메뉴 건너뛰기




Volumn 93, Issue 12, 2007, Pages 4404-4413

Low frequency spectral density of ferrous heme: Perturbations induced by axial ligation and protein insertion

Author keywords

[No Author keywords available]

Indexed keywords

2 METHYLIMIDAZOLE; CARBON MONOXIDE; CHLORIDE PEROXIDASE; CYTOCHROME P450; FERROUS ION; HEME; HORSERADISH PEROXIDASE; IMIDAZOLE DERIVATIVE; MYOGLOBIN; UNCLASSIFIED DRUG;

EID: 37349001025     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.107.114736     Document Type: Article
Times cited : (21)

References (61)
  • 2
    • 0002052550 scopus 로고
    • Heme protein structure and the iron histidine stretching mode
    • Spectroscopy. T. G. Spiro, editor. Wiley-Interscience Publication, New York
    • Kitagawa, T. 1988. Heme protein structure and the iron histidine stretching mode. In Biological Applications of Raman Spectroscopy. T. G. Spiro, editor. Wiley-Interscience Publication, New York. 97-131.
    • (1988) Biological Applications of Raman , pp. 97-131
    • Kitagawa, T.1
  • 3
  • 5
    • 0035223846 scopus 로고    scopus 로고
    • CooA: A heme-containing regulatory protein that serves as a specific sensor of both carbon monoxide and redox state
    • Roberts, G. P., M. V. Thorsteinsson, R. L. Kerby, W. N. Lanzilotta, and T. Poulos. 2001. CooA: a heme-containing regulatory protein that serves as a specific sensor of both carbon monoxide and redox state. Prog. Nucleic Acid Res. Mol. Biol. 67:35-63.
    • (2001) Prog. Nucleic Acid Res. Mol. Biol , vol.67 , pp. 35-63
    • Roberts, G.P.1    Thorsteinsson, M.V.2    Kerby, R.L.3    Lanzilotta, W.N.4    Poulos, T.5
  • 6
    • 0035853755 scopus 로고    scopus 로고
    • Binding of CO at the Pro2 side is crucial for the activation of CO-sensing transcriptional activator CooA. (1)H NMR spectroscopic studies
    • Yamamoto, K., H. Ishikawa, S. Takahashi, K. Ishimori, I. Morishima, H. Nakajima, and S. Aono. 2001. Binding of CO at the Pro2 side is crucial for the activation of CO-sensing transcriptional activator CooA. (1)H NMR spectroscopic studies. J. Biol. Chem. 276:11473-11476.
    • (2001) J. Biol. Chem , vol.276 , pp. 11473-11476
    • Yamamoto, K.1    Ishikawa, H.2    Takahashi, S.3    Ishimori, K.4    Morishima, I.5    Nakajima, H.6    Aono, S.7
  • 9
    • 33847799938 scopus 로고
    • Fluorescence, resonance Raman and radiationless decay in several hemoproteins
    • Adar, F., M. Gouterman, and S. Aronowitz. 1976. Fluorescence, resonance Raman and radiationless decay in several hemoproteins. J. Phys. Chem. 80:2184-2191.
    • (1976) J. Phys. Chem , vol.80 , pp. 2184-2191
    • Adar, F.1    Gouterman, M.2    Aronowitz, S.3
  • 10
    • 37349080685 scopus 로고
    • Vibrational circular-dichroism, Raman, FTIR and electronic CD studies of azide binding to hemeproteins
    • Abstr
    • Asher, S., P. Larkin, N. Ragunathan, T. Freedman, L. Nafie, B. Springer, S. Sligar, and R. Noble. 1990. Vibrational circular-dichroism, Raman, FTIR and electronic CD studies of azide binding to hemeproteins. Biophys. J. 57:A50 (Abstr.).
    • (1990) Biophys. J , vol.57
    • Asher, S.1    Larkin, P.2    Ragunathan, N.3    Freedman, T.4    Nafie, L.5    Springer, B.6    Sligar, S.7    Noble, R.8
  • 11
    • 0031567599 scopus 로고    scopus 로고
    • Circular dichroism spectroscopy of lucina I hemoglobin
    • Boffi, A., J. B. Wittenberg, and E. Chiancone. 1997. Circular dichroism spectroscopy of lucina I hemoglobin. FEBS Lett. 411:335-338.
