Skip to main content

Depth of Immersion of Paramagnetic Centers in Biological Systems

  • Chapter
Distance Measurements in Biological Systems by EPR

Part of the book series: Biological Magnetic Resonance ((BIMR,volume 19))

Abstract

The theory of static and dynamic dipole-dipole and exchange spin-spin interactions between radicals and paramagnetic ions is surveyed. Methods of determination of depth of immersion and localization of a paramagnetic center, and the investigation of electrostatic potential around biologically important molecules are described in detail. Advantages and limitations of different methods are discussed. Applications of the methods to paramagnetic centers of enzymes (cytochrome P-450, the primary donor of the photosynthetic reaction center, and flavin-dependent alcohol oxidase) and to nitroxide spin probes in biological and model membranes are reviewed.

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 169.00
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 219.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info
Hardcover Book
USD 219.99
Price excludes VAT (USA)
  • Durable hardcover edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  • Abragam, A. and Bleaney, B. (1970) Electron Paramagnetic Resonance of Transition Ions, Clarendon Press, Oxford.

    Google Scholar 

  • Alakhverdiev, C. I., Kulikov, A.V., Klimov, V. V., Bogatyrenko, V. R., and Likhtenstein G. I. (1989) Determination of the depth of immersion of P680, pheophitin and secondary donor in photosystem 2 in pea subchloroplasts. Biofizika, 34, 434–439.

    Google Scholar 

  • Alexandrov, I. V. (1975) Theory of Magnetic Relaxation, Nauka, Moscow.

    Google Scholar 

  • Alfilov, E. I., Vosnyak, V. M., and Kazanzev, A. P. (1980) Effect of magnetic field on fluorescence of Rhodopseudomonas spheroidas. Biofizika 25, 498–505.

    Google Scholar 

  • Anni, H., Vanderkooi, J. M., Sharp, K. A., Yonetani,T., Hopkins, S. C., Herenyi, L. and Fidy, J. (1994) Electric field and conformational effects of cytochrome c and solvent on cytochrome c peroxidase studied by high resolution fluorescence spectroscopy. Biochemistry 33, 3475–3486.

    Article  PubMed  CAS  Google Scholar 

  • Aquist, J., Luecke, H., Quiocho, F. A. and Warshel, A. (1991) Dipoles localized at helix termini of proteins stabilize charges. Proc. Natl. Acad. Sci. USA 88, 2026–2030.

    Article  Google Scholar 

  • Averbakh, A.Z., Pekel, N.D., Seredenko V.I., Kulikov, A.V. and Gvozdev, R.I., (1995)Flavin-dependent alcohol oxidase from the yeast Pichiapinus. Biochem. J 310,601–604.

    CAS  Google Scholar 

  • Bashford, D., and Karplus, M. (1990) pKes of ionizable groups in proteins: atomic detail from a continuum electrostatic model. Biochemistry 29, 10219–10225.

    Article  PubMed  CAS  Google Scholar 

  • Berdnikov B. M., Doktorov, A. B. and Makarshin, L. L. (1980) Dipole-dipole broadening of free radicals ESR spectra in the presence of paramagnetic ions. Theor. Eksp. Chem. (Kiev) 16, 765–771.

    CAS  Google Scholar 

  • Blum, H., Leigh, J. S., Salerno, J. C. and Ohnishl, T (1978) The orientation of bovin adrenal cortex cytochrome P-450 in submitochondrial particle multilayers. Arch. Biochem. Biophys 187, 153–157.

    Article  PubMed  CAS  Google Scholar 

  • Bogatyrenko, V. R., Sabo, Ya., Chamorovskii, S K., Zakharova, N.I., Kononenko, A. A. and Kulikov A. V. (1991) Study of localization of bacteriochlorophyl dimer and cytochrome c in reaction centers from Chromatium minutissium by ESR. Biofizika 36, 289–290.

    Google Scholar 

  • Borah, B., and Bryant, R. G. (1981) Nuclear magnetic resonance relaxation dispersion in an aqueous nitroxide system. J. Chem. Phys 75, 3297–3300.

