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Volumn 47, Issue 48, 2008, Pages 12869-12877

Resonance Raman interrogation of the consequences of heme rotational disorder in myoglobin and its ligated derivatives

Author keywords

[No Author keywords available]

Indexed keywords

CYANIDES; DEUTERIUM; HEMOGLOBIN; HYDROCARBONS; PORPHYRINS; RESONANCE; SPECTRUM ANALYSIS;

EID: 57049112699     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi801779d     Document Type: Article
Times cited : (22)

References (54)
  • 1
    • 0001165867 scopus 로고    scopus 로고
    • Nuclear magnetic resonance of hemoproteins
    • Kadish, K. M, Smith, K. M, and Guilard, R, Eds, Academic Press, New York
    • La Mar, G. N., Satterlee, J. D., and De Ropp, J. S. (2000) Nuclear magnetic resonance of hemoproteins. In Porphyrin Handbook (Kadish, K. M., Smith, K. M., and Guilard, R., Eds.) Vol. 5, pp 185-298, Academic Press, New York.
    • (2000) Porphyrin Handbook , vol.5 , pp. 185-298
    • La Mar, G.N.1    Satterlee, J.D.2    De Ropp, J.S.3
  • 2
    • 0021112460 scopus 로고
    • Heme orientational disorder in reconstituted and native sperm whale myoglobin. Proton nuclear magnetic resonance characterizations by heme methyl deuterium labeling in the metcyano protein
    • La Mar, G. N., Davis, N. L., Parish, D. W., and Smith, K. M. (1983) Heme orientational disorder in reconstituted and native sperm whale myoglobin. Proton nuclear magnetic resonance characterizations by heme methyl deuterium labeling in the metcyano protein. J. Mol. Biol. 168, 887-896.
    • (1983) J. Mol. Biol , vol.168 , pp. 887-896
    • La Mar, G.N.1    Davis, N.L.2    Parish, D.W.3    Smith, K.M.4
  • 3
    • 0000836440 scopus 로고
    • Proton NMR study of the mechanism of the heme-apoprotein reaction for myoglobin
    • Jue, T., Krishnamoorthi, R., and La Mar, G. N. (1983) Proton NMR study of the mechanism of the heme-apoprotein reaction for myoglobin. J. Am. Chem. Soc. 105, 5701-5703.
    • (1983) J. Am. Chem. Soc , vol.105 , pp. 5701-5703
    • Jue, T.1    Krishnamoorthi, R.2    La Mar, G.N.3
  • 4
    • 0000380550 scopus 로고
    • Proton NMR investigation of the rate and mechanism of heme rotation in sperm whale myoglobin: Evidence for intramolecular reorientation about a heme two-fold axis
    • La Mar, G. N., Toi, H., and Krishnamoorthi, R. (1984) Proton NMR investigation of the rate and mechanism of heme rotation in sperm whale myoglobin: Evidence for intramolecular reorientation about a heme two-fold axis. J. Am. Chem. Soc. 106, 6395-6401.
    • (1984) J. Am. Chem. Soc , vol.106 , pp. 6395-6401
    • La Mar, G.N.1    Toi, H.2    Krishnamoorthi, R.3
  • 5
    • 0022427462 scopus 로고
    • Proton NMR characterization of metastable and equilibrium heme orientational heterogeneity in reconstituted and native human hemoglobin
    • La Mar, G. N., Yamamoto, Y., Jue, T., Smith, K. M., and Pandey, R. K. (1985) Proton NMR characterization of metastable and equilibrium heme orientational heterogeneity in reconstituted and native human hemoglobin. Biochemistry 24, 3826-3831.
    • (1985) Biochemistry , vol.24 , pp. 3826-3831
    • La Mar, G.N.1    Yamamoto, Y.2    Jue, T.3    Smith, K.M.4    Pandey, R.K.5
  • 6
    • 0023656040 scopus 로고
    • Heme disorder in two myoglobins: Comparison of reorientation rate
    • Bellelli, A., Foon, R., Ascoli, F., and Brunori, M. (1987) Heme disorder in two myoglobins: Comparison of reorientation rate. Biochem. J. 246, 787-789.
