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Electron Spin-Echo Envelope Modulation Studies Of 14N In Biological Systems

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Biomedical EPR, Part A: Free Radicals, Metals, Medicine, and Physiology

Part of the book series: Biological Magnetic Resonance ((BIMR,volume 23))

Abstract

Electron Spin-Echo Envelope Modulation Spectroscopy has provided great insight into the structure and function of many important biomolecules. Since its first application, this pulsed resonance technique has been found to be especially sensitive to those systems containing weak nuclear couplings. This chapter highlights representative Electron Spin-Echo Envelope Modulation investigations into protein systems containing paramagnetic transition ions and free radicals where geometric and electronic information was obtained through the detection and analysis of weak 14N coupling interactions.

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5. References

  • Ashby, C.I.H., Cheng, C.P., and Brown, T.L. (1978) 14N Nuclear Quadrupole Resonance Spectra of Coordinated Imidazole. J. Amer. Chem. Soc. 100, 6057–6063.

    CAS  Google Scholar 

  • Avigliano, L., Davis, J.L., Graziani, M.T., Marchesini Cherries, A., Mims, W.B., Mondovi, B., and Peisach, J. (1981) Electron Spin Echo Spectroscopic Studies of Type 1 and Type 2 Copper in Rhus Vernicifera and in Cucurbita Pepo Medullosa Ascorbate Oxidase. FEBS Letters 136, 80–84.

    Article  CAS  Google Scholar 

  • Baker, E.N., Blundell, F.R.S., T.L, Cutfield, J.F., Cutfield, S.M., Dodson, E.J., Dodson, G.G., Hodgkin, F.R.S., D.M.C., Hubbard, R.E., Issacs, N.W., Reynolds, C.D., Sakabe, K., Sakabe N., and Vijayan N.M. (1988) The Structure of 2Zn Pig Insulin Crystals at 1.5Ã… Resolution. Philos. Trans. R. Soc. London B319, 369–456.

    Google Scholar 

  • Baker, E.N. (1988) Structure of Azurin from Alicaligenes denitrificans. J. Mol. Biol. 203, 1071–1095.

    Article  CAS  PubMed  Google Scholar 

  • Bender, C.J. and Peisach, J. (1998) Electron Spin-Echo Modulation Spectroscopic Study Of The Type I Copper Center Associated With Stellacyanin from Rhus vernicifera. J. Chem. Soc. Faraday Trans. 94, 375–386.

    Article  CAS  Google Scholar 

  • Blumberg, W.E., Mims, W.B., and Zuckerman, D. (1973) Electron Spin Echo Envelope Spectrometry. Rev. Sci. Instruments 44, 546–554.

    Article  CAS  Google Scholar 

  • Brill, A.S. and Venable, Jr., J.H. (1968) The Binding of Transition Metal Ions in Insulin Crystals. J. Mol. Biol. 36, 343–353.

    Article  CAS  PubMed  Google Scholar 

  • Brill, A.S. and Venable, Jr., J.H. (1972) Water Co-ordination in Insulin. J. Mol. Biol. 66, 169–180.

    Article  CAS  PubMed  Google Scholar 

  • Burns, C.S., Aronoff-Spencer, E., Dunham, C.M., Lario, P., Avdievich, N.I., Antholine, W.E., Olmstead, M..M., Vrielink, A., Gerfen, G.J., Peisach, J., Scott, W.G., and Millhauser, G.L. (2002) Molecular Features of the Copper Binding Sites in the Octarepeat Domain of the Prion Protein. Biochemistry 41, 3991–4001.

    Article  CAS  PubMed  Google Scholar 

  • Cammack, R., Chapman, A., McCracken, J., Cornelius, J.B., Peisach, J., and Weiner, J.H. (1988) Electron Spin-Echo Spectroscopic Studies Of Eschericia Coli Fumarate Reductase. Biochim. et Biophys. Acta 956, 307–312.

    CAS  Google Scholar 

  • Cammack, R., Gay, E., and Shergill, J.K. (1999) Studies Of Hyperfine Interactions In [2Fe-2S] Proteins By EPR And Double Resonance Spectroscopy. Coordination Chemistry Reviews, 190–192, 1003–1022.

