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Volumn 88, Issue 4, 2005, Pages 2954-2964

Light-induced relaxation of photolyzed carbonmonoxy myoglobin: A temperature-dependent x-ray absorption near-edge structure (XANES) study

Author keywords

[No Author keywords available]

Indexed keywords

CARBON MONOXIDE; CARBONMONOXYMYOGLOBIN; IRON; MYOGLOBIN; NITROGEN; POTASSIUM; UNCLASSIFIED DRUG;

EID: 22144487665     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.104.054973     Document Type: Article
Times cited : (35)

References (48)
  • 4
    • 0035406449 scopus 로고    scopus 로고
    • Geometrical fitting of experimental XANES spectra by a full multiple-scattering procedure
    • Benfatto, M., and S. Delia Longa. 2001. Geometrical fitting of experimental XANES spectra by a full multiple-scattering procedure. J. Synchr. Rad. 8:1087-1094.
    • (2001) J. Synchr. Rad. , vol.8 , pp. 1087-1094
    • Benfatto, M.1    Delia Longa, S.2
  • 6
    • 0025191367 scopus 로고
    • Temperature-derivative spectroscopy: A tool for protein dynamics
    • Berendzen, J., and D. Braunstein. 1990. Temperature-derivative spectroscopy: a tool for protein dynamics. Proc. Natl. Acad. Sci. USA. 87:1-5.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 1-5
    • Berendzen, J.1    Braunstein, D.2
  • 9
    • 0035146934 scopus 로고    scopus 로고
    • Nitric oxide, cytochrome-c oxidase and myoglobin
    • Brunori, M. 2001. Nitric oxide, cytochrome-c oxidase and myoglobin. Trends Biochem. Sci. 26:21-23.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 21-23
    • Brunori, M.1
  • 12
  • 15
    • 42749100563 scopus 로고    scopus 로고
    • Quantitative analysis of x-ray absorption near edge structure data by a full multiple scattering procedure: The Fe-CO geometry in photolyzed carbonmonoxy-myoglobin single crystal
    • Delia Longa, S., A. Arcovito, M. Girasole, J. L. Hazemann, and M. Benfatto. 2001. Quantitative analysis of x-ray absorption near edge structure data by a full multiple scattering procedure: the Fe-CO geometry in photolyzed carbonmonoxy-myoglobin single crystal. Phys. Rev. Lett. 87:15550-15551.
    • (2001) Phys. Rev. Lett. , vol.87 , pp. 15550-15551
    • Delia Longa, S.1    Arcovito, A.2    Girasole, M.3    Hazemann, J.L.4    Benfatto, M.5
  • 17
    • 0035957014 scopus 로고    scopus 로고
    • The role of structure, energy landscape, dynamics, and allostery in the enzymatic function of myoglobin
    • Frauenfelder, H., B. H. McMahon, R. H. Austin, K. Chu, and J. T. Groves. 2003. The role of structure, energy landscape, dynamics, and allostery in the enzymatic function of myoglobin. Proc. Natl. Acad. Sci. USA. 98:2370-2374.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 2370-2374
    • Frauenfelder, H.1    McMahon, B.H.2    Austin, R.H.3    Chu, K.4    Groves, J.T.5
  • 18
    • 0024316850 scopus 로고
    • Hemoproteins, ligands and quanta
    • Gibson, Q. H. 1989. Hemoproteins, ligands and quanta. J. Biol. Chem. 264:20155-20158.
    • (1989) J. Biol. Chem. , vol.264 , pp. 20155-20158
    • Gibson, Q.H.1
  • 19
    • 9644290699 scopus 로고    scopus 로고
    • Full quantitative multiple-scattering analysis of x-ray absorption spectra: Application to potassium ferro- and ferricyanide complexes
