Abstract
Saturation transfer EPR spectroscopy (STEPR) provides a means for investigating weak spin-spin interaction between spin-labelled molecules because the spectral intensity is proportional to the effective spin-lattice relaxation time,T 1 eff. Rate equations for the spin population defferences yield equivalent results for the dependence ofT 1 eff on the physical (or chemical) and Heisenberg spin exchange rates and show thatT 1 eff depends on the extent of redistribution of saturation throughout the anisotropic spin label powder lineshape. This approach yields a particularly simple formulation for the dependence of the STEPR lineshape on slow rotational diffusion. The effects of spin exchange are readily distinguished from those of slow rotational diffusion because of the insensitivity of the STEPR lineshape in the former case. The characteristic dependence of the STEPR spectral intensity on spin concentration allows determination of the exchange rate and can be used for studying slow translational diffusion, e.g. of spin-labelled proteins. Dipolar relaxation induced by paramagnetic ions gives a linear dependence of the reciprocal spin label STEPR intensity on metal ion concentration. STEPR measurements with spin-labelled lipid molecules in gel phase membranes in the presence of Ni2+ ions yield reliable distance information and provide calibrations for use with other systems.
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References
Thomas D.D., Dalton L.R., Hyde J.S.: J. Chem. Phys.65, 3006–3024 (1976)
Hyde J.S., Dalton L.R. in: Spin Labelling (Berliner L.J. ed.) vol. II, pp. 1–70, New York: Academic Press 1979.
Marsh D., Horváth L.I. in: Advanced EPR. Applications in Biology and Biochemistry (Hoff A.J. ed.), pp. 707–752. Amsterdam: Elsevier 1989.
Horváth L.I., Dux L., Hankovszky H.O., Hideg K., Marsh D.: Biophys. J.58, 231–241 (1990)
Hyde J.S., Subczynski W.K. in: Biological Magnetic Resonance (Berliner L.J., Reuben J. eds.), vol. 8, pp. 399–425. New York: Plenum Press 1989.
Hyde J.S., Swartz H.M., Antholine W.E. in: Spin Labelling (Berliner L.J. ed.), vol. II, pp. 71–113. New York: Academic Press 1979.
Eastman M.P., Kooser R.G., Das M.R., Freed J.H.: J. Chem. Phys.51, 2690–2709 (1969)
Marsh D., Horváth L.I.: J. Magn. Reson. (1992) in press.
Marsh D.: J. Magn. Reson. (1991) submitted for publication.
Yin J.-J., Hyde J.S.: J. Magn. Reson.74, 82–93 (1987)
Slichter C.P.: Principles of Magnetic Resonance, 2nd ed., p. 9. Berlin-Heidelberg-New York: Springer-Verlag 1978.
Fajer P., Thomas D.D., Feix J.B., Hyde J.S.: Biophys. J.50, 1195–1202 (1986)
Marsh D., Horváth L.I.: J. Magn. Reson. (1991) submitted for publication.
Marsh D.: J. Magn. Reson.87, 357–362 (1990)
Khramtsov V.V., Marsh D.: Biochim. Biophys. Acta (1991) in press.
Horváth L.I., Marsh D.: J. Magn. Reson.54, 363–373 (1983)
Páli T., Bartucci R., Horváth L.I., Marsh D.: Biophys. J. (1991) submitted for publication.
Bloembergen N.: Physica15, 386–426 (1949)
Solomon I.: Phys. Rev.99, 559–565 (1955)
Bertini I., Luchinat C.: NMR of Paramagnetic Molecules in Biological Systems. p. 50. Menlo Park: Benjamin/Cummings 1986.
Friedman H.L., Holz M., Hertz H.G.: J. Chem. Phys.70, 3369–3383 (1979)
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Marsh, D. Exchange and dipolar spin-spin interaction and rotational diffusion in saturation transfer EPR spectroscopy. Appl. Magn. Reson. 3, 53–65 (1992). https://doi.org/10.1007/BF03166780
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DOI: https://doi.org/10.1007/BF03166780