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Part of the book series: Biological Magnetic Resonance ((BIMR,volume 24/B))

Abstract

Various aspects of the branch of non-linear spectroscopy that is known as saturation transfer (ST) EPR are reviewed, ranging from its inception to the present day. Initial methodological development was by Hyde and Dalton, followed by the introduction into biology by Hyde and Thomas. ST-EPR is a continuous wave spectroscopy, which extends the sensitivity of conventional nitroxide EPR to the microsecond (or submillisecond) correlation time regime of rotational motion, for spin-labelled membranes and biopolymers. Equally, slow exchange processes are accessible to ST-EPR, as are the paramagnetic relaxation enhancements that are essential to site-directed spin-labelling strategies. Central to the latter are the principles of spin-label oximetry, as developed by Hyde and coworkers at the Milwaukee EPR Centre.

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References

  • Abragam, A. (1961). The Principles of Nuclear Magnetism. Oxford: Oxford University Press, 1961.

    Google Scholar 

  • Baroin A., Thomas D.D., Osborne B., Devaux P.F. (1977) Saturation transfer electron paramagnetic resonance on membrane-bound proteins. I. Rotational diffusion of rhodopsin in the visual receptor membrane. Biochem Biophys Res Commun 78, 442–447.

    Article  PubMed  CAS  Google Scholar 

  • Bloembergen N. (1949). On the interaction of nuclear spins in a crystalline lattice. Physica 15, 386–426.

    CAS  Google Scholar 

  • Cherry R.J., Godfrey R.E. (1981). Anisotropic rotation of bacteriorhodopsin in lipid membranes. Biophys J. 36, 257–276.

    PubMed  CAS  Google Scholar 

  • Clegg R.M., Vaz W.L.C. (1985). “Translation diffusion of proteins and lipids in artificial lipid bilayer membranes. A comparison of experiment with theory.” In Progress in Protein-Lipid Interactions., Watts A., de Pont J.J.H.H.M., eds. Amsterdam: Elsevier,, pp. 173–229.

    Google Scholar 

  • Corless J.M., McCaslin D.R., Scott B.L. (1982). Two-dimensional rhodopsin crystals from disk membranes of frog retinal rod outer segments. Proc Natl Acad Sci USA 79, 1116–1120.

    PubMed  CAS  Google Scholar 

  • Deatherage J.F., Henderson R., Capaldi R.A. (1982) Relationship between membrane and cytoplasmic domains in cytochrome c oxidase by electron microscopy in media of different density. J Mol Biol 158, 501–514.

    PubMed  CAS  Google Scholar 

  • Downer N.W. (1985) Cross-linking of dark adapted frog photoreceptor disk membranes-evidence for monomeric rhodopsin. Biophys J 47, 285–293.

    PubMed  CAS  Google Scholar 

  • Eastman M.P., Kooser R.G., Das M.R., Freed J.H. (1969) Studies of Heisenberg spin exchange in ESR spectra. I. Linewidth and saturation effects. J Chem Phys 51, 2690–2709.

    Article  CAS  Google Scholar 

  • Esmann M., Hideg K., Marsh D. (1994) Influence of poly(ethylene glycol) and aqueous viscosity on the rotational diffusion of membranous Na, K-ATPase. Biochemistry 33, 3693–3697.

    PubMed  CAS  Google Scholar 

  • Esmann M., Marsh D. (1992) Local translational diffusion rates of membranous Na +,K +-ATPase measured by saturation transfer ESR spectroscopy. Proc Natl Acad Sci USA 89, 7606–7609.

    PubMed  CAS  Google Scholar 

  • Evans C.A. (1981) Use of integral of saturation transfer electron paramagnetic spectra to determine molecular rotational correlation times. Slowly tumbling spin labels in the presence of rapidly tumbling spin labels. J Magn Reson 44, 109–116.

    CAS  Google Scholar 

  • Fajer P., Knowles P.F., Marsh D. (1989) Rotational motion of yeast cytochrome oxidase in phosphatidylcholine complexes studied by saturation-transfer electron spin resonance. Biochemistry 28, 5634–5643.

    Article  PubMed  CAS  Google Scholar 

  • Fajer P., Marsh D. (1983a) Analysis of dispersion mode saturation-transfer ESR spectra. Application to model membranes. J Magn Reson 55, 205–215.

