Comparison of electron paramagnetic resonance methods to determine distances between spin labels on human carbonic anhydrase II

Biophysical Journal

Volumn 80, Issue 6, 2001, Pages 2886-2897

  Persson, Malin ^a   Harbridge, James R ^a   Hammarström, Per ^b   Mitri, Ragheed ^a   Mårtensson, Lars Göran ^b   Carlsson, Uno ^b   Eaton, Gareth R ^a   Eaton, Sandra S ^a  

^a UNIVERSITY OF DENVER   (United States)

^b LINKÖPING UNIVERSITY   (Sweden)

Author keywords

[No Author keywords available]

Indexed keywords

CARBONATE DEHYDRATASE II;

ACCURACY; ANALYTIC METHOD; ARTICLE; COMPUTER SIMULATION; ELECTRON; ELECTRON SPIN RESONANCE; ENZYME STRUCTURE; FOURIER ANALYSIS; INTERMETHOD COMPARISON; PHASE TRANSITION; SITE DIRECTED MUTAGENESIS; SPIN LABELING; STRUCTURE ANALYSIS;

EID: 0034998819     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(01)76254-6     Document Type: Article

References (46)

1. Alexander, R. S., S. K. Nair, and D. W. Christianson. 1991. Engineering the hydrophobic pocket of carbonic anhydrase II. Biochemistry. 30: 11064-11072.
2. Barbon, A., M. Brustolon, A. L. Maniero, M. Romanelli, and L.-C. Brunel. 1999. Dynamics and spin relaxation of Tempone in a host crystal: an ENDOR, high-field EPR, and electron spin echo study. Phys. Chem. Chem. Phys. 1:4015-4023.
3. Borbat, P. P., and J. H. Freed. 1999. Multi-quantum ESR and distance measurements. Chem. Phys. Lett. 313:145-154.
4. Eaton, S. S., K. M. More, B. M. Sawant, and G. R. Eaton. 1983a. Use of the EPR half-field transition to determine the interspin distance and the orientation of the interspin vector in systems with two unpaired electrons. J. Am. Chem. Soc. 105:6560-6567.
5. Eaton, S. S., K. M. More, B. M. Sawant, P. M. Boymel, and G. R. Eaton. 1983b. Metal-nitroxyl interactions. 29. EPR studies of spin-labeled copper complexes in frozen solution. J. Magn. Reson. 52:435-449.
6. Eriksson, A. E., T. A. Jones, and A. Liljas. 1988. Refined structure of human carbonic anhydrase II at 2.0 Å resolution. Proteins Struct. Funct. Genet. 4:274-282.
7. Fierke, C. A., T. L. Calderone, and J. F. Krebs. 1991. Functional consequences of engineering the hydrophobic pocket of carbonic anhydrase II. Biochemistry. 30:11054-11063.
8. Freskgård, P.-O., U. Carlsson, L.-G. Mårtensson, and B.-H. Jonsson. 1991. Folding around the C-terminus of human carbonic anhydrase II. FEBS Lett. 289:117-122.
9. Freskgård, P. O., L.-G. Mårtensson, P. Jonasson, B. H. Jonsson, and U. Carlsson. 1994. Assignment of the contribution of the tryptophan residues to the circular dichroism spectrum of human carbonic anhydrase II. Biochemistry. 33:14281-14288.
10. Grassetti, D. R., and J. F. Murray, Jr. 1967. Determination of sulfhydryl groups with 2,2′ and 4,4′-dithiopyridine. Arch. Biochem. Biophys. 119: 41-49.
11. Håkansson, K., U. Carlsson, M. Svensson, and A. Liljas. 1992. Structure of native and apo carbonic anhydrase II and structure of some of its anion-ligand complexes. J. Mol. Biol. 277:1192-1204.
12. Hammarström, P., B. Kalman, B.-H. Jonsson, and U. Carlsson. 1997. Pyrene excimer fluorescence as a proximity probe for investigation of residual structure in the unfolded state of human carbonic anhydrase II. FEBS Lett. 420:63-68.
13. Henderson, L. E., D. Henriksson, and P. O. Nyman. 1976. Primary structure of human carbonic anhydrase C. J. Biol. Chem. 251:5457-5463.
