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Distance Measurements by CW and Pulsed EPR

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Distance Measurements in Biological Systems by EPR

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

Abstract

Distances between unpaired electrons ranging from ca. 5 Å to > 70 Å can be measured by a combination of continuous wave (CW) and pulsed electron paramagnetic resonance (EPR) techniques. An overview of these techniques is provided as an introduction to the volume.

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References

  • Abeles, T. P. and Bos, W. G. (1967). A Dimensional Analysis of Magnetic Susceptibility Calculations. J. Chem. Ed. 44, 438–441.

    CAS  Google Scholar 

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

    Google Scholar 

  • Akita, T., Mazaki, Y., and Kobayashi, K. (1995). Ferromagnetic Spin Interaction in a Crystalline Molecular Complex Formed by Inter-heteromolecule Hydrogen Bonding: a 1:1 Complex of Phenyl Nitronyl Nitroxide Radical and Phenylboronic Acid. J. Chem. Soc. Chem. Commun. 1861–1862.

    Google Scholar 

  • Altenbach, C., Flitsch, S. L., Khorana, H. G., and Hubbell, W. L. (1989). Structural Studies on Transmembrane Proteins. 2. Spin Labeling of Bacteriorhodopsin Mutants at Unique Cysteines. Biochemistry 28, 7806–7812.

    PubMed  CAS  Google Scholar 

  • Anderson, D. J., Hanson, P., McNulty, J., Millhauser, G., Monaco, V., Formaggio, F., Crisma, M., and Tomolo, C. (1999). Solution Structures of TOAC-Labeled Trichogin GA IV Peptides from Allowed (g ≈ 2) and Half-Field Electron Spin Resonance. J. Am. Chem. Soc. 121, 6919–6927.

    CAS  Google Scholar 

  • Arcangeli, C., Bizzarri, A. R., and Cannistraro, S. (1998). Role of interfacial water in the molecular dynamics-simulated dynamical transition of plastocyanin. Chem. Phys. Lett. 291, 7–14.

    CAS  Google Scholar 

  • Astashkin, A. V., Hara, H., and Kawamori, A. (1998) The pulsed electron-electron double resonance and “2+1” electron spin echo study of the oriented oxygen-evolving and Mn-depleted preparations of photosystem II. J. Chem. Phys. 108, 3805–3812.

    CAS  Google Scholar 

  • Banci, L., Bertini, I., Huber, J. G., Luchinat, C. and Rosato, A. (1998). Partial Orientation of Oxidized and Reduced Cytochrome b5 at High Magnetic Fields: Magnetic Susceptibility Anisotropy Contributions and Consequences for Protein Solution Structure Determination. J. Am. Chem. Soc. 120, 12903–12909.

    CAS  Google Scholar 

  • Bertini, I., Molinari, H., and Niccolai, N., eds. (1991). NMR and Biomolecular Structure, VCH Publisher, Weinheim.

    Google Scholar 

  • Bizzarri A. R. and Cannistraro, S. (1999). Molecular dynamics simulation of plastocyanin potential energy fluctuations: 1/f noise. Physica A 267, 257–270.

    CAS  Google Scholar 

  • Bohr, H. and Bnmak, S., eds. (1996). Protein Folds. A Distance-Based Approach. CRC Press, Boca Raton, Florida.

    Google Scholar 

  • Borbat, P. P. and Freed, J. H. (1999). Multi-quantum ESR and Distance Measurements. Chem. Phys. Lett. 313, 145–154.

    CAS  Google Scholar 

  • Brooks, C. L. III, Karplus, M., and Pettitt, B. M., eds. (1988). Proteins: A Theoretical Perspective of Dynamics, Structure, and Thermodynamics. Advances in Chemical Physics, Vol. 71.

    Google Scholar 

  • Buck, M. and Karplus, M. (1999). Internal and Overall Peptide Group Motions in Proteins: Molecular Dynamics Simulations for Lysozyme Compared with Results from X-ray and NMR Spectroscopy. J. Am. Chem. Soc. 121, 9645–9658.