    Google Scholar 

  • Carrington, A. and McLachlan, A.D. (1967) Chapter 7, Introduction to Magnetic Resonance, Harper and Row, New York.

    Google Scholar 

  • Colaneri, M.J. and Peisach, J. (1992) An Electron Spin-Echo Envelope Modulation Study of Cu(II)-Doped Single Crystals of L-Histidine Hydrochloride Monohydrate. J. Amer. Chem. Soc. 114, 5335–5341.

    Article  CAS  Google Scholar 

  • Colaneri, M.J. and Peisach, J. (1995) A Single Crystal EPR and ESEEM Analysis of Cu(II)-Doped Bis(L-histidinato)cadmium Dihydrate. J. Amer. Chem. Soc. 117, 6308–6315.

    Article  CAS  Google Scholar 

  • Colaneri, M.J., Vitali, J., and Peisach, J. (2000) Electron Spin-Echo Envelope Modulation Study of Multicrystalline Cu2+-Insulin; Effects of Cd2+ on the Nuclear Quadrupole Interaction of the Cu2+-Coordinated Imidazole Remote Nitrogen. Biochemistry 39, 584–591.

    Article  CAS  PubMed  Google Scholar 

  • Coremans, J.W.A., Poluektov, O.G., Groenen, E.J.J., Canters, G.W., Nar, H., and Messerschmidt, A. (1996) A W-band Electron Nuclear Double Resonance Study of Single Crystals of 14N and 15N Azurin. J. Amer. Chem. Soc. 118, 12141–12153.

    Article  CAS  Google Scholar 

  • Coremans, J.W.A., Poluektov, O.G., Groenen, E.J.J., Canters, G.W., Nar, H., and Messerschmidt, A. (1997) A W-band Electron Spin Echo Envelope Modulation Study of a Single Crystal of Azurin. J. Amer. Chem. Soc. 119, 4726–4731.

    Article  CAS  Google Scholar 

  • Cornelius, J.B., McCracken, J., Clarkson, R.B., Belford, R.L., and Peisach, J. (1990) Electron Spin Echo Envelope Modulation Angle Selection Studies of Axial Pyridine Coordination to Copper(II) Benzoylacetonate. J. Phys. Chem. 94, 6977–6982.

    Article  CAS  Google Scholar 

  • Debus, R.J., Campbell, K.A, Gregor, W., Li, Z.L., Burnap, R.L., and Britt, R.D. (2001) Does histidine 332 of the D1 polypeptide ligate the manganese cluster in photosystem II? An electron spin echo envelope modulation study. Biochemistry 40, 3690–3699.

    Article  CAS  PubMed  Google Scholar 

  • Deligiannakis, Y., Louloudi, M., and Hadjiliadis, N. (2000) Electron Spin Echo Envelope Modulation (ESEEM) Spectroscopy As A Tool To Investigate The Coordination Environment Of Metal Centers. Coordination Chemistry Reviews, 204, 1–112.

    Article  CAS  Google Scholar 

  • DeRose, V.J., Kim, C.H., Newton, W.E., Dean, D.R., and Hoffman, B.M. (1995) Electron Spin Echo Envelope Modulation Spectroscopic Analysis of Altered Nitrogenase MoFe Proteins from Azotobacter vinelandii. Biochemistry 34, 2809–2814.

    Article  CAS  PubMed  Google Scholar 

  • Dikanov, S.A, and Tsvetkov, Y.D. eds., (1992) Electron Spin Echo Envelope Modulation (ESEEM) Spectroscopy, CRC Press, Boca Raton, Florida.

    Google Scholar 

  • Dikanov, S.A., Felli, I., Viezzoli, M-S., Spoyalov, A., and Hüttermann, J. (1994) X-Band ESEEM Spectroscopy Of 15N Substituted Native And Inhibitor-Bound Superoxide Dismutase. FEBS Letters 345, 55–60.