    • Hayakawa, K., K. Hatada. P. D'Angelo, S. Della Longa, C. R. Natoli, and M. Benfatto. 2004. Full quantitative multiple-scattering analysis of x-ray absorption spectra: application to potassium ferro- and ferricyanide complexes. J. Am. Chem. Soc. 126:15618-15623.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 15618-15623
    • Hayakawa, K.1    Hatada, K.2    D'Angelo, P.3    Della Longa, S.4    Natoli, C.R.5    Benfatto, M.6
  • 20
    • 36549095084 scopus 로고
    • Carbon K-shell electron energy loss spectra of 1- and 2-butenes, trans-1,3-butadiene and perfluoro-2-butene: Bond lengths from continuum shape resonances
    • Hitchcock, A. P., S. Beaulieu, T. Steel, J. Stohr, and F. Sette. 1984. Carbon K-shell electron energy loss spectra of 1- and 2-butenes, trans-1,3-butadiene and perfluoro-2-butene: bond lengths from continuum shape resonances. J. Chem. Phys. 80:3927-3935.
    • (1984) J. Chem. Phys. , vol.80 , pp. 3927-3935
    • Hitchcock, A.P.1    Beaulieu, S.2    Steel, T.3    Stohr, J.4    Sette, F.5
  • 21
    • 0016294586 scopus 로고
    • Low temperature photodissociation of hemoproteins: Carbon monoxide complex of myoglobin and hemoglobin
    • Iizuka, T., H. Yamamoto, M. Kotani, and T. Yonetani. 1974. Low temperature photodissociation of hemoproteins: carbon monoxide complex of myoglobin and hemoglobin. Biochim. Biophys. Acta. 371:126-139.
    • (1974) Biochim. Biophys. Acta , vol.371 , pp. 126-139
    • Iizuka, T.1    Yamamoto, H.2    Kotani, M.3    Yonetani, T.4
  • 22
    • 0033574735 scopus 로고    scopus 로고
    • A steric mechanism for inhibition of CO binding to heme proteins
    • Kachalova, G. S., A. N. Popov, and H. D. Bartunik. 1999. A steric mechanism for inhibition of CO binding to heme proteins. Science. 284:473-476.
    • (1999) Science , vol.284 , pp. 473-476
    • Kachalova, G.S.1    Popov, A.N.2    Bartunik, H.D.3
  • 23
    • 36949091243 scopus 로고
    • Structure of myoglobin: A three-dimensional Fourier synthesis at 2 Å resolution
    • Kendrew, J. C., R. E. Dickerson, B. E. Strandberg, R. G. Hart, and D. R. Davies. 1960. Structure of myoglobin: a three-dimensional Fourier synthesis at 2 Å resolution. Nature. 185:422-427.
    • (1960) Nature , vol.185 , pp. 422-427
    • Kendrew, J.C.1    Dickerson, R.E.2    Strandberg, B.E.3    Hart, R.G.4    Davies, D.R.5
  • 27
    • 0037023751 scopus 로고    scopus 로고
    • Structural dynamics of myoglobin: Ligand migration among protein cavities studied by Fourier transform infrared/temperature derivative spectroscopy
    • Lamb, D. C., K. Nienhaus, A. Arcovito, F. Draghi, A. E. Miele, M. Brunori, and G. U. Nienhaus. 2002. Structural dynamics of myoglobin: ligand migration among protein cavities studied by Fourier transform infrared/temperature derivative spectroscopy. J. Biol. Chem. 277:11636-11644.
    • (2002) J. Biol. Chem. , vol.277 , pp. 11636-11644
    • Lamb, D.C.1    Nienhaus, K.2    Arcovito, A.3    Draghi, F.4    Miele, A.E.5    Brunori, M.6    Nienhaus, G.U.7
  • 29
    • 0020126960 scopus 로고
    • X-ray absorption spectra: K-edges of 3D transition metals, L-edges of 3D and 4D metals and M-edges of palladium
    • Muller, J. E., O. Jepsen, and J. W. Wilkins. 1982. X-ray absorption spectra: K-edges of 3D transition metals, L-edges of 3D and 4D metals and M-edges of palladium. Solid State Commun. 42:365-368.
    • (1982) Solid State Commun. , vol.42 , pp. 365-368