    • (1987) Biochem. J , vol.246 , pp. 787-789
    • Bellelli, A.1    Foon, R.2    Ascoli, F.3    Brunori, M.4
  • 7
    • 0000789217 scopus 로고
    • Proton nuclear magnetic resonance investigation of the mechanism of the reconstitution of myoglobin that leads to metastable heme orientational disorder
    • La Mar, G. N., Pande, U., Hauksson, J. B., Pandey, R. K., and Smith, K. M. (1989) Proton nuclear magnetic resonance investigation of the mechanism of the reconstitution of myoglobin that leads to metastable heme orientational disorder. J. Am. Chem. Soc. 111, 485-491.
    • (1989) J. Am. Chem. Soc , vol.111 , pp. 485-491
    • La Mar, G.N.1    Pande, U.2    Hauksson, J.B.3    Pandey, R.K.4    Smith, K.M.5
  • 8
    • 0038682731 scopus 로고    scopus 로고
    • 1H NMR characterization of equilibrium heme orientational disorder with functional consequences in mouse neuroglobin
    • 1H NMR characterization of equilibrium heme orientational disorder with functional consequences in mouse neuroglobin. J. Am. Chem. Soc. 125, 8080-8081.
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 8080-8081
    • Du, W.1    Syvitski, R.2    Dewilde, S.3    Moens, L.4    La Mar, G.N.5
  • 9
    • 0032506292 scopus 로고    scopus 로고
    • 1H-NMR investigation of the influence of the heme orientation on functional properties of myoglobin
    • 1H-NMR investigation of the influence of the heme orientation on functional properties of myoglobin. Biochim. Biophys. Acta 388, 349-362.
    • (1998) Biochim. Biophys. Acta , vol.388 , pp. 349-362
    • Yamamoto, Y.1    Nakashima, T.2    Kawano, E.3    Chujo, R.4
  • 10
    • 0010394777 scopus 로고    scopus 로고
    • Functional and structural consequences of heme orientational disorder in myoglobin
    • Yamamoto, Y., and Kawano, E. (1997) Functional and structural consequences of heme orientational disorder in myoglobin. J. Inorg. Biochem. 67, 119.
    • (1997) J. Inorg. Biochem , vol.67 , pp. 119
    • Yamamoto, Y.1    Kawano, E.2
  • 11
    • 0037012419 scopus 로고    scopus 로고
    • Heme Distortions in Sperm-Whale Carbonmonoxy Myoglobin: Correlations between Rotational Strengths and Heme Distortions in MD-Generated Structures
    • Kiefl, C., Sreerama, N., Haddad, R., Sun, L., Jentzen, W., Lu, Y., Qiu, Y., Shelnutt, J. A., and Woody, R. W. (2002) Heme Distortions in Sperm-Whale Carbonmonoxy Myoglobin: Correlations between Rotational Strengths and Heme Distortions in MD-Generated Structures. J. Am. Chem. Soc. 124, 3385-3394.
    • (2002) J. Am. Chem. Soc , vol.124 , pp. 3385-3394
    • Kiefl, C.1    Sreerama, N.2    Haddad, R.3    Sun, L.4    Jentzen, W.5    Lu, Y.6    Qiu, Y.7    Shelnutt, J.A.8    Woody, R.W.9
  • 12
    • 0023040250 scopus 로고
    • Bohr effect in monomelic insect hemoglobins controlled by oxygen off-rate and modulated by heme-rotational disorder
    • Gersonde, K., Sick, H., Overkamp, M., Smith, K. M., and Parish, D. W. (1986) Bohr effect in monomelic insect hemoglobins controlled by oxygen off-rate and modulated by heme-rotational disorder. Eur. J. Biochem. 157, 393-404.