    Article  Google Scholar 

  • Bowman, M. K. and Norris, J. R. (1982) Cross relaxation of free radicals in partially ordered solids. J. Phys. Chem 86, 3385–3390.

    Article  CAS  Google Scholar 

  • Case, G. D. and Leigh, J. S., Jr. (1976) Intramitochondrial position of cytochrome haem groups determined by dipolar interaction with paramagnetic cations. Biochem. J. 160, 769–783

    PubMed Central  PubMed  CAS  Google Scholar 

  • Cherepanova, E.S., Kulikov, A.V. and Likhtenstein, G.I. (1990) Localization of paramagnetic centers relative to aqueous and lipid phases by ESR. Biol. Membr. (Moscow) 77, 51–56.

    Google Scholar 

  • Debye, P. (1942) Reaction rates in ionic solutions. Trans.Electrochem. Soc 82, 265–272.

    Article  Google Scholar 

  • Depmeier, B. J., Driessen, A. J., Hehre, W. J., Johnson, J., Peng, A. C., Lou, L. and Yu, J. (1996) MacSpartan version 1.0.2 Wavefunction, Irvine, CA.

    Google Scholar 

  • Derzhansci, A., Georgieva, A., Kotev, K. and Atanasov, B. P. (1970) Heam hydration and displacement in the pre-denaturational conformational transition of the myoglobin molecule. Biochim. Biophys. Acta 214, 83–93.

    Article  Google Scholar 

  • Druzhinin, S. Yu., Fogel, V. R., Syrtsova, L. A., Likhtenstein, G. I. and Kotelnikov, A. I. (1986) Study on the cofactor center localization in nitrogenase by triplet labeling method. Biofisika 31, 16–21.

    CAS  Google Scholar 

  • Dwek, R. A. (1977) NMR in Biology, Academic Press, New York.

    Google Scholar 

  • Eastman, M. P., Bruno, G. V. and Freed, J. H. (1970) Studies of Heisenberg spin exchange. II Effect of radical charge and size. J. Chem. Phys 52, 2511–2522.

    Article  CAS  Google Scholar 

  • Eaton, G. R and Eaton, S. S. (1989) Resolved electron-electron spin-spin splittings in ESR spectra. Biol. Magn. Reson 8, 339–397.

    Article  CAS  Google Scholar 

  • Feher, G. (1992) Three-dimensional structure of the reaction center by X-diffraction from single crystals, Is. J. Chem 32, 375–378.

    Article  Google Scholar 

  • Gilson, M. K. (1993) Multiple-site titration and molecular modeling: two rapid methods for computing energies and forces for ionizable groups in proteins. Proteins 15, 266–282.

    Article  PubMed  CAS  Google Scholar 

  • Gray, H. B., and Ellis, W. R. Jr (1994) Electron Transfer. In: Bioinorganic Chemistry. ( Bertini, I., Gray, G.B., Lippard S.J., and Valentine J.S. eds.) University Science Books, Mill Valley, California, 315–364.

    Google Scholar 

  • Grebenshchikov, Yu. B., Ponomarev, G. V., Evstigneeva, R. P. and Likhtenshtein, G. I. (1972) Spin relaxation of a nitroxide radical upon interaction with porphyrin complexes of VO(II), Fe(III), NI(II), Cu(II) and hemoglobin. Biofizika 17, 910–913.

    PubMed  CAS  Google Scholar 

  • Hecht, J. L., Honig, B., Shin, Y. and Hubbell, W. L. (1995) Electrostatic potential near the surface of DNA: comparing theory and experiment. J. Phys. Chem 99, 7782–7786.

    Article  CAS  Google Scholar 

  • Honig, B. and Nicholls, A. (1995) Classical electrostatics in biology and chemistry. Science 268, 1144–1149.

    Article  PubMed  CAS  Google Scholar 

  • Hyde, J. S. and Subczinski, W. K. (1989) Spin-label oximetry, Biol. Magn. Reson 8, 399–426.