    CAS  Google Scholar 

  • Burchfield, J., Telehowski, P., Rosenberg, R. C., Eaton, S. S., and Eaton, G. R. (1994). A Neutral Water-Soluble Broadening Agent for Spin Label Studies, J. Magn. Reson. B104, 69–72.

    CAS  Google Scholar 

  • Case, G. D. and Leigh, J. S., Jr., (1976). Intramitochondrial Positions of Cytochrome Haem Groups Determined by Dipolar Interactions with Paramagnetic Cations. Biochem. J. 160, 769–783.

    PubMed Central  PubMed  CAS  Google Scholar 

  • Chadhuri, P., Oder, K., Wieghardt, K., Gehring, S., Haase, W., Nuber, B., and Weiss, J. (1988). Moderately Strong Intramolecular Magnetic Exchange Interaction between the Copper(II) Ions Separated by 11.25 Å in [L2Cu2(μ-terephthalato)](C1O4)2 (L = 1,4,7-Trimethyl-1,4,7-triazacyclononane). J. Am. Chem. Soc. 110, 3657–3658.

    Google Scholar 

  • Coffman, R. E. and Buettner, G. R. (1979). A Limit Function for Long-Range Ferromagnetic and Antiferromagnetic Superexchange. J. Phys. Chem. 83, 2387–2392.

    CAS  Google Scholar 

  • Coffman, R. E. and Pezeshk, A. (1986a). Analytical Consideration of Eatons’ Formula for the Interspin Distance between Unpaired Electrons in ESR. J. Magn. Reson. 70, 21–33.

    CAS  Google Scholar 

  • Dalal, D. P., Damoder, R., Eaton, G. R., and Eaton, S. S. (1985a). Estimates of Collision Frequencies and Solvent Effects in Collision Interactions. J. Magn. Reson. 63, 327–332.

    CAS  Google Scholar 

  • Dalal, D. P., Damoder, R., Benner, C., Eaton, G. R., and Eaton, S. S. (1985b). Metal-Nitroxyl Interactions. 44. Collision Interactions Between Transition Metal Complexes and Nitroxyl Radicals in Aqueous Solution. J. Magn. Reson. 63, 125–132.

    CAS  Google Scholar 

  • Damoder, R., More, K. M., Eaton, G. R., and Eaton, S. S. (1983). Metal-Nitroxyl Interactions. 30. Single Crystal EPR Spectra of Two Spin-Labeled Copper Porphyrins. J. Amer. Chem. Soc. 105, 2147–2154.

    CAS  Google Scholar 

  • Diehl, M., Doster, W., Petry, W., and Schober, H. (1997). Water-Coupled Low-Frequency Modes of Myoglobin and Lysozyme Observed by Inelastic Neutron Scattering. Biophys. J. 73, 2726–2732.

    PubMed Central  PubMed  CAS  Google Scholar 

  • Dikanov, S. A. and Tsvetkov, Yu. D. (1992) Electron Spin Echo Envelope Modulation Spectroscopy, CRC Press, Boca Raton, FL.

    Google Scholar 

  • Dzuba, S. A., Kodera, Y., Hara, H., and Kawamori, A. (1993). The Use of Selective Hole Burning in EPR Spectra to Study Spectral Diffusion and Dipolar Broadening. J. Magn. Reson. A 102, 257–260.

    CAS  Google Scholar 

  • Dzuba, S. A. and Kawamori, A. (1996). Selective Hole Burning EPR: Spectral Diffusion and Dipolar Broadening. Concepts in Magnetic Resonance 8, 49–61.

    CAS  Google Scholar 

  • Eaton, S. S. and Eaton, G. R. (1978). Interaction of Spin Labels with Transition Metals. Coord. Chem. Rev. 26, 207–262.

    CAS  Google Scholar 

  • Eaton, S. S. and Eaton, G. R. (1982). Measurement of Spin-Spin Distances from the Intensity of the EPR Half-Field Transition. J. Am. Chem. Soc. 104, 5002–5003.

