Hostname: page-component-848d4c4894-ttngx Total loading time: 0 Render date: 2024-05-06T06:42:44.431Z Has data issue: false hasContentIssue false

Mössbauer spectroscopy of haem proteins

Published online by Cambridge University Press:  17 March 2009

G. Lang
Affiliation:
Nuclear Physics Division, United Kingdom Atomic Energy Research Establishment, Harwell, Didcot, Berks., England

Extract

A fair beginning has been made in understanding the Mössbauer spectra of many types of haem proteins. The diamagnetic compounds have all the usual difficulties associated with the calculation of any quadrupole spectra, with the added complication of larger molecules and much less crystallographic data. In the ferric paramagnets the large molecules are quite helpful in that they prevent interaction between neighbouring sites and make possible long electron spin-relaxation times. The resulting magnetic Mössbauer spectra contain a large amount of information and, by their complexity, tend to be a guard against ambiguity in interpretation. The theoretical problem of the magnetic hyperfine interaction appears more complex than the quadrupole interaction, but this apparent complexity is only superficial in the sense that it requires more complex mathematical manipulations. The underlying physical problem is much simpler in the magnetic case because it involves interactions only with the relatively few unpaired electrons, and is insensitive to all others and has no lattice contribution. Fortunately the unpaired electrons are those which lie high in energy, and are most likely to be involved in the chemical activity of the enzyme. Most of the results on ferric haems have been fairly satisfactory, and it seems likely that many of the uncertainties will be cleared up by further work. From the physicist's point of view it appears reasonable to expect that the search for better agreement between theory and paramagnetic spectra may be a route to a better understanding of the factors affecting the quadrupole interaction. The integral spin paramagnets are an intermediate case, usually requiring large applied field to reveal their magnetic properties. No high-spin ferrous haems have yet been subjected to detailed magnetic experimental or theoretical investigation, but this should be a fruitful field.

Type
Research Article
Copyright
Copyright © Cambridge University Press 1970

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

Bleaney, B. & O'Brien, M. C. M. (1956). Paramagnetic resonance in some complex cyanides of the iron group. II Theory. Proc. Phys. Soc. B.69, 12161230.Google Scholar
Blumberg, W. E. (1967). The EPR of high spin Fe3+ in rhombic fields. In Magnetic Resonance in Biological Systems, pp. 119133. Oxford and New York: Pergamon Press.CrossRefGoogle Scholar
Blumberg, W. E., Peisach, J., Wittenberg, B. A. & Wittenberg, J. B. (1968). The electronic structure of protoheme proteins. I. An electron paramagnetic resonance and optical study of horse radish peroxidase and its derivatives. J. biol. Chem. 243, 18541862.Google Scholar
Burns, G. (1961). Nuclear quadrupole moment of Fe57m. Phys. Rev. 124, 524526.CrossRefGoogle Scholar
Cooke, R. & Debrunner, P. (1968). Mössbauer studies of the iron atom in cytochrome c. J. chem. Phys. 48, 45324537.CrossRefGoogle ScholarPubMed
Debenedetti, S., Lang, G. & ingalls, R. (1961). Electric quadrupole splitting and the nuclear volume effect in the ions of Fe57. Phys. Rev. Lett. 6, 6062.Google Scholar
Debrunner, P. G. (1969). Mössbauer spectroscopy of biomolecules. In Spectroscopic Approaches to Biomolecular Conformation. Ed. Urry, D. W.Chicago: American Medical Association Press.Google Scholar
Eicher, H. & Trautwein, A. (1969). Electronic structure and quadrupole splittings of ferrous iron in hemoglobin. J. chem. Phys. 50, 25402551.Google Scholar
Feher, G. & Richards, P. L. (1967). Determination of the zero field splitting ‘D’ in heme chloride by far-infra red spectroscopy. In Magnetic Resonance in Biological Systems, pp. 141147. Oxford and New York: Pergamon Press.Google Scholar
Fraunfelder, H. (1963). The Mössbauer Effect. New York: W. A. Benjamin.Google Scholar
Gonser, U. & Grant, R. W. (1965). Mössbauer effect in haemoglobin and some iron containing biological compounds. Biophys. J. 5, 823844.CrossRefGoogle ScholarPubMed
Grant, R. W., Cape, J. A. & Gonser, U. (1967). Spin state of divalent Fe in anhydrohemoglobin. Biophys. J. 7, 651658.CrossRefGoogle Scholar
Griffith, J. S. (1957). Theory of electron resonance in ferri-haemoglobin azide. Nature, Lond. 180, 3031.Google Scholar
Iizuka, T. (1969). Analysis of thermal equilibrium between high-spin and low-spin states of ferrimyoglobin complexes. Biochim. biophys. Ada 181, 275286.CrossRefGoogle ScholarPubMed
Iizuka, T., Kotani, M. & Yonetani, T. (1968). A thermal equilibrium between high and low spin states in ferric cytochrome c peroxidase and some discussion on complex ES. Biochim. biophys. Acta 167 (2), 257267.CrossRefGoogle Scholar
Ingalls, R. (1964). Electric-field gradient tensor in ferrous compounds. Phys. Rev. 133, A787A795.Google Scholar
Johnson, C. E. (1966). Hyperfine field of 57Fe in hemin. Phys. Rev. Lett. 21, 491492.Google Scholar
Johnson, C. E. (1967). Hyperfine interactions in ferrous fluosilicate. Proc. phys. Soc. 2, 748757.CrossRefGoogle Scholar
Johnson, C. E., Cranshaw, T. E. & Ridout, M. S. (1965). Hyperfine coupling of Fe3+ in aluminium oxide. Proc. Int. Conf. Magnetism, Nottingham, 1964 (Institute of Physics and The Physical Society, London, 1965), p. 459.Google Scholar
Johnson, C. E., Elstner, E., Gibson, J. F., Benfield, G., Evans, M. C. W. & Hall, D. C. (1968). Mössbauer effect in the ferredoxin of euglena. Nature, Lond. 220, 12911293.CrossRefGoogle ScholarPubMed
Kotani, M. & Morimoto, H. (1967). EPR studies of single crystals of myoglobin and myoglobin fluoride. In Magnetic Resonance in Biological Systems, pp. 135140. Oxford and New York: Pergamon Press.CrossRefGoogle Scholar
Lang, G. (1968 a). Neighbor nucleus effect in a Mössbauer spectrum. Phys. Rev. Lett. 26A, 223224.Google Scholar
Lang, G. (1968 b). Magnetic hyperfine interactions in Mössbauer spectra. Conference on Properties of iron proteins, B.L. (Stanford) Report 208, 106123.Google Scholar
Lang, G., Asakura, T. & Yonetani, T. (1969 a). Mössbauer spectroscopy of mesohaem and protohaem myoglobins and their fluoride complexes.Proceedings of the Conference on Applications of the Mössbauer Effect,Tihany, Hungary. To be published.Google Scholar
Lang, G., Asakura, T. & Yonetani, T. (1969 b). Mössbauer spectroscopy of protohaem and mesohaem cytochrome c peroxidases and their fluorides. Proc. phys. Soc. Journal of Physics C. To be published.Google Scholar
Lang, G., Herbert, D. & Yonetani, T. (1968). Mössbauer spectroscopy of cytochrome c. J. chem. Phys. 49, 944950.Google Scholar
Lang, G. & Marshall, W. (1966). Mössbauer effect in some haemoglobin compounds. Proc. phys. Soc. 87, 334.CrossRefGoogle Scholar
Lang, G. & Oosterhuis, W. T. (1969). Calculated Paramagnetic Mössbauer Spectra of Spin ½ Iron Salts. J. chem. Phys. 51, 36083614.Google Scholar
Maeda, Y. (1967). Mössbauer effect in peroxidase-hydrogen peroxide compounds. Biochem. biophys. Res. Commun. 29, 680685.Google Scholar
Maeda, Y. (1968). Mössbauer spectroscopy of peroxidase and its derivatives. J. physiol. soc. Japan 24, 151159.CrossRefGoogle Scholar
May, L. (1969). Index of Publications in Mössbauer Spectroscopy. Catholic University of America, Washington, D.C.Google Scholar
Maling, J. E. & Weissbluth, M. (1969). The application of Mössbauer spectroscopy to the study of iron in heme proteins. In Solid State Biophysics. Ed. Wyard, S. J.. New York: McGraw-Hill.Google Scholar
Morimoto, H. & Kotani, M. (1966). Fluorine superhyperfine structure in the EPR spectra of the single crystal of the myoglobin fluoride. Biochim. biophys. Acta 126, 176178.Google Scholar
Moss, T. H., Ehrenberg, A. & Bearden, A. J. (1969). Mössbauer spectroscopic evidence for the electronic configuration of iron in horse radish peroxidase and its peroxide derivatives. Biochemistry, to be published.CrossRefGoogle Scholar
Oosterhuis, W. T. & Lang, G. (1969 a). Mössbauer effect in K3Fe(CN)6, Phys. Rev. 178, 439456.CrossRefGoogle Scholar
Oosterhuis, W. T. & Lang, G. (1969 b). Mössbauer effect in low-spin (d7) complex molecules of Fe. J. chem. Phys. 50, 43814387.Google Scholar
Preston, R. S., Hanna, S. S. & Heberle, J. (1962). The Mössbauer effect in metallic iron. Phys. Rev. 128, 22072218.CrossRefGoogle Scholar
Pryce, M. H. L. (1950). A modified perturbation procedure for a problem in paramagnetism. Proc. phys. Soc. 63A, 2529.Google Scholar
Salmeen, I. & Palmer, G. (1968). Electron paramagnetic resonance of beef-heart ferricytochrome c. J. chem. Phys. 48, 20492052.CrossRefGoogle ScholarPubMed
Sancier, K. M., Freeman, G.G., & Mills, J. S.. (1962). Electron spin resonance of nitric oxide-hemoglobin complexes in solution. Science, N. Y. 137, 752754.Google Scholar
Walker, L. R., Wertheim, G. K. & Jaccarino, V. (1961). Interpretation of the Fe57 Isomer Shift. Phys. Rev. Lett. 6, 98101.Google Scholar
Wertheim, G. K. (1964). Mössbauer effect: Principles and applications. New York: Academic Press.Google Scholar
Wittenberg, B. A., Kampa, L., Wittenberg, J. B., Blumberg, W. E. & Peisach, J. (1968). The electronic structure of protoheme proteins. II. An electron paramagnetic resonance and optical study of cytochrome c peroxidase and its derivatives. J. biol. Chem. 243, 18631870.CrossRefGoogle Scholar
Yonetani, T. & Schleyer, H. (1967). Electromagnetic properties of hemoproteins. II. The effect of physical states on electron paramagnetic resonance parameters of hemoproteins. J. biol. Chem. 242, 39193926.CrossRefGoogle ScholarPubMed
Yonetani, T., Schleyer, H. & Ehrenberg, A. (1966). Studies on cytochrome c peroxidase. VII. Electron paramagnetic resonance absorptions of the enzyme and complex ES in dissolved and crystalline forms. J. biol. Chem. 241, 32403242.CrossRefGoogle ScholarPubMed