    Article  CAS  Google Scholar 

  • Hyde, J. S., Swartz, H. M. and Antholine, W. E. (1976) The spin probe-spin label methods. In: Spin Labeling. Theory and Application.Vol. 2. ( Berliner L. ed.) Academic Press, New York, pp. 72–113.

    Google Scholar 

  • Hwang, L. P. and Freed, J. H. (1975) Dynamics effect of pair correlation function on spinrelaxation by translational diffusion in liquids.,J. Chem. Phys. 63, 4017–4025.

    Article  CAS  Google Scholar 

  • Kokorin, A. I., Zamaraev, K. I., Grigoryan, G. L., Ivanov, V. P., and Rozantsev, E. G. (1972) Distance estimation between nitroxyl radicals. Biofizika 17, 34–41.

    PubMed  CAS  Google Scholar 

  • Kotel’nikov, A. I., Likhtenshtein, G. I. and Gvozdev, R. I. (1975) The use of phenomenon of saturation of the ESR signals for study of relief of a macromolecule in the vicinity of paramagnetic center. Studia Biophys. 49, 215–221.

    Google Scholar 

  • Kotel’nikov, A.I., Fogel, V.R., Likhtenshtein, G.I., Postnikova, G.B., and Slyapnikova, E.A. (1981) The use of the exchange deactivation of triplet excited states for the investigation of the structure and electronic conductivity of proteins. Mol. Biol. (Moscow) 15, 281–289.

    Google Scholar 

  • Kulikov, A.V. (1976) Determination of distance between the nitroxide label and a paramagnetic center in spin-labeled proteins from the parameters of the saturation curve of the ESR spectrum of the label at 77K. Mol. Biol. (Moscow) 10, 109–116.

    Google Scholar 

  • Kulikov, A. V. and Likhtenstein, G. I. (1974) Application of saturation curves for evaluating distances in biological objects by the method of double spin-labels. Biofizika 19, 420–424.

    PubMed  CAS  Google Scholar 

  • Kulikov, A. I. and Likhtenshtein, G. I. (1977) The use of spin-relaxation phenomena in the investigation of the structure of model and biological systems by method of spin labels. Adv. Molecul. Relax. Proc 10, 47–78.

    Article  CAS  Google Scholar 

  • Kulikov, A. I., Likhtenshtein, G. I., Rozantzev, E. G., Suskina, and Shapiro, A. V. (1972) Nitroxide bi-and polyradicals as standard models for distance estimation between the nitroxide moities. Biofizika, 17, 42–49.

    PubMed  CAS  Google Scholar 

  • Kulikov A. V., Bogatyrenko, V. R., Melnikov, A. V., Syrtzova, L. A. and Likhtenshtein, G. I. (1979) Determination of distance between cation radical of bacteriochlorophyl dimer and anion of quinone in photosynthetic reaction center from R. rubrum. Biofizika 24, 178–185.

    Google Scholar 

  • Kulikov, A. V., Cherepanova, E. S, and Bogatyrenko V. R. (1981) Determination of the closest distance between a radical and a paramagnetic ion. Theor. Exper. Chem 17, 618–626.

    Article  Google Scholar 

  • Kulikov, A. I., Yudanova, E. I. and Likhtenshtein, G. I. (1983a) Investigation of the spin-exchange of nitroxide radicals using the continuous ESR spectrum saturation technique. J. Phys. Chem. (Moscow) 56, 2982–2987.

    Google Scholar 

  • Kulikov, A. V., Bogatyrenko, V. R., Likhtenstein, G. I., Allakhverdiev, S. I., Klimov, V. V., Shuvalov, V. A., Krasnovskii, A. A. (1983b) Magnetic interaction of Mn with anion radical of pheophytin and cation radical of chlorophyll in reaction centers of photosystem 2, Biofizika 28, 357–363.

