메뉴 건너뛰기




Volumn 49, Issue 7, 2010, Pages 1486-1494

Electron spin-echo envelope modulation (ESEEM) reveals water and phosphate interactions with the KcsA potassium channel

Author keywords

[No Author keywords available]

Indexed keywords

COPPER COMPLEXES; ELECTRON SPIN-ECHO ENVELOPE MODULATION SPECTROSCOPIES; ELECTRON SPIN-ECHO ENVELOPE MODULATIONS; ENZYME MECHANISM; MEMBRANE PROTEINS; METAL CENTERS; MODEL SYSTEM; NATIVE ENVIRONMENT; NATURALLY OCCURRING; OTHER APPLICATIONS; PHOSPHATE INTERACTIONS; POTASSIUM CHANNELS; SITE-DIRECTED SPIN LABELING; STRUCTURAL TOOLS; WATER PERMEATION; WELL-ESTABLISHED TECHNIQUES;

EID: 77449151358     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi9016523     Document Type: Article
Times cited : (38)

References (52)
  • 2
    • 0037389538 scopus 로고    scopus 로고
    • Electron-nuclear double resonance spectroscopy (and electron spin-echo envelope modulation spectroscopy) in bioinorganic chemistry
    • Hoffman, B. M. (2003) Electron-nuclear double resonance spectroscopy (and electron spin-echo envelope modulation spectroscopy) in bioinorganic chemistry. Proc. Natl. Acad. Sci. U.S.A. 100, 3575-3578.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 3575-3578
    • Hoffman, B.M.1
  • 3
    • 0017083127 scopus 로고
    • Assignment of a ligand in stellacyanin by a pulsed electron paramagnetic resonance method
    • Mims, W. B., and Peisach, J. (1976) Assignment of a ligand in stellacyanin by a pulsed electron paramagnetic resonance method. Biochemistry 15, 3863-3869.
    • (1976) Biochemistry , vol.15 , pp. 3863-3869
    • Mims, W.B.1    Peisach, J.2
  • 4
    • 0034743154 scopus 로고    scopus 로고
    • Pulsed EPR spectroscopy: Biological applications
    • Prisner, T., Rohrer, M., and MacMillan, F. (2001) Pulsed EPR spectroscopy: biological applications. Annu. Rev. Phys. Chem. 52, 279-313.
    • (2001) Annu. Rev. Phys. Chem. , vol.52 , pp. 279-313
    • Prisner, T.1    Rohrer, M.2    MacMillan, F.3
  • 5
    • 0038506974 scopus 로고    scopus 로고
    • ENDOR of metalloenzymes
    • Hoffman, B. M. (2003) ENDOR of metalloenzymes. Acc. Chem. Res. 36, 522-529.
    • (2003) Acc. Chem. Res. , vol.36 , pp. 522-529
    • Hoffman, B.M.1
  • 8
    • 0037307520 scopus 로고    scopus 로고
    • Intramembrane polarity by electron spin echo spectroscopy of labeled lipids
    • Bartucci, R., Guzzi, R., Marsh, D., and Sportelli, L. (2003) Intramembrane polarity by electron spin echo spectroscopy of labeled lipids. Biophys. J. 84, 1025-1030.
    • (2003) Biophys. J. , vol.84 , pp. 1025-1030
    • Bartucci, R.1    Guzzi, R.2    Marsh, D.3    Sportelli, L.4
  • 9
    • 33646189366 scopus 로고    scopus 로고
    • Utilizing ESEEM spectroscopy to locate the position of specific regions of membrane-active peptides within model membranes
    • Carmieli, R., Papo, N., Zimmermann, H., Potapov, A., Shai, Y., and Goldfarb, D. (2006) Utilizing ESEEM spectroscopy to locate the position of specific regions of membrane-active peptides within model membranes. Biophys. J. 90, 492-505.
