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

Yisong Guo; Eric Brecht; Kristen Aznavour; Jay C. Nix; Yuming Xiao; Hongxin Wang; Simon J. George; Robert Bau; Stephen Keable; John W. Peters; Michael W.W. Adams; Francis E. Jenney; Wolfgang Sturhahn; Ercan E. Alp; Jiyong Zhao; Yoshitaka Yoda; Stephen P. Cramer

doi:10.1007/s10751-012-0643-2

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

Yisong Guo, Eric Brecht, Kristen Aznavour, Jay C. Nix, Yuming Xiao, Hongxin Wang, Simon J. George, Robert Bau, Stephen Keable, John W. Peters, Michael W.W. Adams, Francis E. Jenney, Wolfgang Sturhahn, Ercan E. Alp, Jiyong Zhao, Yoshitaka Yoda, Stephen P. Cramer

Research output: Contribution to journal › Article › peer-review

11 Scopus citations

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.

Original language	English
Pages (from-to)	77-90
Number of pages	14
Journal	Hyperfine Interactions
Volume	222
Issue number	2
DOIs	https://doi.org/10.1007/s10751-012-0643-2
State	Published - Dec 2013
Externally published	Yes

Funding

Acknowledgements This work was funded by NIH GM-65440 (SPC), EB-001962 (SPC), the DOE Office of Biological and Environmental Research (SPC) and the DOE Office of Basic Energy Sciences (MWWA) Use of the APS is supported by the 334 DOE Office of Basic Energy Sciences. The experiments at SPring-8 were performed with the approval of Japan Synchrotron Radiation Research Institute. (Proposal No.: 2010B0032 - 2012A0032).

Keywords

EXAFS
Mössbauer
Nitrogenase
Normal mode analysis
NRVS
Nuclear resonance vibrational spectroscopy
Nuclear resonant scattering
Rubredoxin
Synchrotron radiation

Access to Document

10.1007/s10751-012-0643-2

Cite this

Guo, Y., Brecht, E., Aznavour, K., Nix, J. C., Xiao, Y., Wang, H., George, S. J., Bau, R., Keable, S., Peters, J. W., Adams, M. W. W., Jenney, F. E., Sturhahn, W., Alp, E. E., Zhao, J., Yoda, Y., & Cramer, S. P. (2013). Nuclear resonance vibrational spectroscopy (NRVS) of rubredoxin and MoFe protein crystals. Hyperfine Interactions, 222(2), 77-90. https://doi.org/10.1007/s10751-012-0643-2

@article{17f1fd30433849ed9eea460dc3d75bc8,

title = "Nuclear resonance vibrational spectroscopy (NRVS) of rubredoxin and MoFe protein crystals",

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.",

keywords = "EXAFS, M{\"o}ssbauer, Nitrogenase, Normal mode analysis, NRVS, Nuclear resonance vibrational spectroscopy, Nuclear resonant scattering, Rubredoxin, Synchrotron radiation",

author = "Yisong Guo and Eric Brecht and Kristen Aznavour and Nix, \{Jay C.\} and Yuming Xiao and Hongxin Wang and George, \{Simon J.\} and Robert Bau and Stephen Keable and Peters, \{John W.\} and Adams, \{Michael W.W.\} and Jenney, \{Francis E.\} and Wolfgang Sturhahn and Alp, \{Ercan E.\} and Jiyong Zhao and Yoshitaka Yoda and Cramer, \{Stephen P.\}",

year = "2013",

month = dec,

doi = "10.1007/s10751-012-0643-2",

language = "English",

volume = "222",

pages = "77--90",

journal = "Hyperfine Interactions",

issn = "0304-3843",

publisher = "Springer",

number = "2",

}

Guo, Y, Brecht, E, Aznavour, K, Nix, JC, Xiao, Y, Wang, H, George, SJ, Bau, R, Keable, S, Peters, JW, Adams, MWW, Jenney, FE, Sturhahn, W, Alp, EE, Zhao, J, Yoda, Y & Cramer, SP 2013, 'Nuclear resonance vibrational spectroscopy (NRVS) of rubredoxin and MoFe protein crystals', Hyperfine Interactions, vol. 222, no. 2, pp. 77-90. https://doi.org/10.1007/s10751-012-0643-2

TY - JOUR

T1 - Nuclear resonance vibrational spectroscopy (NRVS) of rubredoxin and MoFe protein crystals

AU - Guo, Yisong

AU - Brecht, Eric

AU - Aznavour, Kristen

AU - Nix, Jay C.

AU - Xiao, Yuming

AU - Wang, Hongxin

AU - George, Simon J.

AU - Bau, Robert

AU - Keable, Stephen

AU - Peters, John W.

AU - Adams, Michael W.W.

AU - Jenney, Francis E.

AU - Sturhahn, Wolfgang

AU - Alp, Ercan E.

AU - Zhao, Jiyong

AU - Yoda, Yoshitaka

AU - Cramer, Stephen P.

PY - 2013/12

Y1 - 2013/12

N2 - 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.

AB - 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.

KW - EXAFS

KW - Mössbauer

KW - Nitrogenase

KW - Normal mode analysis

KW - NRVS

KW - Nuclear resonance vibrational spectroscopy

KW - Nuclear resonant scattering

KW - Rubredoxin

KW - Synchrotron radiation

UR - https://www.scopus.com/pages/publications/84887623372

U2 - 10.1007/s10751-012-0643-2

DO - 10.1007/s10751-012-0643-2

M3 - Article

AN - SCOPUS:84887623372

SN - 0304-3843

VL - 222

SP - 77

EP - 90

JO - Hyperfine Interactions

JF - Hyperfine Interactions

IS - 2

ER -

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

Abstract

Funding

Keywords

Access to Document

Other files and links

Fingerprint

Cite this