    PubMed  CAS  Google Scholar 

  • Kulikov, A.V., Cherepanova, E.S., Bogatyrenko. V.R., Nasonova, T.A,. Fisher, V.R. and Yakubov, H.M. (1987) Determination of the depth of immersion of radicals into biological matrices by ESR. Bull. Acad. Sci. USSR, Div. Biol. Sci. N 5, 7762–7769.

    Google Scholar 

  • Kulikov, A. V., Cherepanova, E. S., Likhtenshtein, G. I., Uvarov, V. Yu. and Archakov, A. I. (1989) ESR Study of localization of cytochrome P450 in microsomes relative to aqueous and lipid phases. Biologich. Membrany 6, 1085–1094.

    CAS  Google Scholar 

  • Levitch, V. G., Dogonadze, R. R., German, E., Kuznetsov, A. N., and Kharakats, Yu. I. (1970) Theory of homogeneous reaction involving proton transfer. Electrochem. Acta 15, 353–368.

    Article  Google Scholar 

  • Likhtenshtein, G. I. (1968) Determination of the topography of proteins group using specific paramagnetic labels. Mol. Biol. (Moscow) 2, 234–240.

    CAS  Google Scholar 

  • Likhtenstein, G. I. (1976) Spin Labeling Methods in Molecular Biology, pp. 66–88, John Wiley & Son, New York.

    Google Scholar 

  • Likhtenstein, G. I. (1988a) Chemical Physics of Redox Metalloenzymes Catalysis. pp. 45–60, Springer Verlag, Heidelberg.

    Book  Google Scholar 

  • Likhtenshtein, G.I. (1988b) Structure and molecular dynamics of metalloenzymes studied by physical label methods. J. Molec. CataL 47, 128–129.

    Google Scholar 

  • Likhtenshtein, G.I. (1990) Nitroxide in the solution of some problems of chemical biophysics. Pure Appl. Chem 62, 281–288.

    CAS  Google Scholar 

  • Likhtenstein, G. I. (1993) Biophysical Labeling Methods in Molecular Biology, pp. 46–79, Cambridge University Press, New York, Cambridge.

    Book  Google Scholar 

  • Likhtenstein, G. I. (1995) Role of orbital overlap and local dynamics in long-distance electron transfer in photosynthetic centres and model systems. J. Photochem. Photobiol. A: Chemistry 96, 79–92.

    Article  Google Scholar 

  • Likhtenshtein, G. I., and Bobodzhanov, P. Kh. (1968) Investigation of the structure and local conformational changes of proteins and enzymes using double paramagnetic labels. Biofuika 13, 757–764.

    CAS  Google Scholar 

  • Likhtenstein, G. I., Grebentchikov, Yu. B., Bobodzhanov, P. Kh. and Kokhanov, Yu. V. (1970) Study on the proteins microstructure by method of spin-label paramagnetic probe. Mol. Biol. (Moscow) 4, 782–789.

    Google Scholar 

  • Likhtenstein, G. I., Grebentchikov, Yu. B., Rosantev, E. G. and Ivanov, V. P. (1972) Study on the electrostatic charges in proteins by method of paramagnetic probes. Mol. Biol. (Moscow) 6, 498–507.

    Google Scholar 

  • Likhtenshtein, G. I., Kotelnikov, A. I., and Kulikov, A. V. (1981) Structure of reaction centers of photosynthetic bacteria. Dokl. ANSSSR 257, 733–736.

    CAS  Google Scholar 

  • Likhtenshtein, G. I., Kulikov, A. V., Kotelnikov, A. I. and Bogatyrenko, V. R. (1982) Structure and action mechanism of reaction centers of photosynthetic bacteria. Photobiochem. Photobiol 3, 178–182.

    Google Scholar 

  • Likhtenshtein, G. I., Kulikov, A. V., Kotelnikov, A. I., and Levchenko, L. A. (1986) Methods of physical labels–a combined approach to the study of microstructure and dynamics of biological systems. J. Biochem. Biophys. Meth 12, 1–28.