    CAS  Google Scholar 

  • Fajer P., Marsh D. (1983b) Sensitivity of saturation transfer ESR spectra to anisotropic rotation. Application to membrane systems. J Magn Reson 51, 446–459.

    CAS  Google Scholar 

  • Fajer P., Thomas D.D., Feix J.B., Hyde J.S. (1986) Measurement of rotational molecular motion by time-resolved saturation transfer electron paramagnetic resonance. Biophys J 50, 1195–1202.

    PubMed  CAS  Google Scholar 

  • Halbach K. (1954) Über eine neue Methode zur Messung von Relaxationszeiten und über den Spin von Cr 53. Helv Phys Acta 27, 259–282.

    CAS  Google Scholar 

  • Hidalgo C., Thomas D.D., Ikemoto N. (1978) Effect of the lipid environment on protein motion and enzymatic activity of the sarcoplasmic reticulum calcium ATPase. J Biol Chem 253, 6879–6887.

    PubMed  CAS  Google Scholar 

  • Hoffmann W., Pink D.A., Restall C., Chapman D. (1981) Intrinsic molecules in fluid phospholipid bilayers. Fluorescence probe studies. Eur J Biochem 114, 585–589.

    Article  PubMed  CAS  Google Scholar 

  • Holzenburg A., Jones P.C., Franklin T., Páli T., Heimburg T., Marsh D., Findlay J.B.C., Finbow M.E. (1993) Evidence for a common structure for a class of membrane channels. Eur J Biochem 213, 21–30.

    Article  PubMed  CAS  Google Scholar 

  • Horváth L.I., Brophy P.J., Marsh D. (1988) Influence of lipid headgroup on the specificity and exchange dynamics in lipid-protein interactions. A spin label study of myelin proteolipid apoprotein-phospholipid complexes. Biochemistry 27, 5296–5304.

    PubMed  Google Scholar 

  • Horváth L.I., Brophy P.J., Marsh D. (1993) Exchange rates at the lipid-protein interface of the myelin proteolipid protein determined by saturation transfer electron spin resonance and continuous wave saturation studies. Biophys J 64, 622–631.

    PubMed  Google Scholar 

  • Horváth L.I., Dux L., Hankovszky H.O., Hideg K., Marsh D. (1990) Saturation transfer electron spin resonance of Ca 2+-ATPase covalently spin-labeled with β-substitutedvinyl ketone-and maleimide-nitroxide derivatives. Effects of segmental motion and labeling levels. Biophys J 58, 231–241.

    PubMed  Google Scholar 

  • Horváth L.I., Marsh D. (1988) Improved numerical evaluation of saturation transfer electron spin resonance spectra. J Magn Reson 80, 314–317.

    Google Scholar 

  • Horváth L.I., Marsh D. (1983) Analysis of multicomponent saturation transfer ESR spectra using the integral method: application to membrane systems. J Magn Reson 54, 363–373.

    Google Scholar 

  • Hubbell W.L., Altenbach C. (1994) “Site-directed spin-labeling of membrane proteins.” In Membrane protein structure: experimental approaches., White S.H., ed. New York: Oxford University Press, pp. 224–248.

    Google Scholar 

  • Hyde J.S. (1978) “Saturation-transfer spectroscopy.” In Methods in Enzymology, Hirs C.H.W., Timasheff S.N., eds. New York: Academic Press, pp. 480–511.

    Google Scholar 

  • Hyde J.S., Dalton L. (1972) Very slowly tumbling spin labels: adiabatic rapid passage. Chem Phys Lett 16:568–572.

    Article  CAS  Google Scholar 

  • Hyde J.S., Dalton L.R. (1979) “Saturation-transfer spectroscopy.” In Spin-Labeling II. Theory and Applications, Berliner L.J., ed. New York: Academic Press, pp. 71–113.

    Google Scholar 

  • Hyde J.S., Eriksson L.E.G., Ehrenberg A. (1970) EPR relaxation of slowly moving flavin radicals: “Anomalous” saturation. Biochim Biophys Acta 222, 688–692.

