Nuclear resonance vibrational spectroscopy (NRVS) of rubredoxin and MoFe protein crystals

We have applied 57 Fe 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...

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Bibliographic Details
Published in:Hyperfine interactions 2013-12, Vol.222 (Suppl 2), p.77-90
Main Authors: Guo, Yisong, Brecht, Eric, Aznavour, Kristen, Nix, Jay C., Xiao, Yuming, Wang, Hongxin, George, Simon J., Bau, Robert, Keable, Stephen, Peters, John W., Adams, Michael W. W., Jr, Francis E. Jenney, Sturhahn, Wolfgang, Alp, Ercan E., Zhao, Jiyong, Yoda, Yoshitaka, Cramer, Stephen P.
Format: Article
Language:English
Subjects:
Atomic
CHEM
Condensed Matter Physics
Hadrons
Heavy Ions
Molecular
Nuclear Physics
Optical and Plasma Physics
Physics
Physics and Astronomy
Surfaces and Interfaces
Thin Films
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Summary:We have applied 57 Fe 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.
ISSN:0304-3843
1572-9540
DOI:10.1007/s10751-012-0643-2