    • (1997) FEBS Lett , vol.411 , pp. 335-338
    • Boffi, A.1    Wittenberg, J.B.2    Chiancone, E.3
  • 12
    • 0000149465 scopus 로고
    • Photochemical hole-burning in photosynthetic reaction centers
    • Boxer, S. G., D. J. Lockhart, and T. R. Middendorf. 1986. Photochemical hole-burning in photosynthetic reaction centers. Chem. Phys. Lett. 123:476-482.
    • (1986) Chem. Phys. Lett , vol.123 , pp. 476-482
    • Boxer, S.G.1    Lockhart, D.J.2    Middendorf, T.R.3
  • 14
    • 0013129690 scopus 로고
    • Far infrared magnetic resonance of deoxyhemoglobin and deoxymyoglobin
    • Champion, P. M., and A. J. Sievers. 1980. Far infrared magnetic resonance of deoxyhemoglobin and deoxymyoglobin. J. Chem. Phys. 72:1569-1582.
    • (1980) J. Chem. Phys , vol.72 , pp. 1569-1582
    • Champion, P.M.1    Sievers, A.J.2
  • 15
    • 0036290597 scopus 로고    scopus 로고
    • H93G myoglobin cavity mutant as versatile template for modeling heme proteins: Magnetic circular dichroism studies of thiolate- and imidazole-ligated complexes
    • Dawson, J. H., A. E. Pond, and M. P. Roach. 2002. H93G myoglobin cavity mutant as versatile template for modeling heme proteins: magnetic circular dichroism studies of thiolate- and imidazole-ligated complexes. Biopolymers. 67:200-206.
    • (2002) Biopolymers , vol.67 , pp. 200-206
    • Dawson, J.H.1    Pond, A.E.2    Roach, M.P.3
  • 16
    • 0008034283 scopus 로고    scopus 로고
    • Stark-effect spectroscopy of the heme charge-transfer bands of deoxymyoglobin
    • Franzen, S., L. J. Moore, W. H. Woodruff, and S. G. Boxer. 1999. Stark-effect spectroscopy of the heme charge-transfer bands of deoxymyoglobin. J. Phys. Chem. B. 103:3070-3072.
    • (1999) J. Phys. Chem. B , vol.103 , pp. 3070-3072
    • Franzen, S.1    Moore, L.J.2    Woodruff, W.H.3    Boxer, S.G.4
  • 17
    • 0000740326 scopus 로고    scopus 로고
    • Resonance Raman spectra of heme proteins and model compounds
    • Handbook. K. M. Kadish, K. M. Smith, and R. Guilard, editors. Academic Press, New York
    • Kincaid, J. 2000. Resonance Raman spectra of heme proteins and model compounds. In The Porphyrin Handbook. K. M. Kadish, K. M. Smith, and R. Guilard, editors. Academic Press, New York. 225-92.
    • (2000) The Porphyrin , pp. 225-292
    • Kincaid, J.1
  • 18
    • 33845552131 scopus 로고
    • Proton NMR characterization of the ferryl group in model heme complexes and hemoproteins: Evidence for the Fe(IV)=O group in ferryl myoglobin and compound II of horseradish peroxidase
    • Lamar, G. N., J. S. Deropp, L. Latosgrazynski, A. L. Balch, R. B. Johnson, K. M. Smith, D. W. Parish, and R. J. Cheng. 1983. Proton NMR characterization of the ferryl group in model heme complexes and hemoproteins: evidence for the Fe(IV)=O group in ferryl myoglobin and compound II of horseradish peroxidase. J. Am. Chem. Soc. 105:782-787.
    • (1983) J. Am. Chem. Soc , vol.105 , pp. 782-787
    • Lamar, G.N.1    Deropp, J.S.2    Latosgrazynski, L.3    Balch, A.L.4    Johnson, R.B.5    Smith, K.M.6    Parish, D.W.7    Cheng, R.J.8
  • 19
    • 0020649603 scopus 로고
    • Femtosecond photolysis of CO-ligated protoheme and hemoproteins: Appearance of deoxy species with a 350-fsec time constant
    • Martin, J. L., A. Migus, C. Poyart, Y. Lecarpentier, R. Astier, and A. Antonetti. 1983. Femtosecond photolysis of CO-ligated protoheme and hemoproteins: appearance of deoxy species with a 350-fsec time constant. Proc. Natl. Acad. Sci. USA. 80:173-177.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 173-177