    PubMed  CAS  Google Scholar 

  • Hyde J.S., Subczynski W.K. (1989) “Spin-label oximetry.” In Spin Labeling. Theory and Applications, Berliner L.J., Reuben J., eds. New York and London: Plenum Press, pp. 399–425.

    Google Scholar 

  • Hyde J.S., Thomas D.D. (1973) New EPR methods for the study of very slow motion: application to spin-labeled hemoglobin. Ann N Y Acad Sci 222, 680–692.

    PubMed  CAS  Google Scholar 

  • Jesaitis A.J., Yguerabide J. (1986) The lateral mobility of the ATPase in Madin-Darby canine kidney cells. J Cell Biol 102, 1256–1263.

    Article  PubMed  CAS  Google Scholar 

  • Johnson M.E., Hyde J.S. (1981) 35-GHz (Q-band) saturation transfer electron paramagnetic resonance studies of rotational diffusion. Biochemistry 20, 2875–2880.

    PubMed  CAS  Google Scholar 

  • Kirino Y., Ohkuma T., Shimizu H. (1978) Saturation transfer electron spin resonance study on the rotational diffusion of calcium-and magnesium-dependent adenosine triphosphatase in sarcoplasmic reticulum membranes. J Biochem (Tokyo) 84, 111–115.

    CAS  Google Scholar 

  • Knowles P.F., Watts A., Marsh D. (1979) Spin label studies of lipid immobilization in dimyristoylphosphatidylcholine-substituted cytochrome oxidase. Biochemistry, 18, 4480–4487.

    Article  PubMed  CAS  Google Scholar 

  • Kurad D., Jeschke G., Marsh D. (2001) Spin-label HF-EPR of lipid ordering in cholesterol-containing membranes. Appl Magn Reson 21, 469–481.

    Article  CAS  Google Scholar 

  • Kusumi A., Hyde J.S. (1982) Spin-label saturation-transfer electron spin resonance detection of transient association of rhodopsin in reconstituted membranes. Biochemistry 21, 5978–5983.

    Article  PubMed  CAS  Google Scholar 

  • Kusumi A., Ohnishi S., Ito T., Yoshizawa T. (1978) Rotational motion of rhodopsin in the visual receptor membrane as studied by saturation-transfer spectroscopy. Biochim Biophys Acta 507, 539–543.

    CAS  Google Scholar 

  • Langen R., Isas J.M., Luecke H., Haigler H.T., Hubbell W.L. (1998) Membrane-mediated assembly of annexins studied by site-directed spin labeling. J Biol Chem 273, 22453–22457.

    Article  PubMed  CAS  Google Scholar 

  • Leigh Jr. J.S. (1970) ESR rigid-lattice line shape in a system of two interacting spins. J Chem Phys 52, 2608–2612.

    Article  CAS  Google Scholar 

  • Livshits V.A. (1974) Slow anisotropic tumbling in ESR spectra of nitroxyl radicals. J Magn Reson 24, 307–313.

    Google Scholar 

  • Livshits V.A., Dzikovski B.G., Marsh D.(2001) Mechanism of relaxation enhancement of spin labels in membranes by paramagnetic ion salts: dependence on 3d and 4f ions and on the anions. J Magn Reson 148, 221–237.

    Article  PubMed  CAS  Google Scholar 

  • Livshits V.A., Dzikovski B.G., Marsh D. (2003) Anisotropic motion effects in CW non-linear EPR spectra. Spin relaxation enhancement of lipid spin labels. J Magn Reson, in press.

    Google Scholar 

  • Livshits V.A., Marsh D. (2000) Spin relaxation measurements using first-harmonic out-of-phase absorption EPR signals: rotational motion effects. J Magn Reson 145, 84–94.

    Article  PubMed  CAS  Google Scholar 

  • Livshits V.A., Páli T., Marsh D. (1998a) Spin relaxation measurements using first-harmonic out-of-phase absorption EPR signals. J Magn Reson 134, 113–123.

    Article  PubMed  CAS  Google Scholar 

  • Livshits V.A., Páli T., Marsh D. (1998b) Relaxation time determinations by progressive saturation EPR: Effects of molecular motion and Zeeman modulation for spin labels. J Magn Reson 133, 79–91.

