Popescu Research Group

Chemical and Biochemical Applications of Mössbauer Spectroscopy

Hello, everyone and welcome!  You have arrived at the scientific webpage created by Dr. Popescu (Ewbank-Popescu) in an effort to showcase the beauty of Mossbauer (and Electron Paramagnetic Resonance – EPR) spectroscopy, molecular electronic structure and puzzle solving.

In our research, we seek to solve problems pertaining to the chemistry of some life processes involving iron, such as hydrogen generation, biological oxidation, nitrogen binding and fixation. We study aspects of the mechanism, structures of the intermediates and model complexes. The bulk of our experimental work involves Mössbauer and EPR spectroscopy. Our Mössbauer spectroscopy laboratory was established in 2004 at Ursinus College with funds from an NSF-MRI grant (Popescu, 2004-07).  

Some of our current interdisciplinary projects are listed below.  Funding from NSF (NSF-RUI 2010-13, and 2013-2017). All our projects are pursued solely with undergraduate students from primarily undergraduate institutions (Ursinus College, Colgate and University and University of St. Thomas).  Other exciting projects are in various degrees of planning or accomplishment. For the latter, see our publications.

  • The study of novel complexes that aim to model the active site of hydrogenase enzymes.
  • Characterization of novel Fe(I) and other unusual bio-inspired complexes.
  • Studies of iron complexes exhibiting spin transitions.
  • Studies of the dual-function enzyme dehaloperoxidase (DHP) from Amphitrite ornata.
  • Studies of model complexes of Fe(III)-radical model complexes for aminophenol oxidases.

These projects combine spectroscopic characterization of iron bio-inspired complexes with the analysis of enzyme active sites, calculations and biochemical characterization of enzymes, such as DHP. These collaborative projects involve world-class scientists, both synthetic chemists and biochemists, from Texas A&M, Marquette University, University of Delaware, North Carolina State University (Raleigh) and the Pacific Northwest National Laboratory. For details, please follow the links on the right.

In addition, we continue to add exciting projects with new collaborators.  Recently we looked into some interesting iron complexes which exhibit spin crossover.  These complexes are synthesized in the lab of Dr. David Shultz from North Carolina State University, in Raleigh, NC, by Dave's doctoral student, Chris Tichnell. 

For extended studies of paramagnetic complexes, we have done high-field Mössbauer spectroscopy and EPR spectroscopy  by visiting Professors Eckard Münck, Alex Guo and Michael Hendrich at Carnegie Mellon University.  We also use Spin Count, a dedicated program for EPR and Mössbauer spectral analysis, designed by Dr. Mike Hendrich.  We thank them for always being helpful and welcoming.  In-depth studies would not be possible without the use of variable field Mössbauer and EPR, and thus their resources.  Thank you!


About MB Spectroscopy

57Fe-Mössbauer spectroscopy is a specialized spectroscopic technique for the 57Fe isotope. To study one isotope may appear restrictive. Fortunately, iron is the most abundant transition metal in biology and it is present in most important biological processes. Therefore biological 57Fe-Mössbauer spectroscopy (MB) has never been in danger of running out of systems to study. Not only that we are not close to finishing the Fe-proteins in even one bacterium (take P. aeruginosa or E. coli for ex.), but we have not yet understood the structures of some proteins whose study began many years ago (e.g. hydrogenase, nitrogenase etc).

Apart from directly studying protein samples, it is immensely instructive to study model compounds. Model complexes are molecular compounds synthesized by chemists in an attempt to match structural features or functions of enzymatic sites. Typically spectroscopists studying a protein would find a spectroscopic parameter or feature that they cannot explain with any theory that they cook up from books and their experience. That is generally considered a "strange" thing (label applied not before thorough checks). When a synthetic compound is found to match some strange spectroscopic signature of a protein, it is considered a good model. The advantage of studying the model is that often it can be structurally and spectroscopically characterized (X-ray, FTIR, EXAFS, ESR etc). The idea seems to be that even if you found a good model serendipitously, if you understand the model compound conceptually, i.e. you find a theory that explains the spectra, then maybe you can do what Nature does with it (say, produce hydrogen from protons). Moreover, very often, the feature of interest in a protein, may be buried in complex spectra resulting from multiple iron sites, so it is not well resolved. Having a compound exhibiting a well resolved spectrum, can sometimes can enable one to probe the strange feature from many points of view until it is understood. Currently, the people who have seen and often explained the strangest things in bio-inorganic Mössbauer spectroscopy reside in Pittsburgh (Dr. Münck's lab, at Carnegie Mellon University).