    • (2006) Biophys. J. , vol.90 , pp. 492-505
    • Carmieli, R.1    Papo, N.2    Zimmermann, H.3    Potapov, A.4    Shai, Y.5    Goldfarb, D.6
  • 11
    • 61549135446 scopus 로고    scopus 로고
    • Pulsed EPR determination of water accessibility to spin-labeled amino acid residues in LHCIIb
    • Volkov, A., Dockter, C., Bund, T., Paulsen, H., and Jeschke, G. (2009) Pulsed EPR determination of water accessibility to spin-labeled amino acid residues in LHCIIb. Biophys. J. 96, 1124-1141.
    • (2009) Biophys. J. , vol.96 , pp. 1124-1141
    • Volkov, A.1    Dockter, C.2    Bund, T.3    Paulsen, H.4    Jeschke, G.5
  • 13
    • 0033812585 scopus 로고    scopus 로고
    • Identifying conformational changes with site-directed spin labeling
    • Hubbell, W. L., Cafiso, D. S., and Altenbach, C. (2000) Identifying conformational changes with site-directed spin labeling. Nat. Struct. Biol. 7, 735-739.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 735-739
    • Hubbell, W.L.1    Cafiso, D.S.2    Altenbach, C.3
  • 15
    • 33749041288 scopus 로고    scopus 로고
    • Recent advances and applications of site-directed spin labeling
    • Fanucci, G. E., and Cafiso, D. S. (2006) Recent advances and applications of site-directed spin labeling. Curr. Opin. Struct. Biol. 16, 644-653.
    • (2006) Curr. Opin. Struct. Biol. , vol.16 , pp. 644-653
    • Fanucci, G.E.1    Cafiso, D.S.2
  • 16
    • 0034933792 scopus 로고    scopus 로고
    • Polarity and permeation profiles in lipid membranes
    • Marsh, D. (2001) Polarity and permeation profiles in lipid membranes. Proc. Natl. Acad. Sci. U.S.A. 98, 7777-7782.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 7777-7782
    • Marsh, D.1
  • 17
    • 0036296443 scopus 로고    scopus 로고
    • High-field electron spin resonance of spin labels in membranes
    • Marsh, D., Kurad, D., and Livshits, V. A. (2002) High-field electron spin resonance of spin labels in membranes. Chem. Phys. Lipids 116, 93-114.
    • (2002) Chem. Phys. Lipids , vol.116 , pp. 93-114
    • Marsh, D.1    Kurad, D.2    Livshits, V.A.3
  • 18
    • 0015986660 scopus 로고
    • Shape of the hydrophobic barrier of phospholipid bilayers. (Evidence for water penetration in biological membranes)
    • Griffith, O. H., Dehlinger, P. J., and Van, S. P. (1974) Shape of the hydrophobic barrier of phospholipid bilayers. (Evidence for water penetration in biological membranes). J. Membr. Biol. 15, 159-192.
    • (1974) J. Membr. Biol. , vol.15 , pp. 159-192
    • Griffith, O.H.1    Dehlinger, P.J.2    Van, S.P.3
  • 19
    • 0028346566 scopus 로고
    • A collision gradient method to determine the immersion depth of nitroxides in lipid bilayers: Application to spin-labeled mutants of bacteriorhodopsin
    • Altenbach, C., Greenhalgh, D. A., Khorana, H. G., and Hubbell, W. L. (1994) A collision gradient method to determine the immersion depth of nitroxides in lipid bilayers: application to spin-labeled mutants of bacteriorhodopsin. Proc. Natl. Acad. Sci. U.S.A. 91, 1667-1671.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 1667-1671
    • Altenbach, C.1    Greenhalgh, D.A.2    Khorana, H.G.3    Hubbell, W.L.4
  • 20
    • 24144502337 scopus 로고    scopus 로고
    • Accessibility of nitroxide side chains: Absolute Heisenberg exchange rates from power saturation. EPR
    • Altenbach, C., Froncisz, W., Hemker, R., Mchaourab, H., and Hubbell, W. L. (2005) Accessibility of nitroxide side chains: absolute Heisenberg exchange rates from power saturation. EPR. Biophys. J. 89, 2103-2112.
