Biomedical Research and Analysis with Mössbauer Spectroscopy
An effective technique used in the examination of iron atom electronic environments in both biomolecular molecules and whole animal studies, Mössbauer spectroscopy, because of its sensitivity to nuclear hyperfine interactions, yields incredibly accurate data regarding the electronic and magnetic states of nuclei, chemical bonds, and the local electronic environment structure around iron atoms.
A recent article in Chimia (1) examines the contribution of Mössbauer spectroscopy to biomedical sciences in general, and specifically in studies involving bacterial analysis, as well as protein and pharmaceutical studies. The main aim of the authors’ work is to provide an overview of how this technique can be used in the field of biomedicine to allow users to acquire a deeper understanding of the characteristics, roles, and activity of iron-containing proteins and compounds within biological systems.
Discovered by German physicist Rudolph Mössbauer in 1958, the Mössbauer effect is a physical phenomenon involving the resonant and recoil-free emission and absorption of gamma radiation by atomic nuclei bound in a solid (2,3). When these occur, there is no loss of gamma energy to the kinetic energy resulting from the recoiling of nuclei at either the emitting or absorbing end of a gamma transition; these actions occur at the same energy, and result in strong, resonant absorption. This discovery earned the 1961 Nobel Prize in Physics (3).
While not considered as common technique in the fields of biology and medicine, Mössbauer spectroscopy is sensitive enough to detect species at concentrations between 10 and 20 μM for iron containing species (4). Although admittedly not practicable for transition metals such as copper, manganese, or zinc, because of a lack of suitable isotopes and low recoil-free fractions (4,5), the authors of the review believe that the importance of coordination compounds with an iron metal center in inorganic and bioinorganic chemistry as models for biologically important proteins cannot be overstated, as iron has a biological role that no other metal can match. Nearly every lineage of life contains enzymes that have heme units as their active centers, especially hydrogenase enzymes, which show promise as materials for hydrogen storage (6).
The authors of the paper reported Mössbauer spectroscopy’s effectiveness in the investigation of proteins and enzymes that have iron active sites, as well as Fe/S clusters, and its ability for use in the obtaining of kinetic and mechanistic information about processes involving Fe-containing proteins (7,8). In addition, the technique has proved to be useful in the study of a variety of iron-containing medicaments, vitamins, and dietary supplements which have been created and used for the treatment and prevention of iron deficiency anemia, an extremely dangerous condition which can lead to a variety of illnesses (9,10).
Detailed crosssection of an iron atom highlighting its protons neutrons and electrons. © Abdul - stock.adobe.com
References
1. Hassen, J.; Silver, J. Mössbauer Spectroscopy as a Valuable Analysis Technique in Biomedical Research. Chimia (Aarau) 2025, 79 (1-2), 84–92. DOI: 10.2533/chimia.2025.84
2. Rudolf Mössbauer. Wikipedia.https://en.wikipedia.org/wiki/Rudolf_M%C3%B6ssbauer (accessed 2025-03-03)
3. Mössbauer effect. Wikipedia. https://en.wikipedia.org/wiki/M%C3%B6ssbauer_effect (accessed 2025-03-03)
4. Lindahl, P.A.; Holmes-Hampton, G.P. Biophysical Probes of Iron Metabolism in Cells and Organelles. Curr. Opin. Chem. Biol. 2011, 15 (2), 342––346. DOI: 10.1016/j.cbpa.2011.01.007
5. Bandyopadhyay. D. Study of Materials Using Mössbauer Spectroscopy. Int. Mater. Rev. 2006, 51 (3), 171–208. DOI:10.1179/174328006X79490
6. Lubitz, W.; Reijerse, E.; van Gastel, M. [NiFe] and [FeFe] Hydrogenases Studied by Advanced Magnetic Resonance Techniques. Chem. Rev. 2007, 107 (10), 4331–4365. DOI: 10.1021/cr050186q
7. Bill, E. Iron-Sulfur clusters—New Features in Enzymes and Synthetic Models. Hyperfine Interact. 2012, 205, 139–147. DOI: 10.1007/s10751-011-0411-8
8. Pandelia, M. E.; Lanz, N. D.; Booker, S. J.; Krebs C. Mössbauer Spectroscopy of Fe/S Proteins. Biochim. Biophys. Acta 2015, 1853 (6), 1395–1405. DOI: 10.1016/j.bbamcr.2014.12.005
9. Alenkina, I. V.; Oshtrakh, M. I. Control of the Iron State in Pharmaceuticals Used for Treatment and Prevention of Iron Deficiency Using Mössbauer Spectroscopy. J. Pharm. Sci. 2024, 113 (6), 1426–1454. DOI: 10.1016/j.xphs.2024.02.023
10. Ahmet, M. T.; Frampton, C. S.; Silver, J. A Potential Iron Pharmaceutical Composition for the Treatment of Iron-Deficiency Anaemia. The Crystal and Molecular Structure of mer-tris-(3-hydroxy-2-methyl-4H-pyran-4-onato)iron(III). J. Chem. Soc., Dalton Trans. 1988, 1159–1163. DOI: 10.1039/DT9880001159
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