| Literature DB >> 26052177 |
Yisong Guo1, Eric Brecht2, Kristen Aznavour3, Jay C Nix4, Yuming Xiao1, Hongxin Wang5, Simon J George4, Robert Bau3, Stephen Keable2, John W Peters2, Michael W W Adams6, Francis Jenney7, Wolfgang Sturhahn8, Ercan E Alp8, Jiyong Zhao8, Yoshitaka Yoda9, Stephen P Cramer10.
Abstract
We have applied 57Fe nuclear resonance vibrational spectroscopy (NRVS) for the first time to study the dynamics of Fe centers in Fe-S 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 X-ray crystal structure.Entities:
Keywords: 57Fe; EXAFS; Mössbauer; NRVS; nitrogenase; normal mode analysis; nuclear resonant scattering; nuclear resonant vibrational spectroscopy; rubredoxin; synchrotron radiation
Year: 2013 PMID: 26052177 PMCID: PMC4453832 DOI: 10.1007/s10751-012-0643-2
Source DB: PubMed Journal: Hyperfine Interact ISSN: 0304-3843