    CAS  Google Scholar 

  • Eaton, S. S. and Eaton, G. R. (1988a). Interaction of Spin Labels with Transition Metals. Part 2. Coord. Chem. Rev. 83, 29–72.

    CAS  Google Scholar 

  • Eaton, G. R. and Eaton, S. S. (1988b). EPR Studies of Long-Range Intramolecular Electron-Electron Exchange Interaction. Acct. Chem. Res. 21, 107–113.

    CAS  Google Scholar 

  • Eaton, G. R. and Eaton, S. S. (1989). Resolved Electron-Electron Spin-Spin Splitting in EPR Spectra. Biol. Magn. Reson. 8, 339–397.

    CAS  Google Scholar 

  • Eaton, G. R. and Eaton, S. S. (1996). Determination of Electron-Electron Interspin Distance by Electron Spin Echo and Saturation Recovery Electron Paramagnetic Resonance. Current Topics in Biophysics 20, 5–8.

    CAS  Google Scholar 

  • Eaton, S. S., Law, M. L., Peterson, J., Eaton, G. R., and Greenslade, D. J. (1979). MetalNitroxyl Interactions. 7. Quantitative Aspects of EPR Spectra Resulting from Dipolar Interactions. J. Magn. Reson. 33, 135–141.

    CAS  Google Scholar 

  • Eaton, S. S., More, K. M., Sawant, B. M., and Eaton, G. R. (1983). Use of the Half-Field Transition to Determine the Interspin Distance and the Orientation of the Interspin Vector in Systems with two Unpaired Electrons. J. Amer. Chem. Soc. 105, 6560–6567.

    CAS  Google Scholar 

  • Eischenbroich, Ch., Schiemann, O., Burghaus, O., and Harms, K. (1997). Exchange Interaction Mediated by O-HO Bonds: Synthesis, Structure, and EPR Study of the Paramagnetic Organometallic Carboxylic Acid (η7-C7H7)V(η5-C5H4COOH). J. Am. Chem. Soc. 119, 7452–7457.

    Google Scholar 

  • Fielding, L., More, K. M., Eaton, G. R., and Eaton, S. S. (1986). Metal-Nitroxyl Interactions. 51. Collapse of Iron-Nitroxyl Electron-Electron Spin-Spin Splitting Due to the Increase in the Electron Spin Relaxation Rate for High-Spin Iron(III) When Temperature is Increased. J. Am. Chem. Soc. 108, 8194–8196.

    CAS  Google Scholar 

  • Goodson, P. A., Glerup, J., Hodgson, D. J., Michelsen, K., and Rychlewska, U. (1994). Magnetic Exchange through Hydrogen Bonds: Structural and Magnetic Characterization of cis-Hydroxoaquachromium(III) Complexes of Tetradentate and Monodentate Ligands. Inorg. Chem. 33, 359–366.

    CAS  Google Scholar 

  • Goslar, J., Piekara-Sady, L., and Kispert, L. D. (1994). ENDOR Data Tabulations, Ch. VI in Handbook of Electron Spin Resonance, Vol. 1, C. P. Poole, Jr., and H. A. Farach, eds., ALP Press, American Institute of Physics, New York.

    Google Scholar 

  • Grupp, A., and Mehring, M. (1990). Pulsed ENDOR Spectroscopy in Solids, Ch. 4 in Modern Pulsed and Continuous-Wave Electron Spin Resonance. L. Kevan and M. K. Bowman, eds., Wiley, New York.

    Google Scholar 

  • Hamachi, I., Yamada, Y., Matsugi, T., Shinkai, S. (1999) Single-or dual-mode switching of semisynthetic ribonuclease S’ with an iminodiacetic acid moiety in response to the copper(II) concentration. Chem. Eur. J. 5, 1503–1511.

    CAS  Google Scholar 

  • Hara, H. and Kawamori, A. (1997). A Selective Hole Burning Method Applied to Determine Distances between Paramagnetic Species in Photosystems. Appl. Magn. Reson. 13, 241–257.

