Electron Paramagnetic Resonance Spectroscopy of Metalloproteins

  • Richard Cammack
Part of the Methods in Molecular Biology book series (MIMB, volume 17)

Abstract

Electron paramagnetic resonance (EPR), or electron spin resonance (ESR) spectroscopy, is a technique for studying paramagnetic materials, the molecules of which contain unpaired electrons. These comprise organic free radicals and transition metal ions. The biological significance of these rare species is that they often occur at the active sites of enzymes and the electron-transfer systems of bioenergetics. Manganese ions are of special significance in molecular biology, because they can often bind to nucleotides and nucleic acids in a similar way to magnesium, and serve as probes of their environment.

Keywords

Dust Microwave Anisotropy Cobalt Manganese 

References

  1. 1.
    Czoch, R and Francik, A (1989) Instrumental Effects in Homodyne Electron Paramagnetic Resonance Spectrometers Ellis Horwood, Chichester; Wiley, New YorkGoogle Scholar
  2. 2.
    Eaton, G R and Eaton, S. (1990) Electron paramagnetic resonance, in Analytical Instrumentation Handbook (Ewing, G W, ed.), Marcel Dekker, New York, pp. 467–530.Google Scholar
  3. 3.
    Wertz, J. E. and Bolton, J R. (1986) Electron Spin Resonance. McGraw-Hill, New YorkGoogle Scholar
  4. 4.
    Gibson, J F. (1987) Electron paramagnetic resonance in metalloproteins, in Spectroscopy of Inorganic-Based Materials (Hester, R, ed.), Wiley, Chichester, pp 333–406Google Scholar
  5. 5.
    Dutton, P. L (1978) Redox potentiometry. determination of midpoint potentials of oxidation-reduction components of biological electron-transfer systems, in Methods in Enzymology Biomembranes' vol. 54 (Fleischer, S and Packer L, eds.), Academic, New York, pp 411–435.CrossRefGoogle Scholar
  6. 6.
    Ballou, D. P (1978) Freeze-quench and chemical-quench techniques, in Methods in Enzymology: Biomembranes, vol 54 (Fleischer, S and Packer, L, eds), Academic, New York, pp 85–93.CrossRefGoogle Scholar
  7. 7.
    Maret, W and Zeppezauer, M (1988) Preparation of metal-hybrid enzymes, in Methods in Enzymology, vol 158 (Riordan, J F and Vallee, B L, eds), Academic, New York, pp. 79–94.Google Scholar
  8. 8.
    George, G N and Bray, R C (1988) Studies by electron paramagnetic resonance spectroscopy of xanthine oxidase enriched with molybdenum-95 and with molybdenum-97 Biochemistry 27, 3603–3610.CrossRefGoogle Scholar
  9. 9.
    Poole, R K, Blum, H, Scott, R I, Collinge, A, and Ohnishi, T (1980) The orientation of cytochromes in membrane multilayers prepared from aerobically grown Escherichia coli K12. J Gen. Microbiol 119, 145–154Google Scholar
  10. 10.
    Randolph, M L (1972) Quantitative considerations in electron spin resonance studies of biological materials, in Biological Applications of Electron Spin Resonance (Swartz, H M, Bolton, J R, and Borg, D C, eds.), Wiley-Interscience, New York, pp 119–133Google Scholar
  11. 11.
    Rupp, H, Rao, K K, Hall, D O, and Cammack, R (1978) Electron spin relaxation of iron-sulphur proteins studied by microwave power saturation Biochim Biophys Acta 537, 255–269Google Scholar
  12. 12.
    Bray, R C (1988) The morgamc biochemistry of molybdoenzymes. Q Rev. Biophys. 21, 299–330CrossRefGoogle Scholar

Copyright information

© Humana Press Inc., Totowa, NJ 1993

Authors and Affiliations

  • Richard Cammack
    • 1
  1. 1.Division of Biomolecular SciencesKing’s College LondonUK

Personalised recommendations