MB spectroscopy has many useful features, but two are distinctive: (1) a MB spectrum is observed regardless of oxidation or spin state of the iron atoms (unlike EPR, where you don't see diamagnetic compounds); and (2) the spectral patterns of paramagnetic and diamagnetic compounds are easily distinguishable. (Münck, E., Methods in Enzymology, Vol. LIV, pages 346-379) Thus, one analyzes spectra to determine the number of distinct Fe sites in the sample, their oxidation and spin state, and magnetic behavior. These parameters are interpreted in terms of electronic models, allowing predictions of molecular structure and function. Usually it is necessary to record the spectra at cryogenic temperatures (using liquid helium, with a boiling point of 4.2 K, approx. -269 C) in order to resolve paramagnetic spectra.

What can Mössbauer spectroscopy do for me?

Introduction to the technique

Mössbauer spectroscopy is a technique based on the nuclear recoilless γ-ray fluorescence effect, discovered by Rudolf Mössbauer (1929-2011) in 1957. Mössbauer proved experimentally that it is possible to detect recoilless γ-ray absorption by nuclei in certain conditions. Iron Mössbauer spectroscopy is widely used as an analytical tool, in geology, including astro-geology, for identifying the composition of iron-containing samples. In Chemistry, it has known a blossoming development because iron is central in many important catalysts (e.g. Haber-Bosch, Fisher-Tropsch processes), as well as the most abundant transition metal in living systems, found in the active site of many enzymes, such as hydrogenase, methane monooxygenase, ribonucleotide reductase, nitrogenase, to name only a few. Also, iron is absolutely necessary for respiration and metabolism in humans and other mammals, which is why people are rather intent about studying it. The application of Mössbauer spectroscopy to understand the mechanism and structure of novel chemical and biological systems is naturally interdisciplinary. There are other places on the WWW where the reader may find the physics side of the Mössbauer effect. Here we focus more on the chemical applications.

As in most spectroscopic techniques (e.g. electronic absorption), in Mössbauer, we have a source of radiation, a sample and a detector. The source contains the isotope 57Co, which decays radioactively to 57Fe, emitting the 14.4 KeV γ-ray, which can be absorbed by an Fe nucleus in the sample, if the resonance condition is obeyed.



The basic parameters of a simple Mössbauer spectrum (called a quadrupole doublet, shown below on the right) are the isomer shift (δ) and the quadrupole splitting (ΔEQ), both in mm/s. These parameters can reveal information about the oxidation and spin state of the various species of iron in the sample.


1)    Wang, P.; Killian, M.; Saber, M.; Qiu, T.; Yap, G.; Popescu, C. V.; Rosenthal, J.; Dunbar, K. R.; Brunold, T.; Riordan, C.G. “Electronic, Magnetic, Redox Properties and O2 Reactivity of Fe(II) and Ni(II)-o-Semiquinonate Complexes of a Tris(thioether) Ligand: Uncovering the Intradiol Cleaving Reactivity of an Fe(II)-o-semiquinonate Complex” Inorg. Chem. (2017) 56 (17), 10481–10495; DOI: 10.1021/acs.inorgchem.7b01491.

2)    Prokopchuk, D.E., Wiedner, E.S, Walter, E.D., Popescu, C.V., Piro, N.A., Kassel, W.S.A., Bullock, M, Mock, M. T. “Structure and reactivity of Iron Coordination Complexes toward Dinitrogen Catalytic N2 Reduction into Silylamines and Thermodynamics of N2 Binding at Square Planar Fe” J. Am. Chem. Soc. (2017),139, 9291–9301;  DOI: 10.1021/jacs.7b04552.

3)    Tichnell, C. R., Shultz, D. A. Popescu, C.V., *Sokirnyi, I, Boyle, P.D. “Synthesis, Characterization and Photophysical Studies of an Iron(III) Catecholate-Nitronylnitroxide Spin-Crossover Complex” Inorg. Chem. (2015) 54 (9), 4466–4474.

