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Volumn 78, Issue 3, 2000, Pages 1531-1540

Structural changes of the sarcoplasmic reticulum Ca2+-ATPase upon nucleotide binding studied by Fourier transform infrared spectroscopy

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE PHOSPHATE; ADENOSINE TRIPHOSPHATASE (CALCIUM); ADENOSINE TRIPHOSPHATE; ARGININE KINASE; ASPARTIC ACID; CREATINE KINASE; GLUTAMIC ACID; NUCLEOTIDE; PROTEIN P21;

EID: 0034008797     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(00)76705-1     Document Type: Article
Times cited : (40)

References (42)
  • 2
    • 0029565489 scopus 로고
    • 2+-ATPase by site-directed mutagenesis
    • 2+-ATPase by site-directed mutagenesis. Biosci. Rep. 15:243-261.
    • (1995) Biosci. Rep. , vol.15 , pp. 243-261
    • Andersen, J.P.1
  • 3
    • 0027354020 scopus 로고
    • Quantitative studies of the structure of proteins in solution by Fourier-transform infrared spectroscopy
    • Arrondo, J. L. R., A. Muga, J. Castresana, and F. M. Goni. 1993. Quantitative studies of the structure of proteins in solution by Fourier-transform infrared spectroscopy. Prog. Biophys. Mol. Biol. 59:23-56.
    • (1993) Prog. Biophys. Mol. Biol. , vol.59 , pp. 23-56
    • Arrondo, J.L.R.1    Muga, A.2    Castresana, J.3    Goni, F.M.4
  • 4
    • 0030949448 scopus 로고    scopus 로고
    • Time-resolved infrared spectroscopy of intermediates and products from photolysis of 1-(2-nitrophenyl)ethyl phosphates: Reaction of the 2-nitrosoacetophenone byproduct with thiols
    • Barth, A., J. E. T. Corrie, M. J. Gradwell, Y. Maeda, W. Mäntele, T. Meier, and D. R. Trentham. 1997. Time-resolved infrared spectroscopy of intermediates and products from photolysis of 1-(2-nitrophenyl)ethyl phosphates: reaction of the 2-nitrosoacetophenone byproduct with thiols. J. Am. Chem. Soc. 119:4149-4159.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 4149-4159
    • Barth, A.1    Corrie, J.E.T.2    Gradwell, M.J.3    Maeda, Y.4    Mäntele, W.5    Meier, T.6    Trentham, D.R.7
  • 6
    • 0028864590 scopus 로고
    • Photochemical release of ATP from "caged ATP" studied by time-resolved infrared spectroscopy
    • Barth, A., K. Hauser, W. Mäntele, J. E. T. Corrie, and D. R. Trentham. 1995. Photochemical release of ATP from "caged ATP" studied by time-resolved infrared spectroscopy. J. Am. Chem. Soc. 117: 10311-10316.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 10311-10316
    • Barth, A.1    Hauser, K.2    Mäntele, W.3    Corrie, J.E.T.4    Trentham, D.R.5
  • 7
    • 0344653650 scopus 로고    scopus 로고
    • 2+-ATPase: Molecular interpretation of infrared difference spectra
    • 2+-ATPase: molecular interpretation of infrared difference spectra. Biophys. J. 75:538-544.
    • (1998) Biophys. J. , vol.75 , pp. 538-544
    • Barth, A.1    Mäntele, W.2
  • 8
    • 0026030935 scopus 로고
    • Infrared spectroscopic signals arising from ligand binding and conformational changes in the catalytic cycle of sarcoplasmic reticulum ATPase
    • Barth, A., W. Mäntele, and W. Kreutz. 1991. Infrared spectroscopic signals arising from ligand binding and conformational changes in the catalytic cycle of sarcoplasmic reticulum ATPase. Biochim. Biophys. Acta. 1057: 115-123.
    • (1991) Biochim. Biophys. Acta , vol.1057 , pp. 115-123
    • Barth, A.1    Mäntele, W.2    Kreutz, W.3
  • 10
    • 0016797947 scopus 로고
    • Estimation of amino acid residue side-chain absorption in the infrared spectra of protein solutions in heavy water
    • Chirgadze, Y. N., O. V. Fedorov, and N. P. Trushina. 1975. Estimation of amino acid residue side-chain absorption in the infrared spectra of protein solutions in heavy water. Biopolymers. 14:679-694.
    • (1975) Biopolymers , vol.14 , pp. 679-694
    • Chirgadze, Y.N.1    Fedorov, O.V.2    Trushina, N.P.3
  • 13
    • 0015218365 scopus 로고
    • Acetyl phosphate as substrate for calcium uptake in skeletal muscle microsomes
    • de Meis, L., and W. Hasselbach. 1971. Acetyl phosphate as substrate for calcium uptake in skeletal muscle microsomes. J. Biol. Chem. 246: 4759-4763.
    • (1971) J. Biol. Chem. , vol.246 , pp. 4759-4763
    • De Meis, L.1    Hasselbach, W.2
  • 14
    • 0018401053 scopus 로고
    • Energy interconversion by the Ca-dependent ATPase of the sarcoplasmic reticulum
    • de Meis, L., and A. Vianna. 1979. Energy interconversion by the Ca-dependent ATPase of the sarcoplasmic reticulum. Annu. Rev. Biochem. 48:275-292.
    • (1979) Annu. Rev. Biochem. , vol.48 , pp. 275-292
    • De Meis, L.1    Vianna, A.2
  • 15
    • 0023054728 scopus 로고
    • Fourier transform infrared difference spectroscopy of bacteriorhodopsin and 1st photoproducts regenerated with deuterated tyrosine
    • Dollinger, G., L. Eisenstein, L. Shuo-Liang, K. Nakanishi, and J. Termini. 1986. Fourier transform infrared difference spectroscopy of bacteriorhodopsin and 1st photoproducts regenerated with deuterated tyrosine. Biochemistry. 25:6524-6533.
    • (1986) Biochemistry , vol.25 , pp. 6524-6533
    • Dollinger, G.1    Eisenstein, L.2    Shuo-Liang, L.3    Nakanishi, K.4    Termini, J.5
  • 16
    • 0028120538 scopus 로고
    • Impact of point mutations on the structure and thermal stability of ribonuclease T1 in aqueous solution probed by Fourier transform infrared spectroscopy
    • Fabian, H., C. Schultz, J. Backmann, U. Hahn, W. Saenger, H. H. Mantsch, and D. Naumann. 1994. Impact of point mutations on the structure and thermal stability of ribonuclease T1 in aqueous solution probed by Fourier transform infrared spectroscopy. Biochemistry. 33: 10725-10730.
    • (1994) Biochemistry , vol.33 , pp. 10725-10730
    • Fabian, H.1    Schultz, C.2    Backmann, J.3    Hahn, U.4    Saenger, W.5    Mantsch, H.H.6    Naumann, D.7
  • 18
    • 0000461713 scopus 로고
    • Kinetic regulation of catalytic and transport activities in sarcoplasmic reticulum ATPase
    • A. N. Martonosi, editor. Plenum Press, New York
    • Inesi, G., and L. de Meis. 1985. Kinetic regulation of catalytic and transport activities in sarcoplasmic reticulum ATPase. In The Enzymes of Biological Membranes, Vol. 3. A. N. Martonosi, editor. Plenum Press, New York. 157-191.
    • (1985) The Enzymes of Biological Membranes , vol.3 , pp. 157-191
    • Inesi, G.1    De Meis, L.2
  • 19
    • 0343919892 scopus 로고
    • Kinetic isotope effects
    • Longman, Harlow, UK
    • Isaacs, N. S. 1987. Kinetic isotope effects. In Physical Organic Chemistry. Longman, Harlow, UK. 255-281.
    • (1987) Physical Organic Chemistry , pp. 255-281
    • Isaacs, N.S.1
  • 21
    • 0007843909 scopus 로고
    • Beiträge zur kenntnis der monoamido- und diamidophosphorsäure
    • Klement, R., G. Biberacher, and V. Hille. 1957. Beiträge zur Kenntnis der Monoamido- und Diamidophosphorsäure. Z Anorg. Chem. 289:80-89.
    • (1957) Z Anorg. Chem. , vol.289 , pp. 80-89
    • Klement, R.1    Biberacher, G.2    Hille, V.3
  • 22
    • 0001159016 scopus 로고
    • Imidodiphosphate and pyrophosphate: Possible biological significance of similar structures
    • Larsen, M., R. Willett, and R. G. Yount. 1969. Imidodiphosphate and pyrophosphate: possible biological significance of similar structures. Science. 166:1510-1511.
    • (1969) Science , vol.166 , pp. 1510-1511
    • Larsen, M.1    Willett, R.2    Yount, R.G.3
  • 23
    • 0002440989 scopus 로고
    • Etude par spectromérie i. r. et Raman de l'indole et de l'indolizine. Liaison hydrogène NH⋯π*
    • Lautie, A., M. F. Lautie, A. Gruger, and S. A. Fakhri. 1980. Etude par spectromérie i. r. et Raman de l'indole et de l'indolizine. Liaison hydrogène NH⋯π*. Spectrochim. Acta. A36:85-94.
    • (1980) Spectrochim. Acta , vol.A36 , pp. 85-94
    • Lautie, A.1    Lautie, M.F.2    Gruger, A.3    Fakhri, S.A.4
  • 26
    • 77956813361 scopus 로고
    • 2+ transport ATPases of sarco(endo)plasmic reticulum and plasma membranes
    • J. J. H. H. M. DePont, editor. Elsevier Science Publishers, Amsterdam
    • 2+ transport ATPases of sarco(endo)plasmic reticulum and plasma membranes. In Molecular Aspects of Transport Proteins, Vol. 21. J. J. H. H. M. DePont, editor. Elsevier Science Publishers, Amsterdam. 57-116.
    • (1992) Molecular Aspects of Transport Proteins , vol.21 , pp. 57-116
    • Martonosi, A.1
  • 27
    • 0029940235 scopus 로고
    • Structural organization, ion transport, and energy transduction of P-type ATPases
    • Møller, J. V., B. Juul, and M. le Maire. 1995. Structural organization, ion transport, and energy transduction of P-type ATPases. Biochim. Biophys. Acta. 1286:1-51.
    • (1995) Biochim. Biophys. Acta , vol.1286 , pp. 1-51
    • Møller, J.V.1    Juul, B.2    Le Maire, M.3
  • 28
    • 0031469584 scopus 로고    scopus 로고
    • Nucleotide binding to Na,K-ATPase. Effect of ionic strength and charge
    • Nørby, J. G., and M. Esmann. 1997. Nucleotide binding to Na,K-ATPase. Effect of ionic strength and charge. Ann. NY Acad. Sci. 834:410-411.
    • (1997) Ann. NY Acad. Sci. , vol.834 , pp. 410-411
    • Nørby, J.G.1    Esmann, M.2
  • 29
    • 0025310575 scopus 로고
    • Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35 Å resolution: Implications for the mechanism of GTP hydrolysis
    • Pai, E. F., U. Krengel, G. A. Petsko, R. S. Goody, W. Kabsch, and A. Wittinghofer. 1990. Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35 Å resolution: implications for the mechanism of GTP hydrolysis. EMBO J. 9:2351-2359.
    • (1990) EMBO J. , vol.9 , pp. 2351-2359
    • Pai, E.F.1    Krengel, U.2    Petsko, G.A.3    Goody, R.S.4    Kabsch, W.5    Wittinghofer, A.6
  • 30
    • 0021357835 scopus 로고
    • Energetics of the calcium-transporting ATPase
    • Pickart, C. M., and W. P. Jencks. 1984. Energetics of the calcium-transporting ATPase. J. Biol. Chem. 259:1629-1643.
    • (1984) J. Biol. Chem. , vol.259 , pp. 1629-1643
    • Pickart, C.M.1    Jencks, W.P.2
  • 31
    • 0031045929 scopus 로고    scopus 로고
    • Conformational changes of arginine kinase induced by photochemical release of nucleotides from caged nucleotides. An infrared difference-spectroscopy investigation
    • Raimbault, C., F. Besson, and R. Buchet. 1997. Conformational changes of arginine kinase induced by photochemical release of nucleotides from caged nucleotides. An infrared difference-spectroscopy investigation. Eur. J. Biochem. 244:343-351.
    • (1997) Eur. J. Biochem. , vol.244 , pp. 343-351
    • Raimbault, C.1    Besson, F.2    Buchet, R.3
  • 32
    • 0029820647 scopus 로고    scopus 로고
    • Changes of creatine kinase secondary structure induced by the release of nucleotides from caged compounds. An infrared difference-spectroscopy study
    • Raimbault, C., R. Buchet, and C. Vial. 1996. Changes of creatine kinase secondary structure induced by the release of nucleotides from caged compounds. An infrared difference-spectroscopy study. Eur. J. Biochem. 240:134-142.
    • (1996) Eur. J. Biochem. , vol.240 , pp. 134-142
    • Raimbault, C.1    Buchet, R.2    Vial, C.3
  • 34
    • 0002548426 scopus 로고
    • Structures and conformational properties of bases, furanose sugars, and phosphate groups
    • C. R. Cantor, editor. Springer-Verlag, New York, Berlin, Heidelberg, Tokyo
    • Saenger, W. 1984. Structures and conformational properties of bases, furanose sugars, and phosphate groups. In Principles of Nucleic Acid Structure. C. R. Cantor, editor. Springer-Verlag, New York, Berlin, Heidelberg, Tokyo. 51-104.
    • (1984) Principles of Nucleic Acid Structure , pp. 51-104
    • Saenger, W.1
  • 35
    • 0001573755 scopus 로고
    • Vibrational spectra and normal coordinate analysis of p-cresol and 1st deuterated analogs
    • Takeuchi, H., N. Watanabe, and I. Harada. 1988. Vibrational spectra and normal coordinate analysis of p-cresol and 1st deuterated analogs. Spectrochim. Acta A. 44:749-761.
    • (1988) Spectrochim. Acta A. , vol.44 , pp. 749-761
    • Takeuchi, H.1    Watanabe, N.2    Harada, I.3
  • 36
    • 0019877491 scopus 로고
    • Sarcoplasmic reticulum ATPase catalyzes hydolysis of adenyl-5′-yl imidodiphosphate
    • Taylor, J. S. 1981. Sarcoplasmic reticulum ATPase catalyzes hydolysis of adenyl-5′-yl imidodiphosphate. J. Biol. Chem. 256:9793-9795.
    • (1981) J. Biol. Chem. , vol.256 , pp. 9793-9795
    • Taylor, J.S.1
  • 37
    • 0003039165 scopus 로고
    • Infrared and Raman spectra of nucleic acids - Vibrations in the base-residues
    • J. Duchesne, editor. Academic Press, San Diego
    • Tsuboi, M., and S. Takahashi. 1973. Infrared and Raman spectra of nucleic acids - vibrations in the base-residues. In Physico-Chemical Properties of Nucleic Acids, Vol. II. J. Duchesne, editor. Academic Press, San Diego. 91-145.
    • (1973) Physico-chemical Properties of Nucleic Acids , vol.2 , pp. 91-145
    • Tsuboi, M.1    Takahashi, S.2
  • 38
    • 0025613794 scopus 로고
    • 2O) solutions. I. Spectral parameters of amino acid residue absorption bands
    • 2O) solutions. I. Spectral parameters of amino acid residue absorption bands. Biopolymers. 30: 1243-1257.
    • (1990) Biopolymers , vol.30 , pp. 1243-1257
    • Venyaminov, S.Y.1    Kalnin, N.N.2
  • 40
    • 0025740753 scopus 로고
    • The structure of Ras protein: A model for a universal molecular switch
    • Wittinghofer, A., and E. F. Pai. 1991. The structure of Ras protein: a model for a universal molecular switch. Trends Biochem. Sci. 16:382-387.
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 382-387
    • Wittinghofer, A.1    Pai, E.F.2
  • 41
    • 0015236388 scopus 로고
    • Adenylyl imidodiphosphate, an adenosine triphosphate analog containing a P-N-P linkage
    • Yount, R. G., D. Babcock, W. Ballantyne, and D. Ojala. 1971. Adenylyl imidodiphosphate, an adenosine triphosphate analog containing a P-N-P linkage. Biochemistry. 10:2484-2489.
    • (1971) Biochemistry , vol.10 , pp. 2484-2489
    • Yount, R.G.1    Babcock, D.2    Ballantyne, W.3    Ojala, D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.