Suppression of electron spin-echo envelope modulation peaks in double quantum coherence electron spin resonance

Journal of Magnetic Resonance

Volumn 170, Issue 2, 2004, Pages 278-283

  Bonora, Marco ^a   Becker, James ^a   Saxena, Sunil ^a  

^a UNIVERSITY OF PITTSBURGH   (United States)

Author keywords

Dipolar interactions; Distance measurements; Double quantum ESR; FT ESR; Spin labeling

Indexed keywords

FOURIER TRANSFORMS; FREQUENCIES; MICROWAVES; NUCLEIC ACIDS; PROTEINS; QUANTUM THEORY; SENSITIVITY ANALYSIS; TIME DOMAIN ANALYSIS;

DIPOLAR INTERACTIONS; DISTANCE-MEASUREMENTS; DOUBLE QUANTUN ESR; FT-ESR; SPIN-LABELING;

PARAMAGNETIC RESONANCE;

PEPTIDE;

ARTICLE; CHEMISTRY; ELECTRON SPIN RESONANCE; INSTRUMENTATION; MACROMOLECULE; METHODOLOGY; SIGNAL PROCESSING; SPIN LABELING;

ELECTRON SPIN RESONANCE SPECTROSCOPY; MACROMOLECULAR SUBSTANCES; PEPTIDES; SIGNAL PROCESSING, COMPUTER-ASSISTED; SPIN LABELS;

EID: 4544261371     PISSN: 10907807     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmr.2004.07.006     Document Type: Article

References (43)