4)    Bittner, M.M., Lindeman, S.V., Popescu, C.V., Fiedler, A.T “Dioxygen Reactivity of Biomimetic Fe(II) Complexes with Noninnocent Catecholate, o-Aminophenolate, and o-Phenylenediamine Ligands” Inorg. Chem. (2014), 53 , 4047-4061.

5)    Hsieh, C.H.; Erdem, O.; Ding, S.; Crouthers, D.; Lubitz, W.; Popescu, C.V.; Reibenspies, J.; Hall, M. B. Darensbourg, M. Y. “Redox active iron nitrosyl units in proton reduction electrocatalysis” Nature Communications (2014) 5, 3684.

6)    Stoian, S., Hsieh, C.-H.;* Casuras, A.; Singleton, M.L., Darensbourg, M.Y., *McNeely, K.M., *Sweely, K., Popescu, C.V. “Hyperfine Interactions and Electron Distribution in FeIIFeI and FeIFeI Models for the Active Site of the [FeFe]-Hydrogenases”, J. Biol. Inorg. Chem., (2013) 18: 609-622 http://link.springer.com/article/10.1007/s00775-013-1005-5#page-1}

7)    Hsieh, C.-H.; Brothers, S.M.; Hall, M.B.; Popescu, C.V.; Darensbourg, M.Y., “The Ambidentate Thiocyanate Ligand in Dinitrosyl Iron Complexes”, Inorg. Chem.(2013), 52(4): 2119-2124.

8)    Bittner, M.M.,  *Kraus, D., Lindeman, S.V., Popescu, C.V., Fiedler, A.T “Synthetic, Spectroscopic, and DFT Studies of Iron Complexes with Iminobenzo(semi)quinone Ligands: Implications for o-Aminophenol Dioxygenases” Chem. Eur. J. (2013), 19(29): 9686-98

9)    Hsieh, C.-H., Harman, S. D., Singleton, M.L., Reijersee, E.; Lubitz, W.; Popescu, C.V., Brothers, S.M., Reibenspies, J.H., Hall, M.B., Darensbourg, M.Y. "Structural and Spectroscopic Features of Mixed Valent FeIIFeI Complexes and Factors Related to the Rotated Configuration of Diiron Hydrogenase” J. Am. Chem. Soc. (2012), 134, 13089-13102.

10) Liu, T., Li, B., Popescu, C.V., *Bilko, A., Perez, L., Hall, M. B., Darensbourg, M, Y. “Analysis of an Iron Dicarbonyl as Synthetic Analogue of the Hmd or [Fe]-Hydrogenase Active Site” Chem. Eur. J. (2010), 16, 3083-3089.

11) Popescu, C.V., Mock, M.T., Stoian, S.A., Riordan, C.G. “A high-spin organometallic Fe-S compound: Structural and Mössbauer Spectroscopic Studies of [Phenyltris((tert-butylthio)methyl)borate]Fe(Me), Inorg. Chem. (2009) 48 (17), 8317-8324.

12) Li, B., Liu, T., Popescu, C.V., Bilko, A., Darensbourg, M, Y. “Synthesis and Mössbauer Characterization of Octahedral Iron(II) Carbonyl  Complexes FeI2(CO)3L and FeI2(CO)2L2: Developing Models of the [Fe]-H2ase  Active Site” Inorganic Chemistry (2009), 48 (23), 11283-11289.

13) Mock, M.T., Kieber-Emmons, M.T., Popescu, C.V., *Gasda, P., Yap, G.P.A., Riordan, C.G. “A Series of Cyanide-Bridged Binuclear Complexes”, Inorg. Chim. Acta (2009) 362, 4553-4562.

14) Mock, M.T., Popescu, C.V., Yap, G.P.A., Dougherty, W.G., Riordan, C.G. “Monovalent Iron In a Sulfur-rich Environment”, Inorg. Chem. (2008), 47 (6), 1889-1891.

15) Zhang, J., Wallar, B.J., Popescu, C.V., Renner, D.B, Thomas, D.D., Lipscomb, J.D. “Methane Monooxygenase Hydroxylase and B Component Interactions” Biochemistry2006 45, 2913-2926.

16) Wolfe, M. D., Altier, D. J., Stubna, A., Popescu, C. V., Münck, E., Lipscomb, J. D. “Benzoate 1,2-Dioxygenase from Pseudomonas putida: Single Turnover Kinetics and Regulation of a Two Component Rieske Dioxygenase”, Biochemistry 2002,  41(30),  9611-9626.