14. Hubbell, W. L., and C. Altenbach. 1994. Investigation of structure and dynamics of membrane proteins using site-directed spin labeling. Curr. Opin. Struct. Biol. 4:566-573.
15. Hubbell, W. L., A. Fross, R. Langren, and M. A. Lietzow. 1998. Recent advances in site-directed spin labeling of proteins. Curr. Opin. Struct. Biol. 8:649-656.
16. Hunt, J. A., M. Ahmed, and C. A. Fierke. 1999. Metal binding specificity in carbonic anhydrase is influenced by conserved hydrophobic core residues. Biochemistry. 38:9054-9062.
17. Hustedt, E. J., C. E. Cobb, A. H. Beth, and J. M. Beechem. 1993. Measurement of rotational dynamics by the simultaneous nonlinear analysis of optical and EPR data. Biophys. J. 64:614-621.
18. Hustedt, E. J., A. I. Smirnov, C. F. Laub, C. E. Cobb, and A. H. Beth. 1997. Molecular distances from dipolar coupled spin-labels: the global analysis of multifrequency continuous wave electron paramagnetic resonance data. Biophys. J. 74:1861-1877.
19. Khalifah, R. G., D. J. Strader, S. H. Bryant, and S. M. Gibson. 1977. Carbon-13 nuclear magnetic resonance probe of active-site ionizations in human carbonic anhydrase B. Biochemistry. 16:2241-2247.
20. Kokorin, A. I., K. I. Zamarayev, G. L. Grigoryan, V. P. Ivanov, and E. G. Rozantsev. 1972. Measurement of the distances between the paramagnetic centers in solid solutions of nitroxide radicals, biradicals, and spin-labeled proteins. Biofizika. 17:34-41.
21. Kunkel, T. A., J. D. Roberts, and R. A. Zakour. 1987. Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol. 154:367-382.
22. Langen, R., K. J. Oh, D. Cascico, and W. L. Hubbell. 2000. Crystal structures of spin labeled T4 lysozyme mutants: implications for the interpretation of EPR spectra in terms of structure. Biochemistry. 39: 8396-8405.
23. Larsen, R. G., and D. J. Singel. 1993. Double electron-electron resonance spin-echo modulation: spectroscopic measurement of electron spin pair separations in orientationally disordered solids. J. Chem. Phys. 98: 5134-5146.
24. Lindgren, M., M. Svensson, P.-O. Freskgård, U. Carlsson, B.-H. Jonsson, L.-G. Mårtensson, and P. Jonasson. 1993. Probing local mobility in carbonic anhydrase: EPR of spin-labeled SH groups introduced by site-directed mutagenesis. J. Chem. Soc. Perkin Trans. 2:2003-2007.
25. Lindskog, S. 1997. Structure and mechanism of carbonic anhydrase. Pharmacol. Ther. 74:1-20.
26. Mårtensson, L.-G., B.-H. Jonsson, P.-O. Freskgård, A. Kihlgren, M. Svensson, and U. Carlsson. 1993. Characterization of folding intermediates of human carbonic anhydrase II: probing substructure by chemical labeling of sulfhydryl groups introduced by site-directed mutagenesis. Biochemistry. 32:224-231.
27. Martin, R. E., M. Pannier, F. Diederich, V. Gramlich, M. Hubrich, and H. W. Spiess. 1998. Determination of the 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.
28. Mchaourab, H. S., M. A. Lietzow, K. Hideg, and W. L. Hubbell. 1996. Motion of spin-labeled side chains in T4 lysozyme: correlation with protein structure and dynamics. Biochemistry. 35:7692-7704.
29. Milov, A. D., A. G. Maryanov, and Yu. D. Tsvetkov. 1998. Pulsed electron double resonance (PELDOR) and its application in free radicals research. Appl. Magn. Reson. 15:107-143.