    • (2005) Biophys. J. , vol.89 , pp. 2103-2112
    • Altenbach, C.1    Froncisz, W.2    Hemker, R.3    Mchaourab, H.4    Hubbell, W.L.5
  • 21
    • 0028841033 scopus 로고
    • A prokaryotic potassium ion channel with two predicted transmembrane segments from Streptomyces lividans
    • Schrempf, H., Schmidt, O., Kummerlen, R., Hinnah, S., Muller, D., Betzler, M., Steinkamp, T., and Wagner, R. (1995) A prokaryotic potassium ion channel with two predicted transmembrane segments from Streptomyces lividans. EMBO J. 14, 5170-5178.
    • (1995) EMBO J. , vol.14 , pp. 5170-5178
    • Schrempf, H.1    Schmidt, O.2    Kummerlen, R.3    Hinnah, S.4    Muller, D.5    Betzler, M.6    Steinkamp, T.7    Wagner, R.8
  • 26
    • 0033543132 scopus 로고    scopus 로고
    • Structure of the KcsA potassium, channel from Streptomyces lividans: A site-directed spin labeling study of the second transmembrane segment
    • Gross, A., Columbus, L., Hideg, K., Altenbach, C., and Hubbell, W. L. (1999) Structure of the KcsA potassium, channel from Streptomyces lividans: a site-directed spin labeling study of the second transmembrane segment. Biochemistry 38, 10324-10335.
    • (1999) Biochemistry , vol.38 , pp. 10324-10335
    • Gross, A.1    Columbus, L.2    Hideg, K.3    Altenbach, C.4    Hubbell, W.L.5
  • 27
    • 0037192124 scopus 로고    scopus 로고
    • Identification of protein side chains near the membrane-aqueous interface: A site-directed spin labeling study of KcsA
    • Gross, A., and Hubbell, W. L. (2002) Identification of protein side chains near the membrane-aqueous interface: a site-directed spin labeling study of KcsA. Biochemistry 41, 1123-1128.
    • (2002) Biochemistry , vol.41 , pp. 1123-1128
    • Gross, A.1    Hubbell, W.L.2
  • 28
    • 39549107903 scopus 로고    scopus 로고
    • The structure of the lipid-embedded potassium channel voltage sensor determined by double-electron-electron resonance spectroscopy
    • Vamvouka, M., Cieslak, J., Van Eps, N., Hubbell, W., and Gross, A. (2008) The structure of the lipid-embedded potassium channel voltage sensor determined by double-electron-electron resonance spectroscopy. Protein Sci. 17, 506-517.
    • (2008) Protein Sci. , vol.17 , pp. 506-517
    • Vamvouka, M.1    Cieslak, J.2    Van Eps, N.3    Hubbell, W.4    Gross, A.5
  • 29
    • 0021646583 scopus 로고
    • Asymmetric reconstitution of homogeneous Escherichia coli sn-glycerol-3-phosphate acyltransferase into phospholipid vesicles
    • Green, P. R., and Bell, R. M. (1984) Asymmetric reconstitution of homogeneous Escherichia coli sn-glycerol-3-phosphate acyltransferase into phospholipid vesicles. J. Biol. Chem. 259, 14688-14694.
    • (1984) J. Biol. Chem. , vol.259 , pp. 14688-14694
    • Green, P.R.1    Bell, R.M.2
  • 30
    • 0020267981 scopus 로고
    • Estimating the parameters of exponentially damped sinusoids and pole-zero modeling in noise
    • Kumaresan, R., and Tufts, D. W. (1982) Estimating the parameters of exponentially damped sinusoids and pole-zero modeling in noise. IEEE Trans. Acoust., Speech, Signal Process. 30, 833-840.
    • (1982) IEEE Trans. Acoust., Speech, Signal Process. , vol.30 , pp. 833-840
    • Kumaresan, R.1    Tufts, D.W.2
  • 31
    • 0034811157 scopus 로고    scopus 로고
    • Spin and fluorescent probing of the binding interface between tissue factor and factor VIIa at multiple sites
    • Owenius, R., Osterlund, M., Svensson, M., Lindgren, M., Persson, E., Freskgard, P. O., and Carlsson, U. (2001) Spin and fluorescent probing of the binding interface between tissue factor and factor VIIa at multiple sites. Biophys. J. 81, 2357-2369.