1. V.V. Khurshev, A.M. Raitsimring, Y.D. Tsvetkov, Selection of the dipolar interaction by the "2 + 1" Pulse Train ESE, J. Magn. Reson. 81 (1989) 441-454.
2. A.D. Milov, A.G. Maryasov, Y.D. Tsvetkov, Pulsed electron double resonance (PELDOR) and its applications in free-radicals research, Appl. Magn. Reson. 15 (1998) 107-143.
3. P.P. Borbat, J.H. Freed, Multiple-quantum ESR and distance measurements, Chem. Phys. Lett. 313 (1999) 145-154.
4. L.J. Berliner, S.S. Eaton, G.R. Eaton (Eds.), Biological Magnetic Resonance, vol. 19, Kluwer Academic/Plenum Publisher, New York, 2000 (Chapters 8-13).
5. J.H. Freed, New technologies in electron spin resonance, Ann. Rev. Phys. Chem. 51 (2000) 655-689.
6. G. Jeschke, M. Pannier, A. Godt, H.W. Spiess, Dipolar spectroscopy and spin alignment in electron paramagnetic resonance, Chem. Phys. Lett. 331 (2000) 243-252.
7. M. Pannier, S. Veit, A. Godt, G. Jeschke, H.W. Spiess, Deadtime free measurement of dipole-dipole interactions between electron spins, J. Magn. Reson. 142 (2000) 331-340.
8. Y. Zhou, B.E. Bowler, K. Lynch, S.S. Eaton, G.R. Eaton, Interspin distances in spin-labeled metmyoglobin variants determined by saturation recovery EPR, Biophys. J. 79 (2000) 1039-1052.
9. P.P. Borbat, A.J. Costa-Filho, K.A. Earle, J.K. Moscicki, J.H. Freed, Electron spin resonance in studies of membranes and proteins, Science 291 (2001) 266-269.
10. L.V. Kulik, S.A. Dzuba, I.A. Grigoryev, Y.D. Tsvetkov, Electron dipole-dipole interaction in ESEEM of nitroxide biradicals, Chem. Phys. Lett. 343 (2001) 315-324.
11. A.D. Milov, R.I. Samoilova, Y.D. Tsvetkov, V.A. Gusev, F. Formaggio, M. Crisma, C. Toniolo, J. Raap, Spatial distribution of spin-labeled Trichogin GA IV in the gram-positive bacterial cell membrane determined from PELDOR data, Appl. Magn. Reson. 23 (2002) 81-95.
12. G.L. Millhauser, Selective placement of electron spin resonance spin labels: new structural methods for peptides and proteins, Trends Biochem. Sci. 17 (1992) 448-452.
13. W.L. Hubbell, C. Altenbach, Site-directed spin labeling of membrane proteins, in: S.H. White (Ed.), Membrane Protein Structure: Experimental Approaches, Oxford, New York, 1994.
14. L. Columbus, W.L. Hubbell, A new spin on protein dynamics, Trends Biochem. Sci. 27 (2002) 288-295.
15. W.L. Hubbell, C. Altenbach, C.M. Hubbell, H.G. Khorana, Rhodopsin structure, dynamics, and activation: a perspective from crystallography, site-directed spin labeling, sulfhydryl reactivity, and disulfide cross-linking, Adv. Protein Chem. 63 (2003) 243-290.
16. M. Persson, J.R. Harbridge, P. Hammarstrom, R. Mitri, L.G. Martensson, U. Carlsson, G.R. Eaton, S.S. Eaton, Comparison of electron paramagnetic resonance methods to determine distances between spin labels on human carbonic anhydrase II, Biophys. J. 80 (2001) 2886-2897.
17. P.P. Borbat, H.S. Mchaourab, J.H. Freed, Protein structure determination using long-distance constraints from double-quantum coherence ESR: study of T4 lysozyme, J. Am. Chem. Soc. 124 (2002) 5304-5314.
18. +/proline transporter PutP of Escherichia coli, Biophys. J. 86 (2004) 2551-2557.
19. O. Schiemann, A. Weber, T. Edwards, T. Prisner, S. Sigurdsson, Nanometer distance measurements on RNA using PELDOR, J. Am. Chem. Soc. 125 (2003) 3434-3435.
20. O. Schiemann, N. Piton, Y. Mu, G. Stock, J.W. Engels, T.F. Prisner, A PELDOR-based nanometer distance ruler for oligo-nucleotides, J. Am. Chem. Soc. 126 (2004) 5722-5729.
21. E. Narr, A. Godt, G. Jeschke, Selective measurements of a nitroxide-nitroxide separation of 5nm and a nitroxide-copper separation of 2. 5nm in a terpyridine based copper(II) complex by pulse EPR spectroscopy, Angew. Chem. Intl. Ed. 41 (2002) 3907-3910.
22. G. Jeschke, Distance measurements in the nanometer range by pulse EPR, Chem. Phys. Chem. 3 (2002) 927-932.
23. G. Jeschke, Determination of the nanostructure of polymer materials by electron paramagnetic resonance spectroscopy, Macromol. Rapid Commun. 23 (2002) 227-246.
24. I.M.C. vanAmsterdam, M. Ubbink, G.W. Canters, M. Huber, Measurement of a Cu-Cu distance of 26 angstroms by a pulsed EPR method, Angew. Chem. Intl. Ed. 42 (2003) 62-64.
25. M. Bennati, A. Weber, J. Antonic, D.L. Perlstein, J. Robblee, J. Stubbe, Pulsed ELDOR spectroscopy measures the distance between the two tyrosyl radicals in the R2 subunit of the E. coli ribonucleotide reductase, J. Am. Chem. Soc. 125 (200:5) 14988-14989.
26. A.D. Milov, A.G. Maryasov, Y.D. Tsvetkov, J. Raap, Pulsed ELDOR in spin-labeled polypeptides, Chem. Phys. Lett. 303 (1999) 135-143.
27. A.D. Milov, Y.D. Tsvetkov, F. Formaggio, M. Crisma, C. Toniolo, J. Raap, Self-assembling properties of membrane-modifying peptides studied by PELDOR and CW-ESR spectroscopies, J. Am. Chem. Soc. 122 (2000) 3843-3848.
28. A.D. Milov, Y.D. Tsvetkov, F. Formaggio, M. Crisma, C. Toniolo, J. Raap, The secondary structure of a membrane-modifying peptide in a supramolecular assembly studied by PELDOR and CW-ESR spectroscopies, J. Am. Chem. Soc. 123 (2001) 3784-3789.
29. P.P. Borbat, J.H. Freed, Double-Quantum ESR and Distance Measurements, in: L.J. Berliner, S.S. Eaton, G.R. Eaton (Eds.), Biological Magnetic Resonance, vol. 19, Kluwer Academics/ Plenum Publishers, New York, 2000, pp. 383-459.
30. M. Fedin, M. Kalin, I. Gromov, A. Schweiger, Applications of π-photon-induced transparency in two-frequency pulse electron paramagnetic resonance experiments, J. Chem. Phys. 120 (2004) 1361-1368.
31. C. Elsasser, M. Brecht, R. Bittl, Pulsed electron-electron double resonance on multinuclear metal clusters: assignment of spin projection factors based on the dipolar interaction, J. Am. Chem. Soc. 124 (2002) 12606-12611.
32. P.P. Borbat, R.H. Crepeau, J.H. Freed, Multifrequency two-dimensional fourier transform ESR: An X/Ku-Band spectrometer, J. Magn. Reson. 127 (1997) 155-167.
33. C. Gemperle, A. Schweiger, R.R. Ernst, Novel analytical treatments of electron spin-echo envelope modulation with short and extended pulses, J. Magn. Reson. 91 (1991) 273-288.
34. A. Schweiger, G. Jeschke, Principles of Pulse Electron Paramagnetic Resonance, Oxford University Press, 2001 p. 260.
35. A.P. Todd, G.L. Millhauser, ESR spectra reflect local and global mobility in a short spin-labeled peptide throughout the alpha helix-coil transition, Biochemistry 30 (1991) 5515-5523.
36. J.R. Klauder, P.W. Anderson, Spectral diffusion decay in spin resonance experiments, Phys. Rev. 125 (1962) 912-932.
37. R.G. Larsen, D.J. Singel, Double electron-electron resonance spin-echo modulation spectroscopic measurement of electron-spin pair separations in orientationally disordered solids, J. Chem. Phys. 98 (1993) 5134-5146.
38. We found subtraction of an exponential decay sufficient to remove contributions from transverse relaxation and decay due to intermolecular electron-electron interactions.
39. S.A. Dikanov, Y.D. Tsvetkov, Electron Spin Echo Envelope Modulation (ESEEM) Spectroscopy, CRC Press, Boca Raton, FL, 1992.
40. The energy was minimized from various starting geometries and the uncertainties reflect the range of distances obtained in the different energy minimized conformations.
41. L.V. Kulik, I.A. Grigoryev, E.S. Salnikov, S.A. Dzuba, Y.D. Tsvetkov, Electron spin-echo envelope modulation induced by slow intramolecular motion, J. Phys. Chem. A 107 (2003) 3692-3695.
42. To determine the noise we chose the spectral range between 21 and 26MHz (cf. Fig. 2B), which contains some spectral components. These were eliminated by subtracting a second order polynomial from the spectrum. The noise was determined from the resultant baseline.
43. Despite the 2.5 mM concentration of this sample, we do not expect nor observe low frequency peaks due to intermolecular dipolar interactions. The average intermolecular distance between para-magnetic centers is ∼90 Å assuming a homogeneous distribution of molecules.