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Nuclear resonance vibrational spectroscopy (NRVS) of rubredoxin and MoFe protein crystals
Hyperfine Interactions
  • Y Guo
  • E. Brecht
  • K. Aznavour
  • J. C. Nix
  • Y. Xiao
  • H. Wang
  • S. J. George
  • R. Bau
  • Francis E. Jenney, Jr., Philadelphia College of Osteopathic Medicine
  • et al.
Document Type
Article
Publication Date
1-1-2013
Disciplines
Abstract
We have applied 57Fe nuclear resonance vibrational spectroscopy (NRVS) for the first time to study the dynamics of Fe centers in Iron-sulfur protein crystals, including oxidized wild type rubredoxin crystals from Pyrococcus furiosus, and the MoFe protein of nitrogenase from Azotobacter vinelandii. Thanks to the NRVS selection rule, selectively probed vibrational modes have been observed in both oriented rubredoxin and MoFe protein crystals. The NRVS work was complemented by extended X-ray absorption fine structure spectroscopy (EXAFS) measurements on oxidized wild type rubredoxin crystals from Pyrococcus furiosus. The EXAFS spectra revealed the Fe-S bond length difference in oxidized Pf Rd protein, which is qualitatively consistent with the crystal structure. © 2012 Springer Science+Business Media B.V.
Comments

This article was published in Hyperfine Interactions, Volume 222, Issue SUPPL.2, Pages 77-90.

The published version is available at http://dx.doi.org/10.1007/s10751-012-0703-7.

Copyright © 2013 Springer.

Citation Information
Y Guo, E. Brecht, K. Aznavour, J. C. Nix, et al.. "Nuclear resonance vibrational spectroscopy (NRVS) of rubredoxin and MoFe protein crystals" Hyperfine Interactions Vol. 222 Iss. SUPPL.2 (2013) p. 77 - 90
Available at: http://works.bepress.com/francis_jenney/25/