    Article  CAS  PubMed  Google Scholar 

  • Dikanov, S.A., Tyryshkin, A.M., Hüttermann, J., Bogumil, R., and Witzel, H. (1995) Characterization of Histidine Coordination in VO2+-Substituted D-Xylose Isomerase by Orientationally-Selected Electron Spin-Echo Envelope Modulation Spectroscopy. J. Amer. Chem. Soc. 117, 4976–4986

    CAS  Google Scholar 

  • Dikanov, S.A., Tyryshkin, A.M., Felli, I., Reijerse, E.J., and Hüttermann, J. (1995) C-band ESEEM of Strongly Coupled Peptide Nitrogens in Reduced Two-Iron Ferredoxin. J. Magn. Res. B108, 99–102.

    CAS  Google Scholar 

  • Eaton, S.S., Dubach, J., More, K.M., Eaton, G.R., Thurman, G., and Ambruso, D.R. (1989) Comparison of the Electron Spin Echo Envelope Modulation (ESEEM) for Human Lactoferrin and Transferrin Complexes of Copper(II) and Vanadyl Ion. J. Biol. Chem. 264, 4776–4781.

    CAS  PubMed  Google Scholar 

  • Eaton, S.S., Dubach, J., Thurman, G., and Ambruso, D.R. (1990) Electron Spin Echo Envelope Modulation (ESEEM) Evidence for Carbonate Binding to Iron(III) and Copper(II) Transferrin and Lactoferrin. J. Biol. Chem. 265, 7138–7141.

    CAS  PubMed  Google Scholar 

  • Einsle O., Tezcan F.A., Andrade S.L., Schmid B., Yoshida M., Howard J.B., and Rees D.C. Nitrogenase Mofe-Protein At 1.16 Ã… Resolution: A Central Ligand In The Femo-Cofactor. (2002) Science 297, 1696–1700.

    Article  CAS  PubMed  Google Scholar 

  • Gemberle, C., Aebli, G., Schweiger, A., and Ernst, R.R. (1990) Phase Cycling in pulse EPR. J. Magn. Res. 88, 241–244.

    Google Scholar 

  • Goldfarb, D., Fauth, J.-M., Farver, O., and Pecht, I. (1992) Orientation Selective ESEEM Studies on the Blue Oxidases Laccase and Ascorbate Oxidase. Appl.Magn.Reson. 3, 333–343.

    CAS  Google Scholar 

  • Hart, P.J., Nersissian, A.M., Herrmann, R.G., Nalbandyan, R.M., Valentine, J.S., and Eisenberg, D. (1996) A Missing Link In Cupredoxins: Crystal Structure Of Cucumber Stellacyanin At 1.6 Ã… Resolution. Protein Sci. 5, 2175–2183.

    CAS  PubMed  Google Scholar 

  • Hill, C.P., Dauter, Z., Dodson, E.J., Dodson, G.G., and Dunn, M.F. (1991) X-Ray Structure Of An Unusual Ca2+ Site And The Roles Of Zn2+ And Ca2+ In The Assembly, Stability, And Storage Of The Insulin Hexamer. Biochemistry 30, 917–924.

    CAS  PubMed  Google Scholar 

  • Höfer, P, Grupp, A., Nebenfuehr, H., and Mehring, M. Hyperfine Sublevel Correlation (HYSCORE) Spectroscopy, a 2D ESR investigation of the squaric acid radical. (1986) Chem. Phys. Lett. 132, 279–286.

    Google Scholar 

  • Hunt, M.J., Mackay, A.L., and Edmonds, D.T. (1975) Nuclear Quadrupole Resonance of 14N in Imidazole and Related Compounds. Chem. Phys. Lett. 34, 473–475.

    Article  CAS  Google Scholar 

  • Jiang, F., McCracken, J., and Peisach, J. (1990) Nuclear Quadrupole Interactions in Copper(II)-Diethylenetriamine-Substituted Imidazole Complexes and in Copper(II) Proteins. J. Amer. Chem. Soc. 112, 9035–9044.

    CAS  Google Scholar 

  • Ke, M. Torrent, D.G. Museav, K. Morokuma and K. Warncke (1999) Identification of Dimethylbenzimidazole Axial Coordination and Characterization of 14N Superhyperfine and Nuclear Quadrupole Coupling in Cob(II)alamin Bound to Ethanolamine Deaminase in a Catalytically-Engaged Substrate Radical-Cobalt(II) Biradical Site. Biochemistry 38, 12681–12689.