    CAS  Google Scholar 

  • Hdkansson, K., Carlsson, U., Svensson, M., and Liljas, A. (1992). Structure of native and apo carbonic anhydarse II and structure of some of its anion-ligand complexes. J. Mol. Biol. 277, 1192–1204.

    Google Scholar 

  • He, M. M., Voss, J., Hubbell, W. L., and Kaback, H. R. (1995a). Use of Designed Metal-Binding Sites to Study Helix Proximity in the Lactose Pennease of Escherichia coli. 1. Proximity of Helix VII (Asp237 and Asp240) with Helices X (Lys319) and XI (Lys358). Biochemistry 34, 15661–15666.

    PubMed  CAS  Google Scholar 

  • He, M. M., Voss, J., Hubbell, W. L., and Kaback, H. R. (1995b). Use of Designed Metal-Binding Sites to Study Helix Proximity in the Lactose Permesse of Escherichia coli. 2. Proximity of Helix IX (Arg302) with Helix X (His322 and G1u325). Biochemistry 34, 15667–15670.

    PubMed  CAS  Google Scholar 

  • Hellinga, H. W. (1996). Design of Metalloproteins, in Protein Engineering, Principles and Practice, J. L. Cleland and C. S. Craik, eds., Wiley-Liss, pp. 369–398.

    Google Scholar 

  • Hubbell, W. L., Fross, A., Langren, R., and Lietzow, M. A. (1998). Recent advances in site-directed spin labeling of proteins. Curr. Opinion Struct. Biol. 8, 649–656.

    CAS  Google Scholar 

  • Hustedt, E. J., Smimov, A. I., Laub, C. F., Cobb, C. E., and Beth, A. H. (1997). Molecular Distances from Dipolar Coupled Spin-Labels: The Global Analysis of Multifrequency Continuous Wave Electron Paramagnetic Resonance Data. Biophys. J. 72, 1861–1877.

    PubMed Central  PubMed  CAS  Google Scholar 

  • Hyde, J. S., Swartz, H. M., and Antholine, W. E. (1979). The Spin-Probe-Spin Label Method. Ch. 2 in Spin Labeling II: Theory and Applications. L. J. Berliner, ed., Academic Press, New York.

    Google Scholar 

  • Jung, K., Voss, J., He., M., Hubbell, W. L., and Kaback, H. R. (1995). Engineering a Metal Binding Site within a Polytopic Membrane Protein, the Lactose Permesse of Escherichia coli. Biochem. 34, 6272–6277.

    Google Scholar 

  • Kodera, Y., Dzuba, S. A., Hara, H., Kawamori, A. (1994). Distances from tyrosine D’ to the manganese cluster and the acceptor iron in Photosystem II as determined by selective hole burning in EPR spectra. Biochim. Biophys. Acta 1186, 91–99.

    CAS  Google Scholar 

  • Kokorin, A. I., Zamarayev, K. I., Grigoryan, G. L., Ivanov, V. P., and Rozantsev, E. G. (1972). Measurement of the Distances between the Paramagnetic Centres in Solid Solutions of Nitroxide Radicals, Biradicals, and Spin-Labeled Proteins. Biofizika 17, 34–41 (p. 31–39 in transl.)

    Google Scholar 

  • Kokorin, A. I., and Formazyuk, V. E. (1981). New Method of Measuring Distances Between Spin Label and Paramagnetic Ions in Macromolecules. Molek Biol. 15, 930–938 (p. 722–728 in transl.)

    CAS  Google Scholar 

  • Koteiche, H. A., Berengian, A. R., and Mchaourab, H. S. (1998). Identification of Protein Folding Patterns Using Site-Directed Spin Labeling. Structural Characterization of a Sheet and Putative Substrate Binding Regions in the Conserved Domain of aA-Crystallin. Biochem. 37, 12681–12688.

    CAS  Google Scholar 

  • Kuo, L. C., Fukuyama, J. M., and Mahnen, M. W. (1983). Catalytic Conformation of Carboxypeptidase A. The Structure of a True Reaction Intermediate Stabilized at Subzero Temperatures. J. Mol. Biol. 163, 63–105.