    Article  Google Scholar 

  • Likhtenshtein, G. I., Kulikov, A. V. and Kotelnikov, A. V. (1993) Relaxation process involving nitroxyl radical in molecular biology. In: Bioactive Spin Labels ( Zhdanov, R. I., ed.) pp. 125–151, Springer-Verlag, Heidelberg.

    Google Scholar 

  • Likhtenshtein, G. I., Vaisbuch, I., Adin, I., Shames, A., and Glaser, R. (1997) Distribution of electrostatic-field around biological molecules studied by methods of spin-probes and NMR. Biophys. J. 72, Al29.

    Google Scholar 

  • Likhtenshtein, G. I., Adin I., Krasnoselsky,A., Vaisbuch, I. Shames, A., and Glaser, R. (1999) NMR and ESR studies of electric field distribution around biologically important molecules. Biophys. J 77, 443–454.

    Article  PubMed Central  PubMed  CAS  Google Scholar 

  • Marcus, R. A. and Sutin, N. (1985) Electron transfer in chemistry and biology. Biochim. Biophys. Acta 811, 625–632.

    Article  Google Scholar 

  • Marsh, D. (1989) Experimental methods in spin-label analysis. Biol. Magn. Reson 8, 255–285.

    Article  CAS  Google Scholar 

  • McElroy, J. D., Mauzerall, D. C., and Feher, G. (1974) Characterization of primary donor of bacterial photosynthesis.2. Kinetic studies of the light-induced ESR signal at g = 2.0026 and the optical absorbance at cryogenic temperatures. Biochim. Biophys. Acta 333, 261–272.

    Article  PubMed  CAS  Google Scholar 

  • Medzhidov, A. A., Likhtenshtein, G. I. and Kirichenko, L. A. (1969) Metallocomplexes with the paramagnetic ligands. Bull. Acad. Sci. USSR (Chemistry) N 3, 698–902.

    Google Scholar 

  • Michel, H. and Deisenhofer J. (1986) X-ray diffraction studies on a crystalline bacterial photosynthetic center. A progress report and conclusions on the structure of the photosystem II reaction center. In Encyclopedia of Plant Physiology, New Series, v.19, (Stachelin, L.A. and Arntzen, C.J (eds) pp. 371–381, Berlin, Springer-Verlag.

    Google Scholar 

  • More J. K., More K. M., Eaton G. R., and Eaton, S. S. (1990) Metal-nitroxyl interaction. 55: Manganase (III)-nitroxyl electron-electron spin-spin interaction. Pure Appl. Chem 62, 241–246.

    Article  CAS  Google Scholar 

  • Niccolai, N., Valensin, G., Rossi, C. and Gibbons, W. A. (1982) The stereochemistry and dynamics of natural products and biopolymers from proton relaxation spectroscopy: spin-label delineation of inner and outer protons of gramicidin S including hydrogen bonds. J. Am. Chem. Soc 104, 1534–1537.

    Article  CAS  Google Scholar 

  • Nicollai, N., Rossi, C., Valensin, G. Mascagni, P. and Gibbons, W. A. (1984) An investigation of the mechanisms of nitroxide-induced proton relaxation enhancements in biopolymers. J. Phys. Chem 88, 5689–5692.

    Article  Google Scholar 

  • Parmon, V. N., Kokorin, A. I., and Zhidomirov, G. M. (1980) Stable Biradicals, Nauka, Moscow.

    Google Scholar 

  • Perutz, M.F. (1989) Mechanisms of cooperativity and allosteric regulation in proteins. Quart. Rev. Biophys 22, 139–236.

    Article  CAS  Google Scholar 

  • Plachy, W. and Kivelson, D. (1967) Spin exchange in solution of di-tertiary-butyl nitroxide. J. Chem. Phys 47, 3312–3318.

    Article  CAS  Google Scholar 

  • Poulos, T. L., Finzel, B. C., Gunzalus, I. C., Wagner, G. C., and Kraut, J. (1985) The 2.6 A crystal structure of Pseudomonas putida cytochrome P-450. J. Biol. Chem 200, 16122–16130.