    • Martin, J.L.1    Migus, A.2    Poyart, C.3    Lecarpentier, Y.4    Astier, R.5    Antonetti, A.6
  • 20
    • 0035756040 scopus 로고    scopus 로고
    • Ultrafast dynamics of myoglobin probed by time-resolved resonance Raman spectroscopy
    • Mizutani, Y., and T. Kitagawa. 2001. Ultrafast dynamics of myoglobin probed by time-resolved resonance Raman spectroscopy. Chem. Rec. 1:258-275.
    • (2001) Chem. Rec , vol.1 , pp. 258-275
    • Mizutani, Y.1    Kitagawa, T.2
  • 21
    • 0031904189 scopus 로고    scopus 로고
    • Ultrafast time-resolved crystallography
    • Moffat, K. 1998. Ultrafast time-resolved crystallography. Nat. Struct. Biol. 5:641-643.
    • (1998) Nat. Struct. Biol , vol.5 , pp. 641-643
    • Moffat, K.1
  • 22
    • 0001436651 scopus 로고
    • Oxygen-17 nuclear magnetic resonance study of water exchange on water-soluble iron(III) porphyrins
    • Ostrich, I. J., G. Liu, H. W. Dodgen, and J. P. Hunt. 1980. Oxygen-17 nuclear magnetic resonance study of water exchange on water-soluble iron(III) porphyrins. Inorg. Chem. 19:619-621.
    • (1980) Inorg. Chem , vol.19 , pp. 619-621
    • Ostrich, I.J.1    Liu, G.2    Dodgen, H.W.3    Hunt, J.P.4
  • 24
    • 0040397078 scopus 로고
    • Picosecond magnetic circular-dichroism spectroscopy
    • Xie, X. L., and J. D. Simon. 1990. Picosecond magnetic circular-dichroism spectroscopy. J. Phys. Chem. 94:8014-8016.
    • (1990) J. Phys. Chem , vol.94 , pp. 8014-8016
    • Xie, X.L.1    Simon, J.D.2
  • 26
    • 0029833656 scopus 로고    scopus 로고
    • Dlott, D. D., M. D. Fayer, J. R. Hill, C. W. Rella, K. S. Suslick, and C. J. Ziegler. 1996. Vibrational relaxation in metalloporphyrin CO complexes. J. Am. Chem. Soc. 118:7853-7854.
    • Dlott, D. D., M. D. Fayer, J. R. Hill, C. W. Rella, K. S. Suslick, and C. J. Ziegler. 1996. Vibrational relaxation in metalloporphyrin CO complexes. J. Am. Chem. Soc. 118:7853-7854.
  • 27
    • 0033420652 scopus 로고    scopus 로고
    • Nitric oxide complexes of metalloporphyrins: An overview of some mechanistic studies
    • Hoshino, M., L. Laverman, and P. C. Ford. 1999. Nitric oxide complexes of metalloporphyrins: an overview of some mechanistic studies. Coord. Chem. Rev. 187:75-102.
    • (1999) Coord. Chem. Rev , vol.187 , pp. 75-102
    • Hoshino, M.1    Laverman, L.2    Ford, P.C.3
  • 28
    • 0003017303 scopus 로고    scopus 로고
    • Volume and thermodynamic profiles of CO-binding to Fe(II) protoporphyrin IX in detergent micelles
    • Larsen, R. W. 1999. Volume and thermodynamic profiles of CO-binding to Fe(II) protoporphyrin IX in detergent micelles. Inorg. Chim. Acta. 288:74-81.
    • (1999) Inorg. Chim. Acta , vol.288 , pp. 74-81
    • Larsen, R.W.1
  • 29
    • 36449007732 scopus 로고
    • Time-resolved and static optical properties of vibrationally excited porphyrins
    • Rodriguez, J., C. Kirmaier, and D. Holten. 1991. Time-resolved and static optical properties of vibrationally excited porphyrins. J. Chem. Phys. 94:6020-6029.
    • (1991) J. Chem. Phys , vol.94 , pp. 6020-6029
    • Rodriguez, J.1    Kirmaier, C.2    Holten, D.3
  • 31
    • 0002179084 scopus 로고
    • Resonance Raman spectroscopy of metalloporphyrins
    • Spectroscopy. T. G. Spiro, editor. Wiley-Interscience Publication, New York
    • Spiro, T. G., and H. Y. Li. 1988. Resonance Raman spectroscopy of metalloporphyrins. In Biological Applications of Raman Spectroscopy. T. G. Spiro, editor. Wiley-Interscience Publication, New York. 1-37.