17) Popescu, C. V., Münck, E., Fox, B. G, Sanakis, Y., Cummings, J. G., Turner, I. M., Jr., Nelson M. J. “Mössbauer and EPR Studies of the Photoactivation of Nitrile Hydratase”, Biochemistry2001, 40, 7984-7991.

18) Münck, E., Popescu, C. V. “Mössbauer Studies of Exchange Coupled Cluster Assemblies in Biological Systems” Hyperfine Interactions 2000, 126, 59- 67.

19) Bates, D. M., Popescu, C. V., Koroshilova, N.; Vogt, K., Beinert, H. Münck, E., Kiley, P. J. “Substitution of Lucine 28 for Histidine in the E. coli Transcription Factor FNR Results in Increased Stability of the [4Fe-4S]2+ Cluster to Oxygen”, J. Biol. Chem. 2000, 275, 6234.

20) Popescu, C. V., Münck, E. “On the electronic structure of the H-cluster in [Fe]-Hydrogenases”, J. Am. Chem. Soc. 1999, 121, 7877.

21) Popescu, C. V., Bates, D. M., Beinert, H., Münck, E., Kiley, P. J. (1999) “Mössbauer studies of the FNR transcription factor in whole E. Coli cells”, in Iron Metabolism, Wiley-VCH

22) Kyritsis, P., Kümmerle, R., Huber, J. G., Gaillard, J., Guigliarelli, B., Popescu C. V., Münck, E., Moulis, J. -M.  “Unusual NMR, EPR, and Mössbauer Properties of Chromatium vinosum 2[4Fe-4S] Ferredoxin”, Biochemistry 1999, 38, 6335.

23) Popescu, C. V., Bates, D. M., Beinert, H., Münck, E., Kiley, P. J. (1999) “Mössbauer studies of the FNR transcription factor in whole E. Coli cells”, in Iron Metabolism, Wiley-VCH.

24) Popescu, C. V., Bates D. M., Münck E., Beinert, H., Kiley, P. J.  “Mössbauer Spectroscopy as a Tool for the Study of Activation/Inactivation of the Transcription regulator FNR in whole Cells of Escherichia coli”, Proc. Nat. Acad. Sci. USA 1998, 95, 13431.

25) Kauffmann, K., Popescu, C. V., Dong, Y., Lipscomb, J. D., Que, L. Jr, Münck, E. “Mössbauer Evidence for Antisymmetric Exchange in a Diferric Synthetic Complex and Diferric Methane Monooxygenase”, J. Am. Chem. Soc. 1998, 120, 8739.

26) Hsu, H., Koch, S. A., Popescu, C. V., Münck, E.  “Chemistry of Fe Thiolate Complexes with CN- and CO.  Models for the [Fe(CO)(CN)2] Structural Unit in Ni-Fe Hydrogenase Enzymes”,  J. Am. Chem. Soc. 1997, 119, 8371.

27) Khoroshilova, N., Popescu, C. V., Münck, E., Beinert, H., Kiley, P. J.  “Iron-sulfur cluster disassembly in the FNR protein of Escherichia coli by O2: [4Fe-4S] to [2Fe-2S] conversion with loss of biological activity”, Proc. Natl. Acad. Sci USA 1997, 94,6087.

28) Xia, J., Hu, Z., Popescu, C. V., Lindahl, P. A., Münck, E.  “Mössbauer and EPR Study of the Ni-Activated Metallosubunit of Carbon Monoxide Dehydrogenase from Clostridium thermoaceticum”, J. Am. Chem. Soc. 1997, 119, 8301.

2014-2017       National Science Foundation – RUI: Mössbauer Studies of Iron Containing Model complexes and enzymatic active sites ($ 189,000) – CHE-1445959; 
2013-2014       National Science Foundation – RUI: Mössbauer Studies of Iron Containing Model complexes and enzymatic active sites  - CHE-1307650
2012    Sabbatical semester (Fall): Spectroscopy of Iron Containing Model Complexes and Enzymatic Active Sites. (Ursinus College and Carnegie Mellon University)
2010-2014       National Science Foundation – RUI: Mössbauer Studies of Iron Containing Model complexes and enzymatic active sites ($ 165,000) – CHE-0956779

1)    The 253rd ACS National Meeting –August 2017,San Francisco; Mössbauer Spectroscopy of Iron- Selone and and Iron-Thione Complexes Capable of Preventing Oxidative DNA Damage.  Popescu, C. V.; *Morgan Cohara; Stadelman, B.; Brumaghim, J.