    PubMed  CAS  Google Scholar 

  • Kurshev, V. V., Raitsimring, A. M., and Salikhov, K. M. (1988). Angular dependence of the dipole broadening function of the ESR line of single crystals containing paramagnetic centers with an anisotropic g tensor: Era+ in CaWO4. Sov. Phys. Solid State 30, 239–242.

    Google Scholar 

  • Kurshev, V. M., Raitsimring, A. M., and Tsvetkov, Yu. D. (1989). Selection of Dipolar Interaction by the “2+1” Pulse Train ESE. J. Magn. Reson. 81, 441–454.

    CAS  Google Scholar 

  • Langen, R., Oh, K. J., Cascio, D., and Hubbell, W. L. (2000) Crystal Structure of Spin Labeled T4 Lysozyme Mutants: Implications for the Interpretation of EPR Spectra in Terms of Structure. Biochemistry 39, 8396–8405.

    PubMed  CAS  Google Scholar 

  • Leigh, J. S., Jr. (1970). ESR Rigid-Limit Line Shape in a System of Two Interacting Spins. J. Chem. Phys. 52, 2608–2612.

    CAS  Google Scholar 

  • Likhtenshtein, G. I. (1976). Spin Labeling Methods in Molecular Biology, Wiley, New York.

    Google Scholar 

  • Lu, Y. and Valentine, J. S. (1997). Engineering metal-binding sites in proteins. Curr. Opin. Struct. Biol. 7, 495–500.

    PubMed  CAS  Google Scholar 

  • Luckhurst, G. R. (1976) Biradicals as Spin Probes, Spin Labeling: Theory and Applications, L. J. Berliner, ed., Academic Press, N. Y., ch. 4.

    Google Scholar 

  • Mahnen, M. W. and Kuo, L. C. (1983) Spin-Label Probes of Enzyme Action, Magn. Reson. Biol. 2, 53–94.

    Google Scholar 

  • Maret, W. (1993). Detecting Metal-Metal Interactions and Measuring Distances between Metal Centers in Metalloproteins. Methods Enzymol. 226, 594–618.

    PubMed  CAS  Google Scholar 

  • Martin, R. E., Pannier, M., Diederich, F., Gramlich, V., Hubrich, M., and Spiess, H. W. (1998). Determination of End-to-End Distances in a Series of TEMPO Diradicals of up to 2.8 nm Length with a New Four-Pulse Double Electron Electron Resonance Experiment. Angew. Chem. 37, 2834–2837.

    CAS  Google Scholar 

  • Maryasov, A. G., Tsvetkov, Y. D., and Raap, J. (1998). Weakly Coupled Radical Pairs in Solids: ELDOR in ESE Structure Studies. Appl. Magn. Reson. 14, 101–113.

    CAS  Google Scholar 

  • McCracken, J. (1999) Electron Spin Echo Envelope Modulation, Ch. V in Handbook of Electron Spin Resonance, Vol. 2, C. P. Poole, Jr., and H. A. Farach, eds., AIP Press, Springer-Verlag, New York.

    Google Scholar 

  • Mchaourab, H. S., Berengian, A. R., and Koteiche, H. A. (1997). Site-Directed Spin-Labeling Study of the Structure and Subunit Interactions along a Conserved Sequence in the aCrystallin Domain of Heat-Shock Protein 27. Evidence of a Conserved Subunit Interface. Biochem. 36, 14627–14634.

    CAS  Google Scholar 

  • Milov, A. D., Salikhov, K. M., and Shchirov, M. D. (1981). Application of the double resonance method to electron spin echo in a study of the spatial distribution of paramagnetic centers in solids. Soy. Phys. Solid State 23, 565–569.

    Google Scholar 

  • Milov A. D., and Tsvetkov, Yu. D. (1997). Double Electron-Electron Resonance in Electron Spin Echo: Conformations of Spin-Labeled Poly-4-Vinylpyridine in Glassy Solutions. Appl. Magn. Reson. 12, 495–504.