    Article  PubMed  CAS  Google Scholar 

  • Marsh D. (1980) Molecular motion in phospholipid bilayers in the gel phase: long axis rotation. Biochemistry 19, 1632–1637.

    PubMed  CAS  Google Scholar 

  • Marsh D. (1990) Sensitivity analysis of magnetic resonance spectra from unoriented samples. J Magn Reson 87, 357–362.

    CAS  Google Scholar 

  • Marsh D. (1992a) Influence of nuclear relaxation on the measurement of exchange frequencies in CW saturation EPR studies. J Magn Reson 99, 332–337.

    CAS  Google Scholar 

  • Marsh D. (1992b) Exchange and dipolar spin-spin interactions and rotational diffusion in saturation transfer EPR spectroscopy. Appl Magn Reson 3, 53–65.

    Article  CAS  Google Scholar 

  • Marsh D. (1995) Sensitivity of the continuous wave saturation of conventional EPR spectra to slow rotational motion. Spectrochim Acta 51A, 111–114.

    CAS  Google Scholar 

  • Marsh D., Horváth L.I. (1989) “Spin-label studies of the structure and dynamics of lipids and proteins in membranes.” In Advanced EPR. Applications in Biology and Biochemistry, Hoff A.J., ed. Amsterdam: Elsevier, pp. 707–752.

    Google Scholar 

  • Marsh D., Horváth L.I. (1992a) A simple analytical treatment of the sensitivity of saturation transfer EPR spectra to slow rotational diffusion. J Magn Reson 99, 323–331.

    CAS  Google Scholar 

  • Marsh D., Horváth L.I. (1992b) Influence of Heisenberg spin exchange on conventional and phase-quadrature EPR lineshapes and intensities under saturation. J Magn Reson 97, 13–26.

    CAS  Google Scholar 

  • Marsh D., Horváth L.I. (1998) Structure, dynamics and composition of the lipid-protein interface. Perspectives from spin-labelling. Biochim Biophys Acta 1376, 267–296.

    PubMed  CAS  Google Scholar 

  • Marsh D., Kurad D., Livshits V.A. (2002) High-field electron spin resonance of spin labels in membranes. Chem Phys Lipids 116, 93–114.

    PubMed  CAS  Google Scholar 

  • Marsh D., Livshits V.A., Páli T. (1997) Non-linear, continuous-wave EPR spectroscopy and spin-lattice relaxation: spin-label EPR methods for structure and dynamics. J Chem Soc Perkin Trans 2, 2545–2548.

    Google Scholar 

  • Marsh D., Páli T., Horváth L.I. (1998) “Progressive saturation and saturation transfer EPR for measuring exchange processes and proximity relations in membranes.” In Spin Labeling. The Next Millenium., Berliner L.J., ed. New York: Plenum Press, pp. 23–82.

    Google Scholar 

  • Maunsbach A.B., Skriver E., Soderholm M., Hebert H. (1989) “Three-dimensional structure and topography of membrane bound Na,K-ATPase.” In The Na,K-Pump. Part A: Molecular Aspects. Progress in Clinical and Biological Research., Skou J.C., Norby J.G., Maunsbach A.B., Esmann M., eds. New York: Alan Liss, pp. 39–56.

    Google Scholar 

  • McLaughlin A., Gratwohl G., McLaughlin S. (1978) The adsorption of divalent cations to phosphatidylcholine bilayer membranes. Biochim Biophys Acta 513, 338–357.

    PubMed  CAS  Google Scholar 

  • Molin Y.N., Salikov K.M., Zamaraev K.I. (1980) Spin Exchange. Principles and Applications in Chemistry and Biology. Berlin: Springer Verlag.

    Google Scholar 

  • Páli T., Bartucci R., Horváth L.I., Marsh D. (1992) Distance measurements using paramagnetic ion-induced relaxation in the saturation transfer electron spin resonance of spin-labeled biomolecules. Application to phospholipid bilayers and interdigitated gel phases. Biophys J 61, 1595–1602.

    PubMed  Google Scholar 

  • Páli T., Finbow M.E., Marsh D. (1999) Membrane assembly of the 16-kDa proteolipid channel from Nephrops norvegicus studied by relaxation enhancements in spin-label ESR. Biochemistry 38, 14311–14319.