    Article  CAS  PubMed  Google Scholar 

  • Kevan, L. (1979) Modulation of Electron Spin-Echo Decay in Solids., Chapter 8 in Kevan, L. and Schwartz, R.N., eds., Time Domain Electron Spin Resonance, Wiley, New York.

    Google Scholar 

  • Kim, J. and Rees, D.C. (1992) Crystallographic Structure And Functional Implications Of The Nitrogenase Molybdenum-Iron Protein From Azotobacter Vinelandii. Nature 360, 553–560.

    CAS  Google Scholar 

  • Kosman, D.J., Peisach, J., and Mims, W.B. (1980) Pulsed Electron Paramagnetic Resonance Studies of the Copper(II) Site in Galactose Oxidase. Biochemistry 19, 1304–1308.

    Article  CAS  PubMed  Google Scholar 

  • Lee, H-I., Thrasher, K.S., Dean, D.R., Newton, W.E., and Hoffman, B.M. 14N Electron Spin-Echo Envelope Modulation of the S=3/2 Spin System of the Azotobacter vinelendii Nitrogenase Iron-Molybdenum Cofactor. (1998) Biochemistry 37, 13370–13378.

    CAS  PubMed  Google Scholar 

  • Lee, H-I., Benton, P.M.C., Laryukhin, M. Igarashi, R.Y., Dean, D.R., Seefeldt, L.C., and Hoffman, B.M. The Interstitial Atom of the Nitrogenase FeMo-Cofactor: ENDOR and ESEEM Show It Is Not an Exchangeable Nitrogen. (2003) J. Am. Chem. Soc. 125, 5604–5605.

    CAS  PubMed  Google Scholar 

  • Lee, H.C., Ikeda-Saito, M., Yonetani, T., Magliozzo, R.S., and Peisach, J. (1994) Hydrogen Bonding to the Bound Dioxygen in Oxy Cobaltous Myoglobin Reduces the Superhyperfine Coupling to the Proximal Histidine. Biochemistry 31, 7274–7281.

    Google Scholar 

  • Lee, H.C., Peisach, J., Dou, Y., and Ikeda-Saito, M. (1994) Electron-Nuclear Coupling to the Proximal Histidine in Oxy Cobalt-Substituted Distal Histidine Mutants of Human Myoglobin. Biochemistry 33, 7609–7618, 12000.

    CAS  PubMed  Google Scholar 

  • Lin, I-J., Gebel, E.B., Machonkin, T.E., Westler, W.M., and Markley, J.L. (2003) Correlation between Hydrogen Bond Lengths and Reduction Potentials in Clostridium pasteurianum Rubredoxin. J. Amer. Chem. Soc. 125, 1464–1465.

    CAS  Google Scholar 

  • LoBrutto, R., Haley, P.E., Yu, C.-A, Ohnishi, I., and Leigh, J.S. (1986) EPR and Electron Spin Echo Studies of Iron-Sulfur Clusters S-1 and S-2 in Beef Heart Succinate Dehydrogenase. Biophysical Journal 40, 327a.

    Google Scholar 

  • Lucken, E.A.C. (1969) Nuclear Quadrupole Coupling Constants, Academic Press, New York., pp.217–248.

    Google Scholar 

  • Magliozzo, R.S. and Peisach, J. (1993) Evaluation of Nitrogen Nuclear Hyperfine and Quadrupole Coupling Parameters for the Proximal Imidazole in Myoglobin-Azide,-Cyanide, and —Mecaptoethanol Complexes by Electron Spin Echo Envelope Modulation Spectroscopy. Biochemistry 32, 8446–8456.

    Article  CAS  PubMed  Google Scholar 

  • Messerschmidt, A., Rossi, A., Ladenstein, R., Huber, R., Bolognesi, M., Gatti, G., Marchesini, A., Petruzzelli, R., and Finazzi-Agro, A. (1989) X-ray Crystal Structure of the Blue Oxidase Ascorbate Oxidase from Zucchini. J. Mol. Biol. 206, 513–529.

    Article  CAS  PubMed  Google Scholar 

  • McCracken, J., Desai, P.R., Papadopoulos, N.J., Villafranca, J.J., and Peisach, J. (1988) Electron Spin-Echo Studies Of The Copper(II) Binding Sites In Dopamine B-Hydroxylase. Biochemistry 27, 4133–4137.

    Article  CAS  PubMed  Google Scholar 

  • McCracken, J., Peisach, J., and Dooley, D.M. (1987) Cu(II) Coordination Chemistry of Amine Oxidases: Pulsed EPR Studies of Histidine Imidazole, Water, and Exogenous Ligand Coordination. J. Amer. Chem. Soc. 109, 4064–4072.

    Article  CAS  Google Scholar 

  • Merks, R.P.J. and de Beer, R. (1980) Fourier Transform of the 133Cs Modulation of the Electron Spin-echo Envelope of Cs2ZnCl4:Cu2+J. Mag. Res. 37, 305–319.

    CAS  Google Scholar 

  • Mims, W.B. (1972) Electron Spin Echoes, Chapter 4 in Geschwind, S., ed., Electron Paramagnetic Resonance, Plenum Press, New York.

    Google Scholar 

  • Mims, W.B. (1972a) Envelope Modulation in Spin-Echo Experiments. Phys. Rev. B5, 2409–2418.

    Google Scholar 

  • Mims, W.B. (1972b) Amplitudes of Superhyperfine Frequencies Displayed in the Electron-Spin-Echo Envelope. Phys. Rev. B6, 3543–3545.

    Article  Google Scholar 

  • Mims, W.B. and Peisach, J. (1976) Assignment of a Ligand in Stellacyanin by a Pulsed Electron Paramagnetic Resonance Method. Biochemistry 15, 3863–3869.

    Article  CAS  PubMed  Google Scholar 

  • Mims, W.B. and Peisach, J. (1978) The Nuclear Modulation Effect In Electron Spin Echoes For Complexes Of Cu2+ And Imidazole With 14N And 15N J. Chem. Phys. 69, 4921–4930.

    Article  CAS  Google Scholar 

  • Mims, W.B. and Peisach, J. (1979) Measurement of 14N Superhyperfine Frequencies in Stellacyanin by an Electron Spin Echo Method. J. Biol. Chem. 254, 4321–4323.

    CAS  PubMed  Google Scholar 

  • Mims, W.B., Davis, J.L., and Peisach, J. (1984) The Accessibility of Type I Cu(II) Centers in Laccase, Azurin, and Stellacyanin to Exchangeable Hydrogen and Ambient Water. Biophys. J. 45, 755–766.

    CAS  PubMed  Google Scholar 

  • Mims, W.B. and Peisach, J. (1981) Electron Spin Echo Spectroscopy And The Study Of Metalloproteins, 213–263 In Berliner, L.J., Reuben, J., eds., Biological Magnetic Resonance, Plenum Press, New York.

    Google Scholar 

  • Peisach, J. and Blumberg, W.E. (1974) Structural Implications Derived from the Analysis of Electron Paramagnetic Resonance Spectra of Natural and Artificial Copper Proteins. Arch. Biochem. Biophys. 165, 691–708.

    Article  CAS  PubMed  Google Scholar 

  • Peisach, J. (1995) ESEEM Spectroscopy — Probing Active Site Structures Of Metalloproteins. In Oliva-Nishiguchi, H., Packer, L., eds., Bioradicals Detected by ESR Spectroscopy, Birkhauser Verlag, Basil, Switzerland.

    Google Scholar 

  • Peisach, J. (2003) An Appreciation of William H. Orme-Johnson III. J. Inorg. Biochem. 93. 6–10.

    Article  CAS  PubMed  Google Scholar 

  • Reijerse, E.J. and Keijers, C.P. (1987) Model Calculations Of Frequency Domain ESEEM Spectra Of Disordered Systems. J. Magn. Res. 71, 83–88.

    CAS  Google Scholar 

  • Reijerse, E.J. and Dikanov, S.A. (1991) Electron Spin Echo Envelope Modulation Spectroscopy on Orientationally Disordered Systems — LineShape Singularities in S=1/2, 1=1/2 Spin Systems. J. Chem. Phys. 95, 836–845.