    CAS  Google Scholar 

  • Milov, A. D., Maryasov, A. G., and Tsvetkov, Y. D. (1998). Pulsed Electron Double Resonance (PELDOR) and Its Applications in Free Radicals Research. Appl. Magn. Reson. 15, 107–143.

    CAS  Google Scholar 

  • Milov, A. D., Maryasov, A. G., Tvestkov, Yu. D., and Raap, J. (1999). Pulsed ELDOR in spin-labeled polypeptides. Chem. Phys. Lett. 303, 135–143.

    CAS  Google Scholar 

  • Minis, W. B. and Peisach, J. (1981). Electron spin echo spectroscopy and the study of metalloproteins, Biol. Magn. Reson. 3, 213–263.

    Google Scholar 

  • More, K. M., Eaton, G. R., and Eaton, S. S. (1982). Metal-Nitroxyl Interactions. 25. Exchange Interactions via Saturated Linkages in Spin Labeled Porphyrins. Can. J. Chem. 25, 1392–1401.

    Google Scholar 

  • More, J. K., More, K. M., Eaton, G. R., and Eaton, S. S. (1984). Metal-Nitroxyl Interactions. 39. Electron-Electron Spin-Spin Splitting in the EPR Spectra of Nitroxyl Spin-Labeled Mn(II) Complexes in Fluid Solution. J. Amer. Chem. Soc. 106, 5395–5402.

    CAS  Google Scholar 

  • More, K. M., Eaton, G. R., and Eaton, S. S. (1985). Metal-Nitroxyl Interactions. 42. Spin-Spin Interaction in Frozen Solution EPR Spectra of Spin-Labeled Mn(II) Complexes. J. Magn. Reson. 63, 151–167.

    CAS  Google Scholar 

  • Morris, A. T. and Dwek, R. A. (1977). Some Recent Applications of the Use of Paramagnetic Centers to Probe Biological Systems Using Nuclear Magnetic Resonance. Quart. Rev. Biophys. 10, 421–484.

    CAS  Google Scholar 

  • Niimura, N. (1999). Neutrons expand the field of structural biology. Curr. Opin. Struct. Biol. 9, 602–608.

    PubMed  CAS  Google Scholar 

  • Pake, G. E. and Estle, T. L. (1973). The Physical Principles of Electron Paramagnetic Resonance, 2nd Ed., W. A. Benjamin, Inc., Reading, Mass. See pages 157ff.

    Google Scholar 

  • Pannier, M., Veit, S., Godt, A., Jeschke, G., and Spiess, H. W. (2000). Dead-time Free Measurement of Dipole-Dipole Interactions between Electron Spins, J. Magn. Reson. 142, 331–340.

    PubMed  CAS  Google Scholar 

  • Persson, M., Harbridge, J. R., Hammarström, P., Mitri, R., Mdrtensson, L.-G., Carlsson, U., Eaton, G. R., and Eaton, S. S. (2000). Comparison of EPR Methods to Determine Distances between Spin Labels on Human Carbonic Anhydrase II, submitted for publication.

    Google Scholar 

  • Piekara-Sady, L., and Kispert, L. D. (1994). ENDOR Spectroscopy, Ch. V in Handbook of Electron Spin Resonance, Vol. 1, C. P. Poole, Jr., and H. A. Farach, eds., AIP Press, American Institute of Physics, New York.

    Google Scholar 

  • Postnikova, G. B. (1996). Spin-Label Studies of the Conformational Properties of Herne Proteins: a Review. Biochemistry (Moscow) 61, 679–693.

    Google Scholar 

  • Prestegard, J., Tolman, J. R., Al-Hashimi, H. M., and Andrec, M. (1999). Protein Structure and Dynamics from Field-Induced Residual Dipolar Coupings. Biol. Magn. Reson. 17, in press.

    Google Scholar 

  • Rabenstein, M. D. and Shin, Y.-K. (1995). Determination of the distance between two spin labels attached to a macromolecule. Proc. Natl. Acad. Sci. U.S. 92, 8239–8243.