    • (2001) Biophys. J. , vol.81 , pp. 2357-2369
    • Owenius, R.1    Osterlund, M.2    Svensson, M.3    Lindgren, M.4    Persson, E.5    Freskgard, P.O.6    Carlsson, U.7
  • 32
    • 38349057937 scopus 로고    scopus 로고
    • Polarity dependence of EPR parameters for TOAC and MTSSL spin labels: Correlation with DOXYL spin labels for membrane studies
    • Marsh, D., and Toniolo, C. (2008) Polarity dependence of EPR parameters for TOAC and MTSSL spin labels: correlation with DOXYL spin labels for membrane studies. J. Magn. Reson. 190, 211-221.
    • (2008) J. Magn. Reson. , vol.190 , pp. 211-221
    • Marsh, D.1    Toniolo, C.2
  • 33
    • 0037387189 scopus 로고    scopus 로고
    • Potassium channel gating observed with site-directed mass tagging
    • Kelly, B. L., and Gross, A. (2003) Potassium channel gating observed with site-directed mass tagging. Nat. Struct. Biol. 10, 280-284.
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 280-284
    • Kelly, B.L.1    Gross, A.2
  • 34
    • 0035013633 scopus 로고    scopus 로고
    • Molecular architecture of full-length KcsA: Role of cytoplasmic domains in ion permeation and activation gating
    • Cortes, D. M., Cuello, L. G., and Perozo, E. (2001) Molecular architecture of full-length KcsA: role of cytoplasmic domains in ion permeation and activation gating. J. Gen. Physiol. 117, 165-180.
    • (2001) J. Gen. Physiol. , vol.117 , pp. 165-180
    • Cortes, D.M.1    Cuello, L.G.2    Perozo, E.3
  • 36
    • 27844436560 scopus 로고    scopus 로고
    • Specific protein-lipid interactions in membrane proteins
    • Hunte, C. (2005) Specific protein-lipid interactions in membrane proteins. Biochem. Soc. Trans. 33, 938-942.
    • (2005) Biochem. Soc. Trans. , vol.33 , pp. 938-942
    • Hunte, C.1
  • 37
    • 0000242143 scopus 로고
    • Hyperfine sublevel correlation (HYSCORE) spectroscopy - A 2D electron-spin-resonance investigation of the squaric acid radical
    • Hofer, P., Grupp, A., Nebenfuhr, H., and Mehring, M. (1986) Hyperfine sublevel correlation (HYSCORE) spectroscopy - a 2D electron-spin-resonance investigation of the squaric acid radical. Chem. Phys. Lett. 132, 279-282.
    • (1986) Chem. Phys. Lett. , vol.132 , pp. 279-282
    • Hofer, P.1    Grupp, A.2    Nebenfuhr, H.3    Mehring, M.4
  • 39
    • 33846352840 scopus 로고    scopus 로고
    • Dynamics of the nitroxide side chain in spin-labeled proteins
    • Tombolato, F., Ferrarini, A., and Freed, J. H. (2006) Dynamics of the nitroxide side chain in spin-labeled proteins. J. Phys. Chem. B 110, 26248-26259.
    • (2006) J. Phys. Chem. B , vol.110 , pp. 26248-26259
    • Tombolato, F.1    Ferrarini, A.2    Freed, J.H.3
  • 40
    • 0033650104 scopus 로고    scopus 로고
    • Sitedirected spin labeling of proteins. Applications to diphtheria toxin
    • Oh, K. J., Altenbach, C., Collier, R. J., and Hubbell, W. L. (2000) Sitedirected spin labeling of proteins. Applications to diphtheria toxin. Methods Mol. Biol. 145, 147-169.
    • (2000) Methods Mol. Biol. , vol.145 , pp. 147-169
    • Oh, K.J.1    Altenbach, C.2    Collier, R.J.3    Hubbell, W.L.4
  • 41
    • 0015981720 scopus 로고
    • Deuterium magnetic resonance studies of phospholipid bilayers
    • Seelig, J., and Seelig, A. (1974) Deuterium magnetic resonance studies of phospholipid bilayers. Biochem. Biophys. Res. Commun. 57, 406-411.