    • Muller, J.E.1    Jepsen, O.2    Wilkins, J.W.3
  • 30
    • 0001940836 scopus 로고
    • A. Bianconi, L. Incoccia, and S. Stipcich, editors. Springer, Berlin, Germany
    • Natoli, C. R. 1983. EXAFS and Near Edge Structure. A. Bianconi, L. Incoccia, and S. Stipcich, editors. Springer, Berlin, Germany. 43-56.
    • (1983) EXAFS and Near Edge Structure , pp. 43-56
    • Natoli, C.R.1
  • 31
    • 0037208358 scopus 로고    scopus 로고
    • X-ray absorption spectroscopy in biological systems: State-of-the-art analysis
    • Natoli, C. R., M. Benfatto, S. Della Longa, and K. Hatada. 2003. X-ray absorption spectroscopy in biological systems: state-of-the-art analysis J. Synchr. Rad. 10:26-42.
    • (2003) J. Synchr. Rad. , vol.10 , pp. 26-42
    • Natoli, C.R.1    Benfatto, M.2    Della Longa, S.3    Hatada, K.4
  • 32
    • 0027992932 scopus 로고
    • Ligand binding to heme proteins: The effect of light on ligand binding in myoglobin
    • Nienhaus, G. U., J. R. Mourant, K. Chu, and H. Frauenfelder. 1994. Ligand binding to heme proteins: the effect of light on ligand binding in myoglobin. Biochemistry. 33:13413-13430.
    • (1994) Biochemistry , vol.33 , pp. 13413-13430
    • Nienhaus, G.U.1    Mourant, J.R.2    Chu, K.3    Frauenfelder, H.4
  • 33
    • 0032510808 scopus 로고    scopus 로고
    • Structural heterogeneity and ligand binding in carbonmonoxy myoglobin crystals at cryogenic temperatures
    • Nienhaus, G. U., K. Chu, and K. Jesse. 1998. Structural heterogeneity and ligand binding in carbonmonoxy myoglobin crystals at cryogenic temperatures. Biochemistry. 37:6819-6823.
    • (1998) Biochemistry , vol.37 , pp. 6819-6823
    • Nienhaus, G.U.1    Chu, K.2    Jesse, K.3
  • 34
    • 0036157060 scopus 로고    scopus 로고
    • The effect of ligand dynamics on heme electronic transition band III in myoglobin
    • Nienhaus, K., D. C. Lamb, P. Deng, and G. U. Nienhaus. 2002. The effect of ligand dynamics on heme electronic transition band III in myoglobin. Biophys. J. 82:1059-1067.
    • (2002) Biophys. J. , vol.82 , pp. 1059-1067
    • Nienhaus, K.1    Lamb, D.C.2    Deng, P.3    Nienhaus, G.U.4
  • 35
    • 0042242570 scopus 로고    scopus 로고
    • Structural dynamics of myoglobin: Spectroscopic and structural characterization of ligand docking sites in myoglobin mutant L29W
    • Nienhaus, K., P. Deng, J. M. Kriegl, and G. U. Nienhaus. 2003a. Structural dynamics of myoglobin: spectroscopic and structural characterization of ligand docking sites in myoglobin mutant L29W. Biochemistry. 42:9633-9646.
    • (2003) Biochemistry , vol.42 , pp. 9633-9646
    • Nienhaus, K.1    Deng, P.2    Kriegl, J.M.3    Nienhaus, G.U.4
  • 36
    • 0041742184 scopus 로고    scopus 로고
    • Structural dynamics of myoglobin: The effect of internal cavities on ligand migration and binding
    • Nienhaus, K., P. Deng, J. M. Kriegl, and G. U. Nienhaus. 2003b. Structural dynamics of myoglobin: the effect of internal cavities on ligand migration and binding. Biochemistry. 42:9647-9658.
    • (2003) Biochemistry , vol.42 , pp. 9647-9658
    • Nienhaus, K.1    Deng, P.2    Kriegl, J.M.3    Nienhaus, G.U.4
  • 37
    • 0142242162 scopus 로고    scopus 로고
    • Structural dynamics of myoglobin: Ligand migration and binding in Valine-68 mutants
    • Nienhaus, K., P. Deng, J. S. Olson, J. J. Warren, and G. U. Nienhaus. 2003c. Structural dynamics of myoglobin: ligand migration and binding in Valine-68 mutants. J. Biol. Chem. 278:42532-42544.
    • (2003) J. Biol. Chem. , vol.278 , pp. 42532-42544
    • Nienhaus, K.1    Deng, P.2    Olson, J.S.3    Warren, J.J.4    Nienhaus, G.U.5
  • 38
    • 0034624691 scopus 로고    scopus 로고
    • Ligand binding and conformational motions in myoglobin
    • Ostermann, A., R. Waschipky, F. G. Parak, and G. U. Nienhaus. 2000. Ligand binding and conformational motions in myoglobin. Nature. 404:205-208.
    • (2000) Nature , vol.404 , pp. 205-208
    • Ostermann, A.1    Waschipky, R.2    Parak, F.G.3    Nienhaus, G.U.4
  • 39
    • 0025734848 scopus 로고
    • Ligand binding and protein relaxation in heme proteins: A room temperature analysis of NO geminate recombination
    • Petrich, J. W., J. C. Lambry, K. Kuczera, M. Karplus, C. Poyart, and J. L. Martin. 1991. Ligand binding and protein relaxation in heme proteins: a room temperature analysis of NO geminate recombination. Biochemistry. 30:3975-3987.
    • (1991) Biochemistry , vol.30 , pp. 3975-3987
    • Petrich, J.W.1    Lambry, J.C.2    Kuczera, K.3    Karplus, M.4    Poyart, C.5    Martin, J.L.6
  • 40
  • 42
    • 0030768765 scopus 로고    scopus 로고
    • Ligand migration in sperm whale myoglobin
    • Scott, E. E., and Q. H. Gibson. 1997. Ligand migration in sperm whale myoglobin. Biochemistry. 36:11909-11917.
    • (1997) Biochemistry , vol.36 , pp. 11909-11917
    • Scott, E.E.1    Gibson, Q.H.2
  • 45
    • 0035923445 scopus 로고    scopus 로고
    • Protein conformational relaxation and ligand migration in myoglobin: A nanosecond to millisecond molecular movie from time-resolved Laue x-ray diffraction
    • Srajer, V., Z. Ren, T. Y. Teng, M. Schmidt, T. Ursby, D. Bourgeois, C. Pradervand, W. Schildkamp, M. Wulff, and K. Moffat. 2001. Protein conformational relaxation and ligand migration in myoglobin: a nanosecond to millisecond molecular movie from time-resolved Laue x-ray diffraction. Biochemistry. 40:13802-13815.
    • (2001) Biochemistry , vol.40 , pp. 13802-13815
    • Srajer, V.1    Ren, Z.2    Teng, T.Y.3    Schmidt, M.4    Ursby, T.5    Bourgeois, D.6    Pradervand, C.7    Schildkamp, W.8    Wulff, M.9    Moffat, K.10
  • 46
    • 0023657037 scopus 로고
    • 5 K extended x-ray absorption fine structure and 40 K 10-s resolved extended x-ray absorption finen structure studies of photolyzed carboxymyoglobin
    • Teng, T.-Y., H. W. Huang, and G. A. Olah. 1987. 5 K extended x-ray absorption fine structure and 40 K 10-s resolved extended x-ray absorption finen structure studies of photolyzed carboxymyoglobin. Biochemistry. 26:8066-8077.
    • (1987) Biochemistry , vol.26 , pp. 8066-8077
    • Teng, T.-Y.1    Huang, H.W.2    Olah, G.A.3
  • 47
    • 0030821996 scopus 로고    scopus 로고
    • Initial trajectory of carbon monoxide after photodissociation from myoglobin at cryogenic temperatures
    • Teng, T.-Y., V. Srajer, and K. Moffat. 1997. Initial trajectory of carbon monoxide after photodissociation from myoglobin at cryogenic temperatures. Biochemistry. 36:12087-12100.
    • (1997) Biochemistry , vol.36 , pp. 12087-12100
    • Teng, T.-Y.1    Srajer, V.2    Moffat, K.3
  • 48


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