Abstract
The temperature dependence of the Raman electron spin-lattice relaxation rate is a sensitive probe of the low-frequency vibrational spectrum of the structure surrounding a paramagnetic ion. If ρ(ν), the density of these low-frequency vibrational states, varies with frequency as a simple ν m−1 power law, then the Raman relaxation rate varies with temperature as T 3+2m at low temperatures, where m is the spectral dimension. In proteins m is found to be much reduced from the value of 3 that is normally observed in three-dimensional crystalline solids. Various theoretical models are discussed. Data are presented which contrast electron spin relaxation in proteins with that observed in amorphous materials (where two-level tunneling states are involved in the relaxation mechanism) and glasses (where the temporal profile of the spin recovery follows a stretched exponential).
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References
J.P. Allen, Ph.D. Thesis, Physics Department, University of Illinois, Urbana, IL, 1982 (unpublished).
J.P. Allen, J.Y. Colvin, D.G. Stinson, C.P. Flynn, and H.J. Stapleton, Biophys. J. 38, 299 (1982).
S. Alexander and R. Orbach, J. Phys. Lett. (France) 43, L625 (1982).
S. Alexander, O. Entin-Wohlman, and R. Orbach, J. Phys. Lett. (France) 46, L555 (1985).
T.R. Askew, H.J. stapleton, and K.L. Brower, Phys. Rev. B: Solid State 33, 445 (1986).
F.C. Bernstein, T.F. Koetzle, G.J.B. Williams, E.F. Meyer, Jr., M.D. Brice, J.D. Rodgers, 0. Vennard, T. Shimanouchi, and M. Tasumu, J. Mol. Biol. 112, 535 (1977).
T. Bray, G.C. Brown, Jr., and A. Kiel, Phys. Rev. 127, 730 (1962).
J.T. Colvin and H.J. Stapleton, J. Chem. Phys. 82, 4699 (1985).
R. Elber and M. Karplus, Phys. Rev. Lett. 56, 394 (1986).
J.P. Gayda, P. Bertrand, A. Deville, C. More, G. Roger, J.F. Gibson, and R. Cammack, Biochim. Biophys. Acta. 581, 15 (1979).
N. Go, T. Noguti, and T. Nishikawa, Proc. Natl. Acad. Sci. U.S.A. 80, 3696 (1983).
J.S. Helman, A. Coniglio, and C. Tsallis, Phys. Rev. Lett. 53, 1195 (1984).
R.C. Herrick and H.J. Stapleton, J. Chem. Phys. 65, 4778 (1976).
C. Mailer and C.P.S. Taylor, Biochim. Biophys. Acta 322, 195 (1973).
P.J. Muench, T.R. Askew, J.T. Colvin, and H.J. Stapleton, J. Chem. Phys. 81, 63 (1984).
P.J. Muench, G.C. Wagner, and H.J. Stapleton, Bull. Am. Phys. Soc. 31, 388 (1986).
R. Orbach and H.J. Stapleton, “Electron Spin-Lattice Relaxation” in Electron Paramagnetic Resonance, S. Geschwind, Ed., Plenum, New York, 1972
R. Rammal and G.J. Toulouse, J. Phys. Lett. (France) 44, L13 (1983).
C.P. Scholes, H.T. Janakiraman, and T.E. King, Biophys. J. 45, 1027 (1984).
D.L. Smith, H.J. Stapleton, and M.B. Weissman, Phys. Rev. B: Solid State (to be published) (1986).
H.J. Stapleton, Magn. Reson. Rev. 1, 65 (1972).
H.J. Stapleton, Phys. Rev. Lett. 54, 1734 (1985).
H.J. Stapleton, J.P. Allen, C.P. Flynn, D.G. Stinson, and S. Kurtz, Phys. Rev. Lett. 45, 1456 (1980).
G.C. Wagner, J.T. Colvin, J.P. Allen, and H.J. Stapleton, J. Am. Chem. Soc. 107, 5589 (1985).
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Stapleton, H.J. (1987). Spectral Dimensions of Paramagnetic Proteins. In: Barrett, T.W., Pohl, H.A. (eds) Energy Transfer Dynamics. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-71867-0_20
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DOI: https://doi.org/10.1007/978-3-642-71867-0_20
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