    • (1974) Biochem. Biophys. Res. Commun. , vol.57 , pp. 406-411
    • Seelig, J.1    Seelig, A.2
  • 42
    • 34547687784 scopus 로고    scopus 로고
    • Isotope labeling strategies for the study of high-molecular-weight proteins by solution. NMR spectroscopy
    • Tugarinov, V., Kanelis, V., and Kay, L. E. (2006) Isotope labeling strategies for the study of high-molecular-weight proteins by solution. NMR spectroscopy. Nat. Protoc. 1, 749-754.
    • (2006) Nat. Protoc. , vol.1 , pp. 749-754
    • Tugarinov, V.1    Kanelis, V.2    Kay, L.E.3
  • 43
    • 70349298715 scopus 로고    scopus 로고
    • A combined pulse EPR and Monte Carlo simulation study provides molecular insight on peptide-membrane interactions
    • Gordon-Grossman, M., Gofman, Y., Zimmermann, H., Frydman, V., Shai, Y., Ben-Tal, N., and Goldfarb, D. (2009) A combined pulse EPR and Monte Carlo simulation study provides molecular insight on peptide-membrane interactions. J. Phys. Chem. B 113, 12687-12695.
    • (2009) J. Phys. Chem. B , vol.113 , pp. 12687-12695
    • Gordon-Grossman, M.1    Gofman, Y.2    Zimmermann, H.3    Frydman, V.4    Shai, Y.5    Ben-Tal, N.6    Goldfarb, D.7
  • 45
    • 0015243222 scopus 로고
    • Lipid bilayer structure in the membrane of Mycoplasma laidlawii
    • Engelman, D. M. (1971) Lipid bilayer structure in the membrane of Mycoplasma laidlawii. J. Mol. Biol. 58, 153-165.
    • (1971) J. Mol. Biol. , vol.58 , pp. 153-165
    • Engelman, D.M.1
  • 46
    • 22944490571 scopus 로고    scopus 로고
    • Distance measurements between, paramagnetic centers and a planar object by matrix Mims electron nuclear double resonance
    • Zanker, P. P., Jeschke, G., and Goldfarb, D. (2005) Distance measurements between, paramagnetic centers and a planar object by matrix Mims electron nuclear double resonance. J. Chem. Phys. 122, 024515.
    • (2005) J. Chem. Phys. , vol.122 , pp. 024515
    • Zanker, P.P.1    Jeschke, G.2    Goldfarb, D.3
  • 47
    • 0028349917 scopus 로고
    • Characterization of the active site of p21 ras by electron spin-echo envelope modulation spectroscopy with selective labeling: Comparisons between GDP and GTP forms
    • Halkides, C. J., Farrar, C. T., Larsen, R. G., Redfield A. G., and Singel, D. J. (1994) Characterization of the active site of p21 ras by electron spin-echo envelope modulation spectroscopy with selective labeling: comparisons between GDP and GTP forms. Biochemistry 33, 4019-4035.
    • (1994) Biochemistry , vol.33 , pp. 4019-4035
    • Halkides, C.J.1    Farrar, C.T.2    Larsen, R.G.3    Redfield, A.G.4    Singel, D.J.5
  • 50
    • 16544379913 scopus 로고    scopus 로고
    • Structural biology. Voltage sensor meets lipid membrane
    • MacKinnon, R. (2004) Structural biology. Voltage sensor meets lipid membrane. Science 306, 1304-1305.
    • (2004) Science , vol.306 , pp. 1304-1305
    • MacKinnon, R.1
  • 52
    • 33845637597 scopus 로고    scopus 로고
    • Phospholipids and the origin of cationic gating charges in voltage sensors
    • Schmidt, D., Jiang, Q. X., and MacKinnon, R. (2006) Phospholipids and the origin of cationic gating charges in voltage sensors. Nature 444, 775-779.
    • (2006) Nature , vol.444 , pp. 775-779
    • Schmidt, D.1    Jiang, Q.X.2    MacKinnon, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.