    CAS  Google Scholar 

  • Raitsimring, A., Peisach, J., Lee, H. C., and Chen, X. (1992). Measurement of Distance Distributions between Spin Labels in Spin-Labeled Hemoglobin Using an Electron Spin Echo Method. J. Phys. Chem. 96, 3526–3531.

    CAS  Google Scholar 

  • Rakowsky, M. H., More, K. M., Kulikov, A. V., Eaton, G. R., and Eaton, S. S. (1995). Time-Domain Electron Paramagnetic Resonance as a Probe of Electron-Electron Spin-Spin Interaction in Spin-Labeled Iron Porphyrins. J. Amer. Chem. Soc. 117, 2049–2057.

    CAS  Google Scholar 

  • Read, R. J. and Wemmer, D. E. (1999). Biophysical Methods–Bigger, better, faster, and automatically too? Editorial overview. Curr. Opin. Struct. Biol. 9, 591–593.

    CAS  Google Scholar 

  • Reed, C. A. and Orosz, R. D. (1993). Spin Coupling Concepts in Bioinorganic Chemistry. in Research Frontiers in Magnetochemistry. C. J. O’Connor, ed., World Scientific, Singapore.

    Google Scholar 

  • Regan, L. (1993). The design of metal-binding sites in proteins. Ann. Rev. Biophys. Biomol. Struct. 22, 257–281.

    CAS  Google Scholar 

  • Salikhov, K. M., Kandrashkin, Yu. E., and Salikhov, A. K. (1992). Peculiarities of free induction and primary spin echo signals for spin-correlated radical pairs, Appl. Magn. Reson. 3, 199–217.

    CAS  Google Scholar 

  • Saxena, S. and Freed, J. H. (1996). Double quantum two-dimensional Fourier transform electron spin resonance: distance measurements. Chem. Phys. Lett. 251, 102–110.

    CAS  Google Scholar 

  • Saxena, S. and Freed, J. H. (1997). Theory of double quantum two-dimensional electron spin resonance with application to distance measurements. J. Chem. Phys. 107, 1317–1340.

    CAS  Google Scholar 

  • Schlichter, J., Friedrich, J., Herenyi, L., and Fidy, J. (2000). Protein dynamics at low temperatures. J. Chem. Phys. 112, 3045–3050.

    CAS  Google Scholar 

  • Shigemori, K., Hara, H., Kawamori, A., and Akabori, K. (1998). Determination of distances from tyrosine to D and QA and chlorophyllz in photosystem II studied by ‘2+1’ pulsed EPR. Biochim. Biophys. Acta 1363, 187–198.

    PubMed  CAS  Google Scholar 

  • Sigel, H. and Sigel, A. (1994). Metal Ions in Biological Systems, Vol. 30, Metalloenzymes Involving Amino Acid-Residue and Related Radicals. Marcel Dekker, New York.

    Google Scholar 

  • Sigel, H. and Sigel, A. (1999). Metal Ions in Biological Systems, Vol. 36, Interelations Between Free Radicals and Metal Ions in Life Processes. Marcel Dekker, New York.

    Google Scholar 

  • Steinhoff, H.-J., Radzwill, N., Thevis, W., Lenz, V., Brandenburg, D., Antson, A., Dodson, G., and Wolimer, A. (1997) Determination of Interspin Distances between Spin Labels Attached to Insulin: Comparison of Electron Paramagnetic Resonance Data with the X-Ray Structure. Biophys. J. 73, 3287–3298.

    PubMed Central  PubMed  CAS  Google Scholar 

  • Stowell, M. H. B., Miyazawa, A., and Unwin, N. (1998). Macromolecular structure determination by electron microscopy: new advances and recent results. Curr. Opin. Struct. Biol. 8, 595–600.

    PubMed  CAS  Google Scholar 

  • Sun, J., Voss, J., Hubbell, W. L., and Kaback, H. R. (1999). Proximity between Periplasmic Loops in the Lactose Permease of Escherichia coli as Determined by Site Directed Spin Labeling. Biochem. 38, 3100–3105.