    Google Scholar 

  • Rich, P., Tiede, D.M, Bonner, W. D., Jr. (1979) Studies on the molecular organization of cytochromes P-450 and b5 in the microsomal membrane. Biochim. Biophys. Acta 546, 307–315.

    Article  PubMed  CAS  Google Scholar 

  • Safronov S. N., Mstislayskii V. I., Safronova U. I. and Muromtsev, V. I. (1969) Method of determination of relaxation times from saturation curves of the signals in the fast transmission conditions. Savodskaya Laboratoria 35, 1463–1465.

    Google Scholar 

  • Salikhov, K.M., Doctorov, A.B., Mohn, Yu.N., and Zamaraev, K.I. (1971) Spin relaxation of radicals and complexes upon encounters in solution J. Magn. Reson. 5, 189–196.

    CAS  Google Scholar 

  • Salikhov, K. M., Semenov, A. G., and Tsvetkov, Yu. D. (1976) Electron Spin Echo and Its Application. Nauka, Novosibirsk p. 342

    Google Scholar 

  • Sletten, E., Jackson, J. I., Burns, P. D. and La Mar, G. N. (1983) Effects of cross relaxation on the analysis of T1 data in paramagnetic proteins. J. Magn. Reson 52, 492–496.

    CAS  Google Scholar 

  • Solomon, J. and Bloembergen, N. (1956) Nuclear magnetic interaction in HF molecule. J. Chem. Phys, 25, 261–266.

    Article  CAS  Google Scholar 

  • Sundin, A. (1991) MacMimic version 2.1. InStar Software, Lund, Sweden.

    Google Scholar 

  • Syrtsova, L. A., Likhtenstein, G. I., Pisarkaya, T. N., Berdinskii, V. L., Lezina, V. P. and Stepanyants, A. U. (1974) Estimation of the distance between the ATPase and substrate-binding sites in nitrogenase by the NMR- H method. Mol. Biol. (Moscow) 8, 656–662.

    Google Scholar 

  • Taylor, J. C., Leigh, J. S. and Cohn, M. (1969) The effect of dipole-dipole interaction between nitroxide radical and a paramagnetic ion on the line shape of the ESR spectra of radical. Proc. Natl. Acad. Sci. USA 64, 219–206.

    Article  PubMed Central  PubMed  CAS  Google Scholar 

  • Tiede, D. M., Prince, R. C., Reed, G. H., and Dutton, P. L. (1976) EPR properties of the electron camer intermediate between the reaction center bacteriochlorophyls and the primary acceptor. FEBS Lett. 65, 301–304.

    Article  PubMed  CAS  Google Scholar 

  • Wien, R. W., Morriset, J. D. and McConnell, H. M. (1972) Spin-label induced nuclear relaxation. Distances between bound sacchat’ides, histidine-15, and tryptophan-123 on lysozyme in solution. Biochemistry 11, 3707–3716.

    Article  PubMed  CAS  Google Scholar 

  • Zamaraev K. I., Molin Yu. N., Salikhov K. M. (1977) Spin Exchange. Theory and Physicochemical Application, Nauka, Novosibirsk pp. 267–278.

    Google Scholar 

  • Zamaraev K. I., Mohn Yu. N., Salikhov K. M. (1981) Spin Exchange. Theory and Physicochemical Application Springer-Verlag.

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Editor information

Editors and Affiliations

Rights and permissions

Reprints and permissions

Copyright information

© 2002 Kluwer Academic / Plenum Publishers, New York

About this chapter

Cite this chapter

Likhtenshtein, G.I. (2002). Depth of Immersion of Paramagnetic Centers in Biological Systems. In: Berliner, L.J., Eaton, G.R., Eaton, S.S. (eds) Distance Measurements in Biological Systems by EPR. Biological Magnetic Resonance, vol 19. Springer, Boston, MA. https://doi.org/10.1007/0-306-47109-4_7

Download citation

  • DOI: https://doi.org/10.1007/0-306-47109-4_7

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4757-0575-1

  • Online ISBN: 978-0-306-47109-4

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics