| References |
Gonser, U., Grant, R.W., Mössbauer effect in hemoglobin and some iron-containing biological compounds (1965) Biophys J, 5, pp. 823-844. , COI: 1:CAS:528:DyaF28XksFakug%3D%3D; Vertes, A., Korecz, L., Burger, K., (1979) Mössbauer spectroscopy, , Academia Kiada, Budapest; Spartalian, K., Lang, G., (1980) In: Cohen RL (ed) Applications of Mössbauer spectroscopy, vol 2, , Academic Press, New York; Dickson, D.P.E., Johnson, C.E., (1980) Applications of Mössbauer spectroscopy, , Cohen RL, (ed), 2, Academic Press, New York; Trautwein, A., Diemann, E., (1980) Bill E (1981) In, , Transition metal chemistry, Proceedings of the Workshop: Verlag Chimie, Weinheim; Huynh, B.H., Kent, T.A., Mössbauer studies of biomolecules (1983) Stud Phys Theoret Chem, 25, pp. 490-560. , COI: 1:CAS:528:DyaL3sXksV2ksLo%3D; Dickson, D.P.E., (1984) Mössbauer spectroscopy applied to inorganic chemistry, , Long GJ, (ed), 1, Plenum, New York; Oshtrakh, M.I., Biomedical applications of Mössbauer effect (1991) Hyperfine Interact, 66, pp. 127-139. , COI: 1:CAS:528:DyaK38XlsVOksQ%3D%3D; Trautwein, A.X., Bill, E., Bominaar, E.L., Winkler, H., (1991) Structure and bonding, , 78, Springer, Berlin; Oshtrakh, M.I., Mössbauer effect in biomedical research: variations of quadrupole splitting in relation to the qualitative changes of biomolecules (1996) Z Naturforsch, 51a, pp. 381-388; Oshtrakh, M.I., Mössbauer spectroscopy of iron containing biomolecules and model compounds in biomedical research (1999) J Mol Struct, 480-481, pp. 109-120; Oshtrakh, M.I., Study of the relationship of small variations of the molecular structure and the iron state in iron containing proteins by Mössbauer spectroscopy: biomedical approach (2004) Spectrochim Acta, Part A: Molec and Biomolec Spectroscopy, 60, pp. 217-234. , COI: 1:STN:280:DC%2BD3srovF2rug%3D%3D; Oshtrakh, M.I., The relationship of Mössbauer hyperfine parameters and structural variations of iron containing proteins and model compounds in biomedical research (2004) Hyperfine Interact, 159, pp. 337-343. , COI: 1:CAS:528:DC%2BD28Xis1alsLY%3D; Oshtrakh, M.I., Mössbauer spectroscopy: application in biomedical research (2005) Hyperfine Interact, 165, pp. 313-320; Oshtrakh, M.I., Biomedical applications of Mössbauer spectroscopy (2006) J Radioanal Nucl Chem, 269, pp. 407-415. , COI: 1:CAS:528:DC%2BD28Xpt1Crtb8%3D; Papaefthymiou, G.C., The Mössbauer and magnetic properties of ferritin cores (2010) Biochim Biophys Acta, 1800, pp. 886-897. , COI: 1:CAS:528:DC%2BC3cXnvVyhurs%3D; Kamnev, A.A., Kovács, K., Alenkina, I.V., Oshtrakh, M.I., (2013) Mössbauer spectroscopy: applications in chemistry, biology, and nanotechnology, , Sharma VK, Klingelhofer G, Nishida T, (eds), Wiley, Hoboken; Oshtrakh, M.I., Semionkin, V.A., Milder, O.B., Novikov, E.G., Biomedical application of Mössbauer spectroscopy with high velocity resolution: preliminary results (2008) Proceedings of the international conference “Mössbauer spectroscopy in materials science 2008”, AIP conference proceedings, , Mashlan M, Zboril R, (eds), 1070, American Institute of Physics, Melville; Oshtrakh, M.I., Semionkin, V.A., Grokhovsky, V.I., Milder, O.B., Novikov, E.G., Mössbauer spectroscopy with high velocity resolution: new possibilities of chemical analysis in material science and biomedical research (2009) J Radioanal Nucl Chem, 279, pp. 833-846. , COI: 1:CAS:528:DC%2BD1MXislOiur8%3D; Oshtrakh, M.I., Semionkin, V.A., Milder, O.B., Novikov, E.G., Mössbauer spectroscopy with high velocity resolution: new possibilities in biomedical research (2009) J Mol Struct, 924-926, pp. 20-26; Oshtrakh, M.I., Semionkin, V.A., Milder, O.B., Novikov, E.G., Possibilities of Mössbauer spectroscopy with a high velocity resolution in studying small variations in 57Fe hyperfine parameters of iron-containing proteins (2010) Bull Rus Acad Sci: Phys, 74, pp. 407-411; Oshtrakh, M.I., Semionkin, V.A., Milder, O.B., Alenkina, I.V., Novikov, E.G., Biomedical application of Mössbauer spectroscopy with a high velocity resolution: revealing of small variations (2010) Spectroscopy, 24, pp. 593-599. , COI: 1:CAS:528:DC%2BC3cXhsVejs73F; Oshtrakh, M.I., Alenkina, I.V., Milder, O.B., Semionkin, V.A., Mössbauer spectroscopy with a high velocity resolution in the study of iron-containing proteins and model compounds (2011) Spectrochim Acta, Part A: Molec and Biomolec Spectroscopy, 79, pp. 777-783. , COI: 1:CAS:528:DC%2BC3MXnt12rsL4%3D; Frauenfelder, H., (1963) The Mössbauer effect, , Benjamin, New York; Goldanskii, V.I., Herber, R.H., (1968) Chemical applications of Mössbauer spectroscopy, , Academic Press, New York; Greenwood, N.N., Gibb, T.C., (1971) Mössbauer spectroscopy, , Chapman and Hall, London; Gutlich, P., Link, R., Trautwein, A., (1978) Mössbauer spectroscopy and transition metal chemistry, , Springer, Berlin; Gutlich, P., Bill, E., Trautwein, A., (2011) Mössbauer spectroscopy and transition metal chemistry. Fundamentals and applications, , Springer, Heidelberg; Oshtrakh, M.I., Semionkin, V.A., Milder, O.B., Novikov, E.G., Mössbauer spectroscopy with high velocity resolution: an increase of analytical possibilities in biomedical research (2009) J Radioanal Nucl Chem, 281, pp. 63-67. , COI: 1:CAS:528:DC%2BD1MXptFCmu7w%3D; Semionkin, V.A., Oshtrakh, M.I., Milder, O.B., Novikov, E.G., A high velocity resolution Mössbauer spectrometric system for biomedical research (2010) Bull Russ Acad Sci: Phys, 74, pp. 416-420; Oshtrakh, M.I., Semionkin, V.A., Mössbauer spectroscopy with a high velocity resolution: advances in biomedical, pharmaceutical, cosmochemical and nanotechnological research (2013) Spectrochim Acta, Part A: Molec and Biomolec Spectroscopy, 100, pp. 78-87. , COI: 1:CAS:528:DC%2BC38Xhs12hs7vN; Antonini, E., Brunori, M., (1971) Hemoglobin and myoglobin in their reactions with ligands, , North-Holland, Amsterdam; Wittenberg, J.B., Bergersen, F.J., Appleby, C.A., Turner, G.L., Wittenberg, J.B., Bergersen, F.J., Appleby, C.A., Turner, G.L., Facilitated oxygen diffusion. The role of leghemoglobin in nitrogen fixation by bacteroids isolated from soybean root nodules (1974) J Biol Chem, 249, pp. 4057-4066. , COI: 1:STN:280:DyaE2czgtFKlsA%3D%3D; Weissbluth, M., (1974) Hemoglobin. Cooperativity and electronic properties, , Springer, Berlin; Banerjee, R., Haemoglobin: function in relation to structure (1983) Life Chem Rep, 1, pp. 209-278. , COI: 1:CAS:528:DyaL3sXksV2js70%3D; Rifkind, J.M., (1987) Advances in inorganic biochemistry, , Eichhorn GL, Marzilli LG, (eds), 7, Elsevier, New York; Perutz, M.F., Wilkinson, A.J., Paoli, M., Dodson, G.G., The stereochemical mechanism of the cooperative effects in hemoglobin revisited (1998) Annu Rev Biophys Biomol Struct, 27, pp. 1-34. , COI: 1:CAS:528:DyaK1cXktVSlt7s%3D; Oshtrakh, M.I., Kumar, A., Kundu, S., Berkovsky, A.L., Semionkin, V.A., Study of human, rabbit and pig oxyhemoglobins using high velocity resolution Mössbauer spectroscopy in relation to their structural and functional variations (2011) J Mol Struct, 993, pp. 292-296. , COI: 1:CAS:528:DC%2BC3MXlt1Sntrs%3D; Oshtrakh, M.I., Berkovsky, A.L., Kumar, A., Kundu, S., Vinogradov, A.V., Konstantinova, T.S., Semionkin, V.A., Heme iron state in various oxyhemoglobins probed using Mössbauer spectroscopy with a high velocity resolution (2011) Biometals, 24, pp. 501-512. , COI: 1:CAS:528:DC%2BC3MXlvVWjurs%3D; Oshtrakh, M.I., Kumar, A., Alenkina, I.V., Zakharova, A.P., Semionkin, V.A., Kundu, S., Characterization of monomeric soybean leghemoglobin using Mössbauer spectroscopy with a high velocity resolution (2014) Hyperfine Interact, 226, pp. 431-438. , COI: 1:CAS:528:DC%2BC2cXnt12itg%3D%3D; Kumar, A., Alenkina, I.V., Zakharova, A.P., Oshtrakh, M.I., Semionkin, V.A., Hyperfine interactions in soybean and lupin oxy-leghemoglobins studied using Mössbauer spectroscopy with a high velocity resolution (2015) Hyperfine Interact, 230, pp. 131-139. , COI: 1:CAS:528:DC%2BC2MXis1ehsrw%3D; Kumar, A., Zakharova, A.P., Alenkina, I.V., Oshtrakh, M.I., Semionkin, V.A., An analysis of the features of the Mössbauer spectra of soybean leghemoglobin a in oxy- and deoxy-forms in relation to protein structure (2015) Bull Russ Acad Sci: Phys, 79, pp. 1041-1045. , COI: 1:CAS:528:DC%2BC2MXhsVGjurfO; Shaanan, B., Structure of human oxyhaemoglobin at 2.1 Å resolution (1983) J Mol Biol, 171, pp. 31-59. , COI: 1:CAS:528:DyaL2cXkslegsA%3D%3D; Marti, M.A., Capece, L., Bikiel, D.E., Falcone, B., Estrin, D.A., Oxygen affinity controlled by dynamical distal conformations: the soybean leghemoglobin and the Paramecium caudatum hemoglobin cases (2007) Proteins, 68, pp. 480-487. , COI: 1:CAS:528:DC%2BD2sXmvVaks70%3D; Oshtrakh, M.I., Alenkina, I.V., Vinogradov, A.V., Konstantinova, T.S., Semionkin, V.A., Differences of the 57Fe hyperfine parameters in both oxyhemoglobin and spleen from normal human and patient with primary myelofibrosis (2013) Hyperfine Interact, 222, pp. 55-60. , COI: 1:CAS:528:DC%2BC3sXmvVylsL8%3D; Festa, R.S., Asakura, T., Oxygen dissociation curves in children with anemia and malignant disease (1979) Am J Hematol, 7, pp. 233-244. , COI: 1:STN:280:DyaL3c3hslCmuw%3D%3D; Oshtrakh, M.I., Semionkin, V.A., Mössbauer spectroscopy of haemoglobins: study of the relationship of Fe2+ electronic and molecular structure of the active site (1986) FEBS Lett, 208, pp. 331-336. , COI: 1:CAS:528:DyaL2sXhslWgsLw%3D; Oshtrakh, M.I., Semionkin, V.A., Variation of Mössbauer spectra hyperfine parameters of oxyhemoglobin during leukaemia (1987) Biophysica (Moscow), 32, pp. 197-202. , COI: 1:STN:280:DyaL2s3hsVansQ%3D%3D; Oshtrakh, M.I., Semionkin, V.A., Mössbauer study of red blood cells from patients with erythremia (1989) FEBS Lett, 257, pp. 41-44. , COI: 1:CAS:528:DyaK3cXlsFOq; Theil, E.C., Ferritin: structure, gene regulation, and cellular function in animals, plants, and microorganisms (1987) Annu Rev Biochem, 56, pp. 289-315. , COI: 1:CAS:528:DyaL2sXltFWiu7g%3D; Harrison, P.M., Arosio, P., The ferritins: molecular properties, iron storage function and cellular regulation (1996) Biochim Biophys Acta, 1275, pp. 161-203; Andrews, S.C., Iron storage in bacteria (1998) Adv Microb Physiol, 40, pp. 281-351. , COI: 1:CAS:528:DyaK1MXmsVei; Oshtrakh, M.I., Alenkina, I.V., Dubiel, S.M., Semionkin, V.A., Structural variations of the iron cores in human liver ferritin and its pharmaceutically important models: a comparative study using Mössbauer spectroscopy with a high velocity resolution (2011) J Mol Struct, 993, pp. 287-291. , COI: 1:CAS:528:DC%2BC3MXlt1Sntro%3D; Alenkina, I.V., Oshtrakh, M.I., Klepova, Y.V., Dubiel, S.M., Sadovnikov, N.V., Semionkin, V.A., Comparative study of the iron cores in human liver ferritin, its pharmaceutical models and ferritin in chicken liver and spleen tissues using Mössbauer spectroscopy with a high velocity resolution (2013) Spectrochim Acta, Part A: Molec and Biomolec Spectroscopy, 100, pp. 88-93. , COI: 1:CAS:528:DC%2BC38Xhs12iur7K; Alenkina, I.V., Oshtrakh, M.I., Semionkin, V.A., Kuzmann, E., Comparative study of nanosized iron cores in human liver ferritin and its pharmaceutically important models Maltofer® and Ferrum Lek using Mössbauer spectroscopy (2013) Bull Russ Acad Sci: Phys, 77, pp. 739-744. , COI: 1:CAS:528:DC%2BC3sXhtVGrtLbM; Alenkina, I.V., Oshtrakh, M.I., Klencsár, Z., Kuzmann, E., Chukin, A.V., Semionkin, V.A., 57Fe Mössbauer spectroscopy and electron paramagnetic resonance studies of human liver ferritin, Ferrum Lek and Maltofer® (2014) Spectrochim Acta, Part A: Molec and Biomolec Spectroscopy, 130, pp. 24-36. , COI: 1:CAS:528:DC%2BC2cXptVCksL0%3D; Alenkina, I.V., Oshtrakh, M.I., Tugarova, A.V., Biró, B., Semionkin, V.A., Kamnev, A.A., Study of the Rhizobacterium Azospirillum brasilense Sp245 using Mössbauer spectroscopy with a high velocity resolution: implication for the analysis of ferritin-like iron cores (2014) J Mol Struct, 1073, pp. 181-186. , COI: 1:CAS:528:DC%2BC2cXovVagsL4%3D; Oshtrakh, M.I., Alenkina, I.V., Vinogradov, A.V., Konstantinova, T.S., Kuzmann, E., Semionkin, V.A., Mössbauer spectroscopy of the iron cores in human liver ferritin, ferritin in normal human spleen and ferritin in spleen from patient with primary myelofibrosis: preliminary results of comparative analysis (2013) Biometals, 26, pp. 229-239. , COI: 1:CAS:528:DC%2BC3sXlsF2it78%3D; Oshtrakh, M.I., Alenkina, I.V., Vinogradov, A.V., Konstantinova, T.S., Semionkin, V.A., The 57Fe hyperfine interactions in iron storage proteins in liver and spleen tissues from normal human and two patients with mantle cell lymphoma and acute myeloid leukemia: a Mössbauer effect study (2015) Hyperfine Interact, 230, pp. 123-130. , COI: 1:CAS:528:DC%2BC2MXls1WmtA%3D%3D; Oshtrakh, M.I., Semionkin, V.A., Milder, O.B., Novikov, E.G., Iron containing vitamins and dietary supplements: control of the iron state using Mössbauer spectroscopy with high velocity resolution (2009) Hyperfine Interact, 190, pp. 67-74. , COI: 1:CAS:528:DC%2BD1MXls1yqs70%3D; Oshtrakh, M.I., Novikov, E.G., Dubiel, S.M., Semionkin, V.A., Study of vitamins and dietary supplements containing ferrous fumarate and ferrous sulfate using Mössbauer spectroscopy (2010) Proceedings of the international conference “Mössbauer spectroscopy in materials science 2010”, AIP conference proceedings, pp. 75-81. , Tuček J, Miglierini M, (eds), American Institute of Physics, 1258, Melville, New York; Oshtrakh, M.I., Novikov, E.G., Dubiel, S.M., Semionkin, V.A., Variations of 57Fe hyperfine parameters in medicaments containing ferrous fumarate and ferrous sulfate (2010) Hyperfine Interact, 197, pp. 287-294. , COI: 1:CAS:528:DC%2BC3MXhvVCjtLg%3D; Oshtrakh, M.I., Novikov, E.G., Dubiel, S.M., Semionkin, V.A., Comparative study of Ascofer® and ferrous gluconate using Mössbauer spectroscopy with a high velocity resolution (2014) Hyperfine Interact, 226, pp. 451-457. , COI: 1:CAS:528:DC%2BC3sXhsleksrzM; Dubiel, S.M., Cieslak, J., Gozdyra, R., Effect of time and storing conditions on iron forms in ferrous gluconate and Ascofer® (2011) J Mol Struct, 991, pp. 171-177. , COI: 1:CAS:528:DC%2BC3MXjtFOhur8%3D |