    Article  CAS  Google Scholar 

  • Rowan L.G., Hahn, E.L., and Mims, W.B. (1965) Electron-Spin-Echo Envelope Modulation. Physical Review 137, A61–71.

    Article  Google Scholar 

  • Singh, V., Zhu, Z., Davidson, V.L., and McCracken, J. (2000) Characterization of the Tryptophan Tryptophyl-Semiquinone Catalytic Intermediate of Methylamine Dehydrogenase by Electron Spin-Echo Envelope Modulation Spectroscopy. J. Amer. Chem. Soc. 122, 931–938.

    Article  CAS  Google Scholar 

  • Thomann, H., Bernardo, M., Newton, W.E., and Dean, D.R. (1991) N Coordination of FeMo Cofactor Requires His-195 of the MoFe Protein α Subunit and is Essential for Biological Nitrogen Fixation. Proc. Natl. Acad. Sci. U.S.A. 88, 6620–6623.

    CAS  PubMed  Google Scholar 

  • Tipton, P.A., McCracken, J., Cornelius, J.B., and Peisach, J. (1989) Electron Spin Echo Envelope Modulation Studies of Pyruvate Kinase Active-Site Complexes. Biochemistry, 28, 5720–5728.

    Article  CAS  PubMed  Google Scholar 

  • Townes, C.H. and Dailey, B.P. (1949) Determination of Electronic Structure of Molecules from Nuclear Quadrupole Effects. J. Chem. Phys. 17, 782–796.

    Article  CAS  Google Scholar 

  • Warncke, K, Brooks, H.B., Babcock, G.T., Davidson, V.L., and McCracken, J. (1993) The Nitrogen Atom of Substrate Methylamine is Incorporated into the Tryptophan Tryptophyl-Semiquinone Catalytic Intermediate in Methylamine Dehydrogenase. J. Amer. Chem. Soc. 115, 6464–6465.

    Article  CAS  Google Scholar 

  • Warncke, K, Babcock, G.T., McGuirl, M.A., Dooley, D.M., and McCracken, J. (1994) Structure of the Topa-semiquinone Catalytic Intermediate of Amine Oxidase as Revealed by Magnetic Interactions with Exchangeable 2H and 1H Nuclei. J. Amer. Chem. Soc. 116, 4028–4037.

    CAS  Google Scholar 

  • Willer, M., Granwehr, J., Forrer, J., and Schweiger, A. (1998) Two-Dimensional Nuclear-Zeeman-Resolved Electron Spin Echo Envelope Modulation (NZ-ESEEM) Spectroscopy. J. Magn. Reson. 133, 46–52.

    Article  CAS  PubMed  Google Scholar 

  • Zhang, C., Markham, G.D., and LoBrutto, R. (1993) Coordination of Vanadyl(IV) Cation in Complexes of S-Adenosylmethionine Synthetase: Multifrequency Electron Spin Echo Envelope Modulation Study. Biochemistry 32, 9866–9873.

    CAS  PubMed  Google Scholar 

  • Zweier, J., Aisen, P., Peisach, J., and Mims, W.B. (1979) Pulsed Electron Paramagnetic Resonance Studies of the Copper Complexes of Transferrin. J. Biol. Chem. 254, 3512–3515.

    CAS  PubMed  Google Scholar 

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Authors and Affiliations

  1. Department of Chemistry and Physics, State University of New York, Old Westbury, New York, 11568

    Michael J. Colaneri

  2. Department of Physiology and Biophysics, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, New York, 10461

    Michael J. Colaneri & Jack Peisach

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  1. University of Denver, Denver, Colorado

    Sandra R. Eaton , Gareth R. Eaton  & Lawrence J. Berliner ,  & 

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Dedicated to the memory of Professor Larry Kevan, 1938 – 2002.

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Colaneri, M.J., Peisach, J. (2005). Electron Spin-Echo Envelope Modulation Studies Of 14N In Biological Systems. In: Eaton, S.R., Eaton, G.R., Berliner, L.J. (eds) Biomedical EPR, Part A: Free Radicals, Metals, Medicine, and Physiology. Biological Magnetic Resonance, vol 23. Springer, Boston, MA. https://doi.org/10.1007/0-387-26741-7_15

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