2)    EUROBIC 13, The European Biological Inorganic Chemistry Conference2016, Budapest, Hungary; Mössbauer and Theoretical Studies of Bimetalic Complexes containing Metal-Nitroxide units. Popescu, C. V.; Shengda Ding; Pokhraj Gosh; Marcetta Y. Darensbourg.

3)    Bucknell University, The Chemistry Seminar Series – March 29, 2016, Lewisburg, PA, Mössbauer Studies of Iron Complexes with Hydrogen-Evolving Activity. Popescu, C. V.

4)    Colgate University – The Natural Sciences Division Colloquium, Spring 2016  – Analyzing Molecules with Mössbauer Spectroscopy to reveal Iron’s Catalytic Power. Popescu, C.V.

5)    The 251st ACS National Meeting – San Diego, 2016; Mössbauer Spectroscopy and Electronic Structure of Iron-Nitrosyl Complexes. Popescu, C. V.; Pokhraj Gosh; *Morgan Cohara; Marcetta Y. Darensbourg.

6)    The 250th ACS National Meeting – Boston, August, 2015; Mössbauer Studies of multimetallic assemblies of complexes with different spin states. Popescu, C. V.; Pokhraj Gosh; *Kaye Kuphal; *Nicholas Baglieri; Marcetta Y. Darensbourg.

7)    The 248th ACS National Meeting – San Francisco, August, 2014; Mössbauer Studies of the ferryl, ferrous, and ferric states of the dehaloperoxidase from Amphitrite ornata. Popescu, C. V.; Barrios, David; *Miller, Danielle B.; Ghiladi, Reza A.

8)    The 248th ACS National Meeting – San Francisco, August, 2014; Mössbauer Studies of a low-spin monovalent iron complex; Popescu, C. V.; Wang, P.; *DeHont, Raymond; Mock, Michael T.; Riordan, Charles G.

9)    The 248th ACS National Meeting – San Francisco, August, 2014; Mössbauer and Magnetometry Studies of a ferric complex with spin transition. Popescu, C. V.; *Sokirnyi, Ivan; Tichnell, Christopher; Shultz, David.

10) The 247th ACS National Meeting – Dallas,  March, 2013; Mössbauer Studies of the dual-function protein Dehaloperoxidase. Popescu, C. V., *Danielle Miller, Reza Ghiladi

11) The International Conference on Biological Inorganic Chemistry – ICBIC 16 – Grenoble, France, July 21-26, 2013: Hyperfine Interactions in the 2Fe subcluster of the [Fe-Fe] hydrogenases. Popescu, C. V., S. Stoian, *A. Casuras, C.-H. Hsieh, M. Singleton, M. Y. Darensbourg.

12) The 244th ACS National Meeting – Philadelphia, PA August 19-23, 2012; Mössbauer Studies of mixed-valence FeIIFeI and FeIFeI model complexes illustrating states of the H-cluster in the [Fe-Fe]-hydrogenases. C. V. Popescu, S. Stoian, A. Casuras, C.-H. Hsieh, M. Singleton, M. Y. Darensbourg.(INOR-49)

13) The 244th ACS National Meeting – Philadelphia, PA August 19-23, 2012; Mössbauer Studies of model complexes for the [Fe-Fe]-hydrogenases: Electronic Structure of Mixed-Valent Complexes Containing Low-Spin FeI. C. V. Popescu, S. Stoian, A. Casuras, C.-H. Hsieh, M. Singleton, M. Y. Darensbourg. (INOR-699)

14) The 244th ACS National Meeting – Philadelphia, PA August 19-23, 2012; Mössbauer Studies of the enzyme dehaloperoxidase from A. ornata. D. Miller, C. V. Popescu, J. Birabaharan, R. Dumarieh, R. Ghiladi. (CHED-178)

15) Gordon Research Conference: Iron-Sulfur Enzymes, Mount Holyoke College, Massachusetts, June 10-14, 2012: Mössbauer Studies of Low-spin Monovalent Iron and the Mixed-Valence Fe(II)Fe(I) Oxidized state of the [Fe-Fe]-Hydrogenases, C. V. Popescu, S. Stoian, A. Casuras, C.-H. Hsieh, M. Singleton, M. Y. Darensbourg.

