Chapter 5: Mössbauer Spectroscopy
Published:03 Jun 2010
Y. Qiu and C. Chen, in Nuclear Analytical Techniques for Metallomics and Metalloproteomics, ed. C. Chen, Z. Chai, and Y. Gao, The Royal Society of Chemistry, 2010, ch. 5, pp. 128-162.
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This chapter aims to introduce the Mössbauer effect and hyperfine structure of Mössbauer spectroscopy. Owing to its excellent energy resolution, it can provide detailed structural data of metal sites when applying to metalloproteomics studies. The main applications in the metalloprotein studies are the structural characterization of iron-containing proteins, including the iron electronic structure, coordination environment; the qualitative and quantitative changes of iron containing proteins during pathological processes or the effect of environmental factors; as well as their conformational changes and reaction dynamics. The first two sections provide an overall review of Mössbauer spectroscopy in its physical principles, facilities, Equipments, performance, data processing and application. The followed section introduces the application for elemental speciation in environmental and biological samples using Mössbauer spectroscopy. Some other nuclear related techniques for ultrafine interaction study like nuclear magnetic resonance (NMR) spectroscopy, electron paramagnetic resonance (EPR), and resonance Raman spectroscopy are also outlined for study the structure of metalloproteins. Finally, the advantages and limitations are discussed.