiliation:
Department of Applied Science, University of California, Davis, CA 95616
R. Tittsworth
Affiliation:
Department of Chemistry, Louisiana State University, Baton Rouge, LA 70803
B. Hales
Affiliation:
Department of Chemistry, Louisiana State University, Baton Rouge, LA 70803
N. Campobasso
Affiliation:
Department of Biological Sciences, Purdue University, West Lafayette, IN 47907.
J. Bolin
Affiliation:
Department of Biological Sciences, Purdue University, West Lafayette, IN 47907.
S. P. Cramer
Affiliation:
Department of Applied Science, University of California, Davis, CA 95616
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Abstract

We have studied both the atomic and electronic structures of nitrogenase Mo-Fe proteins using EXAFS and L-edge spectroscopy. The Mo and Fe K-edge EXAFS data show not only 2.37, 2.70, 2.29, and 2.63 Å first shell Mo-S, Mo-Fe, Fe-S, and Fe-Fe distances, but also 3.8, 4.3 and 5.1 Å second shell Fe-Fe, Fe-S, and Mo-Fe interactions. These observed distances are consistent with recent crystallographic models for the M-center. The average Mcenter distances have been defined with unprecedented accuracy. The nitrogenase Fe L-edge spectra have been obtained for the first time, and the result suggests that the Fe exists in both Fe2+ and Fe3+ states.

Type
Research Article
Information
MRS Online Proceedings Library (OPL) , Volume 307: Symposium L – Applications of Synchrotron Radiation Techniques to Materials Science , 1993 , 63
Copyright
Copyright © Materials Research Society 1993

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References

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