16) "The Villanova University Physics Colloquium", February 12, 2012 - "Mössbauer studies of monovalent iron in search for a good model for the hydrogenase" C. V. Popescu.

17) The International Conference on Biological Inorganic Chemistry – ICBIC 15 – Vancouver, Canada, August 6 – 13, 2011;  "Mössbauer studies of model complexes illustrating different states of the H-cluster in [Fe-Fe] hydrogenases" C. V. Popescu, S. Stoian, A. Casuras, M. Singleton, M. Y. Darensbourg.

18) The 239th ACS National Meeting – Boston, MA, August 16-20, 2010; "Advances in the characterization of discrete states of the hydrogenase active site" C. V. Popescu, A. Bilko, M. Singleton, M. Y. Darensbourg.

19) Gordon Research Conference: Iron-Sulfur Enzymes, Colby-Sawyer College, New Hampshire, June 6-11, 2010;  "Mössbauer studies of model complexes for the active site of the Fe-only hydrogenases" C. V. Popescu, Marcetta Darensbourg, Michael Singleton, Andrey Bilko.

20) The 238th ACS National Meeting – Washington, D.C., August 16-20, 2009;

“Mössbauer Studies of a high-spin ferrous organometallic complex”, C. V. Popescu,M. T. Mock,     S. A. Stoian, C. G. Riordan.

21) The International Conference on Biological Inorganic Chemistry – ICBIC 13 – Vienna, Austria, July 15 – 22, 2007.  “Synthetic, structural and Mössbauer studies of novel high-spin iron complexes supported by a tri-thioether ligand” - C. V. Popescu, M. Mock, S. A. Stoian and C. G. Riordan.

22) The National CUR Conference – De Pauw, Indiana, June 22-26, 2006; “Mössbauer spectroscopy: challenge and opportunity for undergraduate researchers” – C.V. Popescu, Michael Mock, Charles Riordan.

23) The Bryn Mawr - Haverford Chemistry Colloquium, October 28, 2005 - "Mössbauer studies of model compounds for the active sites of hydrogenases and Carbon Monoxide Dehydrogenase" Popescu, C. V.

24) International Conference on Biological Inorganic Chemistry – ICBIC 12 – Ann Arbor, Michigan, July 31-August 5, 2005; Poster: Mössbauer studies of the effects of ligand binding and redox changes in the active center of the [NiFe]-hydrogenase from Allochromatium vinosum - Popescu, C. V., Surerus, K. K., Ravi, N., Duin, E., Roseboom, W., Münck, E. and Albracht, S.P.J.

25) The 228th ACS National Meeting - Philadelphia, August 22-26, 2004; “57Fe - Mössbauer spectroscopic studies of model compounds for the Fe-only hydrogenases”, DeHont, R. F.; Chiarella, G.; Melgarejo, D.; Stoian, S.; Koch, S.; Münck, E.; Popescu, C. V.

26) The National CUR Conference – La Crosse, Wisconsin, June 16-22, 2004 – “Fluorescence and Mössbauer spectroscopic studies of biologically relevant systems” – C.V. Popescu, Raymond DeHont.

27) The 10th International Workshop in ESR Spectroscopy and Imaging – April 2003, Fukuoka, Japan – “Mutagenesis and ESR studies of the component interactions in the methane monooxygenase from M. trichosporium” Popescu, C.V., Cornea, R. L., Lipscomb, J. D., Thomas, D. D.

28) Biophysical Society National Meeting – 2003 “Fluorescence studies of the component interactions in Methane Monooxygenase from M. trichosporium OB3b” Popescu, C.V., Lipscomb, J.D., Thomas, D.D. Biophys. J. Abstracts.

29) International Conference for Bioinorganic Chemistry – ICBIC 11 - Florence, Italy, 2001 “Mössbauer and EPR Studies of the Photoactivation of Nitrile Hydratase” - Popescu, C.V., Münck, E., Fox, B. G, Sanakis, Y., Cummings, J. G., Turner, I. M., Jr., Nelson M. J.