    CAS  Google Scholar 

  • Tang, J., Thurnauer, M. C., and Norris, J. R. (1994). Electron spin echo envelope modulation due to exchange and dipolar interactions in a spin-correlated radical pair. Chem. Phys. Lett. 219, 283–290.

    CAS  Google Scholar 

  • Tarek, M. and Tobias, D. J. (1999). Environmental Dependence of the Dynamics of Protein Hydration Water. J. Am. Chem. Soc. 121, 9740–9741.

    CAS  Google Scholar 

  • Thomson, C. (1968). Electron Spin Resonance Studies of the Triplet State. Q. Rev. Phys. Soc. 22, 45–74.

    CAS  Google Scholar 

  • Voss, J., Salwinski, L., Kaback, H. R., and Hubbell, W. L. (1995a). A method for distance determination in proteins using a designed metal ion binding site and site-directed spin labeling: Evaluation with T4 lysozyme. Proc. Natl. Acad. Sci. USA 92, 12295–12299.

    PubMed Central  PubMed  CAS  Google Scholar 

  • Voss, J., Hubbell, W. L., and Kaback, H. R. (1995b). Distance determination in proteins using designed metal ion binding sites and site-directed spin labeling: Application to the lactose permease of Escherichia coli. Proc. Natl. Acad. Sci. USA 92, 12300–12303.

    PubMed Central  PubMed  CAS  Google Scholar 

  • Voss, J., Hubbell, W. L., and Kaback, H. R. (1998). Helix Packing in the Lactose Permease Determined by Metal-Nitroxide Interaction. Biochem. 37, 211–216.

    CAS  Google Scholar 

  • Weil, J. A., Bolton, J. R., and Wertz, J. E. (1994). Electron Paramagnetic Resonance: Elementary Theory and Practical Applications. John Wiley & Sons, Inc., New York.

    Google Scholar 

  • Wider, G. and Wüthrich, K. (1999). NMR spectroscopy of large molecules and multimolecular assemblies in solution. Curr. Opin. Struct. Biol. 9, 594–601.

    PubMed  CAS  Google Scholar 

  • Yager, T. D., Eaton, G. R., and Eaton, S. S. (1978). (Cr(oxalate)3)3- as a Broadening Agent in Nitroxyl Spin Probe Studies. J. C. S. Chem. Commun., 944–945.

    Google Scholar 

  • Yoshioka, N., Irisawa, M., Mochizuki, Y., Kato, T., Inoue, H., and Ohba, S. (1997). Unusually Large Magnetic Interactions Observed in Hydrogen-Bonded Nitronyl Nitroxides. Chem. Lett. 251–252.

    Google Scholar 

  • Zwahlen, C., Gardner, K. H., Sarma, S. P., Horita, D. A., Byrd, R. A., and Kay, L. E. (1998). An NMR Experiment for Measuring Methyl-Methyl NOEs in 13C-Labeled Proteins with High Resolution. J. Am. Chem. Soc. 120, 7617–7625.

    CAS  Google Scholar 

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Authors and Affiliations

  1. Department of Chemistry and Biochemistry, University of Denver, Denver, Colorado, 80208, USA

    Sandra S. Eaton & Gareth R. Eaton

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  1. Sandra S. Eaton
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Editors and Affiliations

  1. Ohio State University, Columbus, Ohio, USA

    Lawrence J. Berliner

  2. Department of Chemistry and Biochemistry, University of Denver, 80208, Denver, Colorado, USA

    Gareth R. Eaton  & Sandra S. Eaton  & 

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© 2002 Kluwer Academic / Plenum Publishers, New York

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Eaton, S.S., Eaton, G.R. (2002). Distance Measurements by CW and Pulsed EPR. 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_1

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  • DOI: https://doi.org/10.1007/0-306-47109-4_1

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4757-0575-1

  • Online ISBN: 978-0-306-47109-4

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