30. Milov, A. D., K. M. Salikhov, and M. D. Shirov. 1981. Application of the double resonance method to electron spin echo in a study of the spatial distribution of paramagnetic centers in solids. Sov. Phys. Solid State. 23:565-569.
31. Nair, S. K., T. L. Calderone, D. W. Christianson, and C. A. Fierke. 1991. Altering the mouth of a hydrophobic pocket: structure and kinetics of human carbonic anhydrase II mutants at residue Val-121. J. Biol. Chem. 266:17320-17325.
32. Nakagawa, K., M. B. Candelaria, W. W. C. Chik, S. S. Eaton, and G. R. Eaton. 1992. Electron spin relaxation times of chromium(V). J. Magn. Reson. 98:81-91.
33. Nyman, P. O., and S. Lindskog. 1964. Amino acid composition of various forms of bovine and human erythrocyte carbonic anhydrase. Biochim. Biophys. Acta. 85:141-151.
34. Ottemann, K. M., T. E. Thorgeirsson, A. F. Kolodziej, Y.-K. Shin, and D. E. Koshland, Jr. 1998. Direct measurement of small ligand-induced conformational changes in the aspartate chemoreceptor using EPR. Biochemistry. 37:7062-7069.
35. Pannier, M., S. Veit, A. Godt, G. Jeschke, and H. W. Spiess. 2000. Dead-time free measurement of dipole-dipole interactions between electron spins. J. Magn. Reson. 142:331-340.
36. Persson, M. P., P. Hammarström, M. Lindgren, B.-H. Jonsson, M. Svensson, and U. Carlsson. 1999. EPR mapping of interactions between spin-labeled variants of human carbonic anhydrase II and GroEL: evidence for increased flexibility of the hydrophobic core by the interaction. Biochemistry. 38:432-441.
37. Quine, R. W., G. R. Eaton, and S. S. Eaton. 1987. Pulsed EPR spectrometer. Rev. Sci. Instrum. 58:1709-1724.
38. Rabenstein, M. D., and Y.-K. Shin. 1995. Determination of the distance between two spin labels attached to a macromolecule. Proc. Natl. Acad. Sci. U.S.A. 92:8239-8243.
39. Raitsimring, A., J. Peisach, H. C. Lee, and X. Chen. 1992. Measurement of distance distributions between spin labels in spin-labeled hemoglobin using an electron spin echo method. J. Phys. Chem. 96:3526-3531.
40. Rickli, E. E., S. A. S. Ghanzafar, B. H. Gibbon, and J. T. Edsall. 1964. Carbonic anhydrases from human erythrocytes J. Biol. Chem. 239: 1065-1078.
41. Rinard, G. A., R. W. Quine, J. R. Harbridge, R. Song, G. R. Eaton, and S. S. Eaton. 1999. Frequency dependence of EPR signal-to-noise. J. Magn. Reson. 140:218-227.
42. Sanger, F., S. Nicklen, and A. R. Coulson. 1977. DNA sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. U.S.A. 74: 5463-5467.
43. Saxena, S., and J. H. Freed. 1997. Theory of double quantum two-dimensional electron spin resonance with application to distance measurements. J. Chem. Phys. 107:1317-1340.
44. Sun, J., J. Voss, W. L. Hubbell, and H. R. Kaback. 1999. Proximity between periplasmic loops in the lactose permease of Escherichia coli as determined by site-directed spin labeling. Biochemistry. 38:3100-3105.
45. Svensson, M., P. Jonasson, P.-O. Freskgård, B.-H. Jonsson, M. Lindgren, L.-G. Mårtensson, M. Gentile, K. Boren, and U. Carlsson. 1995. Mapping the folding intermediate of human carbonic anhydrase II: probing substructure by chemical reactivity and spin and fluorescence labeling of engineered cysteine residues. Biochemistry. 34:8606-8620.
46. Toy, A. D., S. H. H. Chaston, J. R. Pilbrow, and T. D. Smith. 1971. An electron spin resonance study of the copper(II) chelates of certain monothio-β-diketonates and diethyldithiocarbamate. Inorg. Chem. 10: 2219-2225.