    • (1986) Eur. J. Biochem , vol.157 , pp. 393-404
    • Gersonde, K.1    Sick, H.2    Overkamp, M.3    Smith, K.M.4    Parish, D.W.5
  • 13
  • 14
    • 38849152184 scopus 로고    scopus 로고
    • Effect of Reversed Heme Orientation on Circular Dichroism and Cooperative Oxygen Binding of Human Adult Hemoglobin
    • Nagai, M., Nagai, Y., Aki, Y., Imai, K., Wada, Y., Nagatomo, S., and Yamamoto, Y. (2008) Effect of Reversed Heme Orientation on Circular Dichroism and Cooperative Oxygen Binding of Human Adult Hemoglobin. Biochemistry 47, 517-525.
    • (2008) Biochemistry , vol.47 , pp. 517-525
    • Nagai, M.1    Nagai, Y.2    Aki, Y.3    Imai, K.4    Wada, Y.5    Nagatomo, S.6    Yamamoto, Y.7
  • 15
    • 0001520987 scopus 로고
    • Influence of heme orientation on oxygen affinity in native sperm whale myoglobin
    • Livingston, D. J., Davis, N. L., La Mar, G. N., and Brown, W. D. (1984) Influence of heme orientation on oxygen affinity in native sperm whale myoglobin. J. Am. Chem. Soc. 106, 3025-3026.
    • (1984) J. Am. Chem. Soc , vol.106 , pp. 3025-3026
    • Livingston, D.J.1    Davis, N.L.2    La Mar, G.N.3    Brown, W.D.4
  • 16
    • 0023108441 scopus 로고
    • Functional effects of heme orientational disorder in sperm whale myoglobin
    • Light, W. R., Rohlfs, R. J., Palmer, G., and Olson, J. S. (1987) Functional effects of heme orientational disorder in sperm whale myoglobin. J. Biol. Chem. 262, 46-52.
    • (1987) J. Biol. Chem , vol.262 , pp. 46-52
    • Light, W.R.1    Rohlfs, R.J.2    Palmer, G.3    Olson, J.S.4
  • 17
    • 0023100151 scopus 로고
    • Functional consequences of haem orientational disorder in sperm-whale and yellow-fin-tuna myoglobins
    • Aojula, H. S., Wilson, M. T., and Morrison, I. G. (1987) Functional consequences of haem orientational disorder in sperm-whale and yellow-fin-tuna myoglobins. Biochem. J. 243, 205-210.
    • (1987) Biochem. J , vol.243 , pp. 205-210
    • Aojula, H.S.1    Wilson, M.T.2    Morrison, I.G.3
  • 18
    • 0021777960 scopus 로고
    • Resonance Raman spectroscopy as a probe of heme protein structure and dynamics
    • Spiro, T. G. (1985) Resonance Raman spectroscopy as a probe of heme protein structure and dynamics. Adv. Protein Chem. 37, 111-159.
    • (1985) Adv. Protein Chem , vol.37 , pp. 111-159
    • Spiro, T.G.1
  • 19
    • 0000740326 scopus 로고    scopus 로고
    • Resonance Raman spectra of heme proteins and model compounds
    • Kadish, K. M, Smith, K. M, and Guilard, R, Eds, Academic Press, New York
    • Kincaid, J. R. (2000) Resonance Raman spectra of heme proteins and model compounds. In Porphyrin Handbook (Kadish, K. M., Smith, K. M., and Guilard, R., Eds.) Vol. 7, pp 225-291, Academic Press, New York.
    • (2000) Porphyrin Handbook , vol.7 , pp. 225-291
    • Kincaid, J.R.1
  • 20
    • 0016400375 scopus 로고
    • Resonance Raman spectra of heme proteins. Effects of oxidation and spin state
    • Spiro, T. G., and Strekas, T. C. (1974) Resonance Raman spectra of heme proteins. Effects of oxidation and spin state. J. Am. Chem. Soc. 96, 338-345.
    • (1974) J. Am. Chem. Soc , vol.96 , pp. 338-345
    • Spiro, T.G.1    Strekas, T.C.2
  • 21
    • 0002052550 scopus 로고
    • The heme protein structure and the iron histidine stretching mode
    • Spiro, T. G, Ed, Wiley & Sons, New York
    • Kitagawa, T. (1988) The heme protein structure and the iron histidine stretching mode. In Biological Applications of Raman Spectroscopy (Spiro, T. G., Ed.) Vol. 3, pp 97-131, Wiley & Sons, New York.
    • (1988) Biological Applications of Raman Spectroscopy , vol.3 , pp. 97-131
    • Kitagawa, T.1
  • 22
    • 0027096191 scopus 로고
    • Hydrogen bonding of iron-coordinated histidine in heme proteins
    • Rousseau, D. G., and Rousseau, D. L. (1992) Hydrogen bonding of iron-coordinated histidine in heme proteins. J. Struct. Biol. 109, 13-17.
    • (1992) J. Struct. Biol , vol.109 , pp. 13-17
    • Rousseau, D.G.1    Rousseau, D.L.2
  • 23
    • 57049084592 scopus 로고    scopus 로고
    • - and NO. In Biological Applications of Raman Spectroscopy (Spiro, T. G., Ed.) 3, pp 39-95, Wiley & Sons, New York.
    • - and NO. In Biological Applications of Raman Spectroscopy (Spiro, T. G., Ed.) Vol. 3, pp 39-95, Wiley & Sons, New York.
  • 24
    • 0000732729 scopus 로고    scopus 로고
    • Resonance Raman scattering: A probe of heme protein-bound nitric oxide
    • Feelisch, M, and Stamler, J, Eds, pp, Wiley & Sons, New York
    • Wang, J., Caughey, W. S., and Rousseau, D. L. (1996) Resonance Raman scattering: A probe of heme protein-bound nitric oxide. In Methods in Nitric Oxide Research (Feelisch, M., and Stamler, J., Eds.) pp 427-454, Wiley & Sons, New York.
    • (1996) Methods in Nitric Oxide Research , pp. 427-454
    • Wang, J.1    Caughey, W.S.2    Rousseau, D.L.3
  • 25
    • 38949111373 scopus 로고    scopus 로고
    • The impact of altered protein-heme interactions on the resonance Raman spectra of heme proteins. Studies of heme rotational disorder
    • Rwere, F., Mak, P. J., and Kincaid, J. R. (2008) The impact of altered protein-heme interactions on the resonance Raman spectra of heme proteins. Studies of heme rotational disorder. Biopolymers 89, 179-186.
    • (2008) Biopolymers , vol.89 , pp. 179-186
    • Rwere, F.1    Mak, P.J.2    Kincaid, J.R.3
  • 26
    • 0003466782 scopus 로고
    • Rapid base-catalyzed deuterium exchange at the ring-adjacent methyl and methylene positions of octaalkyl and natural-derivative porphyrins and metalloporphyrins
    • Godziela, G. M., Kramer, S. K., and Goff, H. M. (1986) Rapid base-catalyzed deuterium exchange at the ring-adjacent methyl and methylene positions of octaalkyl and natural-derivative porphyrins and metalloporphyrins. Inorg. Chem. 25, 4286-4288.
    • (1986) Inorg. Chem , vol.25 , pp. 4286-4288
    • Godziela, G.M.1    Kramer, S.K.2    Goff, H.M.3
  • 27
    • 0035955173 scopus 로고    scopus 로고
    • Resonance Raman studies of selectively labelled hemoglobin tetramers
    • Podstawka, E., Kincaid, J. R., and Proniewicz, L. M. (2001) Resonance Raman studies of selectively labelled hemoglobin tetramers. J. Mol. Struct. 596, 157-162.
    • (2001) J. Mol. Struct , vol.596 , pp. 157-162
    • Podstawka, E.1    Kincaid, J.R.2    Proniewicz, L.M.3
  • 28
    • 7044247187 scopus 로고    scopus 로고
    • Effects of systematic peripheral group deuteration on the low-frequency resonance Raman spectra of myoglobin derivatives
    • Mak, P. J., Podstawka, E., Kincaid, J. R., and Proniewicz, L. M. (2004) Effects of systematic peripheral group deuteration on the low-frequency resonance Raman spectra of myoglobin derivatives. Biopolymers 75, 217-228.
    • (2004) Biopolymers , vol.75 , pp. 217-228
    • Mak, P.J.1    Podstawka, E.2    Kincaid, J.R.3    Proniewicz, L.M.4
  • 29
    • 33845232631 scopus 로고    scopus 로고
    • Low frequency resonance Raman spectra of isolated α and β subunits of hemoglobin and their deuterated analogues
    • Podstawka, E., Mak, P. J., Kincaid, J. R., and Proniewicz, L. M. (2006) Low frequency resonance Raman spectra of isolated α and β subunits of hemoglobin and their deuterated analogues. Biopolymers 83, 455-466.
    • (2006) Biopolymers , vol.83 , pp. 455-466
    • Podstawka, E.1    Mak, P.J.2    Kincaid, J.R.3    Proniewicz, L.M.4
  • 30
    • 0002263294 scopus 로고
    • Laboratory methods
    • Smith, K. M, Ed, pp, Elsevier/North Holland, Amsterdam
    • Fuhrhop, J.-H., and Smith, K. M. (1975) Laboratory methods. In Porphyrin and Metalloporphyrins (Smith, K. M., Ed.) pp 757-869, Elsevier/North Holland, Amsterdam.
    • (1975) Porphyrin and Metalloporphyrins , pp. 757-869
    • Fuhrhop, J.-H.1    Smith, K.M.2
  • 31
    • 0022435279 scopus 로고
    • Use of the nuclear Overhauser effect to assign proton NMR resonances in a low-spin paramagnetic hemin
    • Barbush, M., and Dixon, D. W. (1985) Use of the nuclear Overhauser effect to assign proton NMR resonances in a low-spin paramagnetic hemin. Biochem. Biophys. Res. Commun. 129, 70-75.
    • (1985) Biochem. Biophys. Res. Commun , vol.129 , pp. 70-75
    • Barbush, M.1    Dixon, D.W.2
  • 32
    • 0000196392 scopus 로고
    • Synthesis and Properties of metalloporphyrins
    • Dolphin, D, Ed, Academic Press, New York
    • Buchler, J. W. (1978) Synthesis and Properties of metalloporphyrins. In The Porphyrins; Structure and Synthesis, Part A (Dolphin, D., Ed.) Vol. 1, pp 389-483, Academic Press, New York.
    • (1978) The Porphyrins; Structure and Synthesis, Part A , vol.1 , pp. 389-483
    • Buchler, J.W.1
  • 33
    • 0016798421 scopus 로고
    • Analytical chromatography of hemins on silica gel
    • DiNello, R. K., and Dolphin, D. H. (1975) Analytical chromatography of hemins on silica gel. Anal. Biochem. 64, 444-449.
    • (1975) Anal. Biochem , vol.64 , pp. 444-449
    • DiNello, R.K.1    Dolphin, D.H.2
  • 34
    • 0019755179 scopus 로고
    • Preparation of myoglobins
    • Antonini, E, Bernardi, L. R, and Chiancone, E, Eds, Academic Press, New York
    • Wittenberg, J. B., and Wittenberg, B. A. (1981) Preparation of myoglobins. In Methods in Enzymology (Antonini, E., Bernardi, L. R., and Chiancone, E., Eds.) Vol. 76, pp 29-42, Academic Press, New York.
    • (1981) Methods in Enzymology , vol.76 , pp. 29-42
    • Wittenberg, J.B.1    Wittenberg, B.A.2
  • 35
    • 0019763671 scopus 로고
    • Preparation and properties of apohemoglobin and reconstituted hemoglobins
    • Antonini, E, Bernardi, L. R, and Chiancone, E, Eds, Academic Press, New York
    • Ascoli, F., Fanelli, M. R. R., and Antonini, E. (1981) Preparation and properties of apohemoglobin and reconstituted hemoglobins. In Methods in Enzymology (Antonini, E., Bernardi, L. R., and Chiancone, E., Eds.) Vol. 76, pp 72-87, Academic Press, New York.
    • (1981) Methods in Enzymology , vol.76 , pp. 72-87
    • Ascoli, F.1    Fanelli, M.R.R.2    Antonini, E.3
  • 36
    • 0001206096 scopus 로고
    • Metastable photoproducts from carbon monoxide myoglobin
    • Rousseau, D. L., and Argade, P. V. (1986) Metastable photoproducts from carbon monoxide myoglobin. Proc. Natl. Acad. Sci. U.S.A. 83, 1310-1314.
    • (1986) Proc. Natl. Acad. Sci. U.S.A , vol.83 , pp. 1310-1314
    • Rousseau, D.L.1    Argade, P.V.2
  • 37
    • 54949132862 scopus 로고    scopus 로고
    • Defining resonance Raman spectral responses to substrate binding by cytochrome P450 from Pseudomonas putida
    • Mak, P. J., Kaluka, D., Manyumwa, M. E., Zhang, H., Deng, T., and Kincaid, J. R. (2008) Defining resonance Raman spectral responses to substrate binding by cytochrome P450 from Pseudomonas putida. Biopolymers 89, 1045-1053.
    • (2008) Biopolymers , vol.89 , pp. 1045-1053
    • Mak, P.J.1    Kaluka, D.2    Manyumwa, M.E.3    Zhang, H.4    Deng, T.5    Kincaid, J.R.6
  • 38
    • 1242330313 scopus 로고    scopus 로고
    • Phe393 Mutants of Cytochrome P450 BM3 with Modified Heme Redox Potentials Have Altered Heme Vinyl and Propionate Conformations
    • Chen, Z., Ost, T. W. B., and Schelvis, J. P. M. (2004) Phe393 Mutants of Cytochrome P450 BM3 with Modified Heme Redox Potentials Have Altered Heme Vinyl and Propionate Conformations. Biochemistry 43, 1798-1808.
    • (2004) Biochemistry , vol.43 , pp. 1798-1808
    • Chen, Z.1    Ost, T.W.B.2    Schelvis, J.P.M.3
  • 39
    • 0032168882 scopus 로고    scopus 로고
    • Functional Implications of the Proximal Hydrogen-Bonding Network in Myoglobin: A Resonance Raman and Kinetic Study of Leu89, Ser92, His97, and F-Helix Swap Mutants
    • Peterson, E. S., Friedman, J. M., Chien, E. Y. T., and Sligar, S. G. (1998) Functional Implications of the Proximal Hydrogen-Bonding Network in Myoglobin: A Resonance Raman and Kinetic Study of Leu89, Ser92, His97, and F-Helix Swap Mutants. Biochemistry 37, 12301-12319.
    • (1998) Biochemistry , vol.37 , pp. 12301-12319
    • Peterson, E.S.1    Friedman, J.M.2    Chien, E.Y.T.3    Sligar, S.G.4
  • 40
    • 0025296867 scopus 로고
    • High-resolution study of the three-dimensional structure of horse heart metmyoglobin
    • Evans, S. V., and Brayer, G. D. (1990) High-resolution study of the three-dimensional structure of horse heart metmyoglobin. J. Mol. Biol. 213, 885-897.
    • (1990) J. Mol. Biol , vol.213 , pp. 885-897
    • Evans, S.V.1    Brayer, G.D.2
  • 41
    • 0030467166 scopus 로고    scopus 로고
    • Assignment of protoheme resonance Raman spectrum by heme labeling in myoglobin
    • Hu, S., Smith, K. M., and Spiro, T. G. (1996) Assignment of protoheme resonance Raman spectrum by heme labeling in myoglobin. J. Am. Chem. Soc. 118, 12638-12646.
    • (1996) J. Am. Chem. Soc , vol.118 , pp. 12638-12646
    • Hu, S.1    Smith, K.M.2    Spiro, T.G.3
  • 42
    • 0001314340 scopus 로고    scopus 로고
    • Heme-protein interactions in cytochrome c peroxidase revealed by site-directed mutagenesis and resonance Raman spectra of isotopically labeled hemes
    • Smulevich, G., Hu, S., Rodgers, K. R., Goodin, D. B., Smith, K. M., and Spiro, T. G. (1996) Heme-protein interactions in cytochrome c peroxidase revealed by site-directed mutagenesis and resonance Raman spectra of isotopically labeled hemes. Biospectroscopy 2, 365-376.
    • (1996) Biospectroscopy , vol.2 , pp. 365-376
    • Smulevich, G.1    Hu, S.2    Rodgers, K.R.3    Goodin, D.B.4    Smith, K.M.5    Spiro, T.G.6
  • 43
    • 0023897845 scopus 로고
    • 4-Vinyl and 2,4-divinyl deuteration effects on the low frequency resonance Raman bands of myoglobin: Correlation with the structure of vinyl group
    • Uchida, K., Susai, Y., Hirotani, E., Kimura, T., Yoneya, T., Takeuchi, H., and Harada, I. (1988) 4-Vinyl and 2,4-divinyl deuteration effects on the low frequency resonance Raman bands of myoglobin: Correlation with the structure of vinyl group. J. Biochem. 103, 979-985.
    • (1988) J. Biochem , vol.103 , pp. 979-985
    • Uchida, K.1    Susai, Y.2    Hirotani, E.3    Kimura, T.4    Yoneya, T.5    Takeuchi, H.6    Harada, I.7
  • 44
    • 0029583786 scopus 로고
    • Determinants of the Vinyl Stretching Frequency in Protoporphyrins. Implications for Cofactor-Protein Interactions in Heme Proteins
    • Kalsbeck, W. A., Ghosh, A., Pandey, R. K., Smith, K. M., and Bocian, D. F. (1995) Determinants of the Vinyl Stretching Frequency in Protoporphyrins. Implications for Cofactor-Protein Interactions in Heme Proteins. J. Am. Chem. Soc. 117, 10959-10968.
    • (1995) J. Am. Chem. Soc , vol.117 , pp. 10959-10968
    • Kalsbeck, W.A.1    Ghosh, A.2    Pandey, R.K.3    Smith, K.M.4    Bocian, D.F.5
  • 45
    • 0242386453 scopus 로고    scopus 로고
    • Relationship between heme vinyl conformation and the protein matrix in peroxidases
    • Marzocchi, M. P., and Smulevich, G. (2003) Relationship between heme vinyl conformation and the protein matrix in peroxidases. J. Raman Spectrosc. 34, 725-736.
    • (2003) J. Raman Spectrosc , vol.34 , pp. 725-736
    • Marzocchi, M.P.1    Smulevich, G.2
  • 46
    • 33845183059 scopus 로고
    • Consistent porphyrin force field. 3. Out-of-plane modes in the resonance Raman spectra of planar and ruffled nickel octaethylporphyrin
    • Li, X.-Y., Czernuszewicz, R. S., Kincaid, J. R., and Spiro, T. G. (1989) Consistent porphyrin force field. 3. Out-of-plane modes in the resonance Raman spectra of planar and ruffled nickel octaethylporphyrin. J. Am. Chem. Soc. 111, 7012-7023.
    • (1989) J. Am. Chem. Soc , vol.111 , pp. 7012-7023
    • Li, X.-Y.1    Czernuszewicz, R.S.2    Kincaid, J.R.3    Spiro, T.G.4
  • 47
    • 0003096407 scopus 로고
    • Consistent porphyrin force field. 2. Nickel octaethylporphyrin skeletal and substituent mode assignments from nitrogen-15, meso-d4, and methylene-d16 Raman and infrared isotope shifts
    • Li, X.-Y., Czernuszewicz, R. S., Kincaid, J. R., Stein, P., and Spiro, T. G. (1990) Consistent porphyrin force field. 2. Nickel octaethylporphyrin skeletal and substituent mode assignments from nitrogen-15, meso-d4, and methylene-d16 Raman and infrared isotope shifts. J. Phys. Chem. 94, 47-61.
    • (1990) J. Phys. Chem , vol.94 , pp. 47-61
    • Li, X.-Y.1    Czernuszewicz, R.S.2    Kincaid, J.R.3    Stein, P.4    Spiro, T.G.5
  • 48
    • 0001098625 scopus 로고
    • Resonance Raman spectra of octaethylporphyrinatonickel(II) and meso-deuterated and nitrogen-15 and substituted derivatives. I. Observation and assignments of nonfundamental Raman lines
    • Kitagawa, T., Abe, M., and Ogoshi, H. (1978) Resonance Raman spectra of octaethylporphyrinatonickel(II) and meso-deuterated and nitrogen-15 and substituted derivatives. I. Observation and assignments of nonfundamental Raman lines. J. Chem. Phys. 69, 4516-4525.
    • (1978) J. Chem. Phys , vol.69 , pp. 4516-4525
    • Kitagawa, T.1    Abe, M.2    Ogoshi, H.3
  • 49
    • 0001098626 scopus 로고
    • Resonance Raman spectra of octaethylporphyrinatonickel(II) and meso-deuterated and nitrogen-15 substituted derivatives. II. A normal coordinate analysis
    • Abe, M., Kitagawa, T., and Kyogoku, Y. (1978) Resonance Raman spectra of octaethylporphyrinatonickel(II) and meso-deuterated and nitrogen-15 substituted derivatives. II. A normal coordinate analysis. J. Chem. Phys. 69, 4526-4534.
    • (1978) J. Chem. Phys , vol.69 , pp. 4526-4534
    • Abe, M.1    Kitagawa, T.2    Kyogoku, Y.3
  • 50
    • 0033550059 scopus 로고    scopus 로고
    • Resonance Raman Studies of Cytochrome P450BM3 and Its Complexes with Exogenous Ligands
    • Deng, T. J., Proniewicz, L. M., Kincaid, J. R., Yeom, H., Macdonald, I. D. G., and Sligar, S. G. (1999) Resonance Raman Studies of Cytochrome P450BM3 and Its Complexes with Exogenous Ligands. Biochemistry 38, 13699-13706.
    • (1999) Biochemistry , vol.38 , pp. 13699-13706
    • Deng, T.J.1    Proniewicz, L.M.2    Kincaid, J.R.3    Yeom, H.4    Macdonald, I.D.G.5    Sligar, S.G.6
  • 51
    • 0000822936 scopus 로고    scopus 로고
    • Structural evolution of the heme group during the allosteric transition in hemoglobin: Insights from resonance Raman spectra of isotopically labeled heme
    • Jayaraman, V., and Spiro, T. G. (1996) Structural evolution of the heme group during the allosteric transition in hemoglobin: Insights from resonance Raman spectra of isotopically labeled heme. Biospectroscopy 2, 311-316.
    • (1996) Biospectroscopy , vol.2 , pp. 311-316
    • Jayaraman, V.1    Spiro, T.G.2
  • 52
    • 1842513886 scopus 로고    scopus 로고
    • Observation of Multiple CN-Isotope-Sensitive Raman Bands for CN Adducts of Hemoglobin, Myoglobin, and Cytochrome c Oxidase: Evidence for Vibrational Coupling between the Fe-C-N Bending and Porphyrin In-Plane Modes
    • Hirota, S., Ogura, T., Shinzawa-Itoh, K., Yoshikawa, S., and Kitagawa, T. (1996) Observation of Multiple CN-Isotope-Sensitive Raman Bands for CN Adducts of Hemoglobin, Myoglobin, and Cytochrome c Oxidase: Evidence for Vibrational Coupling between the Fe-C-N Bending and Porphyrin In-Plane Modes. J. Phys. Chem. 100, 15274-15279.
    • (1996) J. Phys. Chem , vol.100 , pp. 15274-15279
    • Hirota, S.1    Ogura, T.2    Shinzawa-Itoh, K.3    Yoshikawa, S.4    Kitagawa, T.5
  • 53
    • 33748610542 scopus 로고    scopus 로고
    • 15N NMR Studies of Iron-Bound Cyanides of Heme Proteins and Related Model Complexes: Sensitive Probe for Detecting Hydrogen-bonding Interactions at the Proximal and Distal Sides
    • 15N NMR Studies of Iron-Bound Cyanides of Heme Proteins and Related Model Complexes: Sensitive Probe for Detecting Hydrogen-bonding Interactions at the Proximal and Distal Sides. Inorg. Chem. 45, 6816-6827.
    • (2006) Inorg. Chem , vol.45 , pp. 6816-6827
    • Fujii, H.1    Yoshida, T.2


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