    PubMed  Google Scholar 

  • Páli T., Horváth L.I., Marsh D. (1993) Continuous-wave saturation of two-component, inhomogeneously broadened, anisotropic EPR spectra. J Magn Reson A101, 215–219.

    Google Scholar 

  • Páli T., Livshits V.A., Marsh D. (1996) Dependence of saturation-transfer EPR intensities on spin-lattice relaxation. J Magn Reson B 113, 151–159.

    PubMed  Google Scholar 

  • Portis A.M. (1955) Rapid passage in electron spin resonance. Phys Rev 100, 1219–1224.

    Article  CAS  Google Scholar 

  • Robinson B.H., Dalton L.R. (1980) Anisotropic rotational diffusion studied by passage saturation transfer electron paramagnetic resonance. J Chem Phys 72, 1312–1324.

    Article  CAS  Google Scholar 

  • Rousselet A., Devaux P.F. (1977) Saturation transfer electron paramagnetic resonance on membrane bound proteins. II. Absence of rotational diffusion of the cholinergic receptor protein in Torpedo marmorata membrane fragments. Biochem Biophys Res Commun 78, 448–454.

    Article  PubMed  CAS  Google Scholar 

  • Ryba N.J.P., Marsh D. (1992) Protein rotational diffusion and lipid/protein interactions in recombinants of bovine rhodopsin with saturated diacylphosphatidylcholines of different chain lengths studied by conventional and saturation transfer electron spin resonance. Biochemistry 31, 7511–7518.

    Article  PubMed  CAS  Google Scholar 

  • Saffman P.G., Delbrück M. (1976) Brownian motion in biological membranes. Proc Natl Acad Sci USA 72, 3111–3113.

    Google Scholar 

  • Slichter, C. P. (1978) Principles of Magnetic Resonance. Berlin-Heidelberg-New York: Springer-Verlag,.

    Google Scholar 

  • Snel M.M.E., Marsh D. (1994) Membrane location of apocytochrome c and cytochrome c determined from lipid-protein spin exchange interactions by continuous wave saturation electron spin resonance. Biophys J 67, 737–745.

    Article  PubMed  CAS  Google Scholar 

  • Solomon I. (1955) Relaxation processes in a system of 2 spins. Phys Rev 99, 559–565.

    Article  CAS  Google Scholar 

  • Squier T.C., Thomas D.D. (1986) Methodology for increased sensitivity and precision in saturation transfer electron paramagnetic resonance studies of molecular dynamics. Biophys J 49, 921–935.

    PubMed  CAS  Google Scholar 

  • Tardieu A. (1972) Thesis/Dissertation. Université de Paris-Sud..

    Google Scholar 

  • Thomas D.D., Dalton L.R., Hyde J.S. (1976) Rotational diffusion studied by passage saturation transfer electron paramagnetic resonance. J Chem Phys 65, 3006–3024.

    Article  CAS  Google Scholar 

  • Thomas D.D., McConnell H.M. (1974) Calculation of paramagnetic resonance spectra sensitive to very slow rotational motion. Chem Phys Lett 25, 470–475.

    Article  CAS  Google Scholar 

  • Thomas D.D., Seidel J.C., Hyde J.S., Gergely J. (1975) Motion of subfragment-1 in myosin and its supramolecular complexes: saturation transfer electron paramagnetic resonance. Proc Natl Acad Sci USA 72, 1729–1733.

    PubMed  CAS  Google Scholar 

  • Weger M. (1960) Passage effects in paramagnetic resonance experiments. Bell Syst Tech J 39, 1013–1112.

    Google Scholar 

  • Yin J.J., Hyde J.S. (1987) Application of rate equations to ELDOR and saturation recovery experiments on N-14-N-15 spin label pairs. J Magn Reson 74, 82–93.

    CAS  Google Scholar 

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Marsh, D., Horváth, L.I., Pálib, T., Livshits, V.A. (2005). Saturation Transfer Spectroscopy of Biological Membranes. In: Eaton, S.R., Eaton, G.R., Berliner, L.J. (eds) Biomedical EPR, Part B: Methodology, Instrumentation, and Dynamics. Biological Magnetic Resonance, vol 24/B. Springer, Boston, MA. https://doi.org/10.1007/0-306-48533-8_11

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