    • (1988) Biological Applications of Raman , pp. 1-37
    • Spiro, T.G.1    Li, H.Y.2
  • 32
    • 0001668230 scopus 로고
    • Geminate processes in the reaction of nitric-oxide with 1- methylimidazole-iron(II) porphyrin complexes: Steric, solvent polarity, and viscosity effects
    • Traylor, T. G., D. Magde, J. Marsters, K. Jongeward, G. Z. Wu, and K. Walda. 1993. Geminate processes in the reaction of nitric-oxide with 1- methylimidazole-iron(II) porphyrin complexes: steric, solvent polarity, and viscosity effects. J. Am. Chem. Soc. 115:4808-4813.
    • (1993) J. Am. Chem. Soc , vol.115 , pp. 4808-4813
    • Traylor, T.G.1    Magde, D.2    Marsters, J.3    Jongeward, K.4    Wu, G.Z.5    Walda, K.6
  • 33
    • 17744362896 scopus 로고    scopus 로고
    • CO rebinding to protoheme: Investigations of the proximal and distal contributions to the geminate rebinding barrier
    • Ye, X., A. C. Yu, G. Y. Georgiev, F. Gruia, D. Ionascu, W. X. Cao, J. T. Sage, and P. M. Champion. 2005. CO rebinding to protoheme: investigations of the proximal and distal contributions to the geminate rebinding barrier. J. Am. Chem. Soc. 127:5854-5861.
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 5854-5861
    • Ye, X.1    Yu, A.C.2    Georgiev, G.Y.3    Gruia, F.4    Ionascu, D.5    Cao, W.X.6    Sage, J.T.7    Champion, P.M.8
  • 34
    • 36449006469 scopus 로고
    • Photon-echoes and related 4-wave-mixing spectroscopies using phase-locked pulses
    • Cho, M. H., N. F. Scherer, G. R. Fleming, and S. Mukamel. 1992. Photon-echoes and related 4-wave-mixing spectroscopies using phase-locked pulses. J. Chem. Phys. 96:5618-5629.
    • (1992) J. Chem. Phys , vol.96 , pp. 5618-5629
    • Cho, M.H.1    Scherer, N.F.2    Fleming, G.R.3    Mukamel, S.4
  • 35
    • 33751157106 scopus 로고
    • Femtosecond wavepacket spectroscopy: Influence of temperature, wavelength, and pulse duration
    • Jonas, D. M., S. E. Bradforth, S. A. Passino, and G. R. Fleming. 1995. Femtosecond wavepacket spectroscopy: influence of temperature, wavelength, and pulse duration. J. Phys. Chem. 99:2594-2608.
    • (1995) J. Phys. Chem , vol.99 , pp. 2594-2608
    • Jonas, D.M.1    Bradforth, S.E.2    Passino, S.A.3    Fleming, G.R.4
  • 36
    • 0035121238 scopus 로고    scopus 로고
    • Investigations of amplitude and phase excitation profiles in femtosecond coherence spectroscopy
    • Kumar, A. T. N., F. Rosca, A. Widom, and P. M. Champion. 2001. Investigations of amplitude and phase excitation profiles in femtosecond coherence spectroscopy. J. Chem. Phys. 114:701-724.
    • (2001) J. Chem. Phys , vol.114 , pp. 701-724
    • Kumar, A.T.N.1    Rosca, F.2    Widom, A.3    Champion, P.M.4
  • 37
    • 0035870565 scopus 로고    scopus 로고
    • Investigations of ultrafast nuclear response induced by resonant and nonresonant laser pulses
    • Kumar, A. T. N., F. Rosca, A. Widom, and P. M. Champion. 2001. Investigations of ultrafast nuclear response induced by resonant and nonresonant laser pulses. J. Chem. Phys. 114:6795-6815.
    • (2001) J. Chem. Phys , vol.114 , pp. 6795-6815
    • Kumar, A.T.N.1    Rosca, F.2    Widom, A.3    Champion, P.M.4
  • 38
    • 0002924146 scopus 로고
    • Femtosecond optical spectroscopy: A direct look at elementary chemical events
    • Mukamel, S. 1990. Femtosecond optical spectroscopy: a direct look at elementary chemical events. Annu. Rev. Phys. Chem. 41: 647-681.
    • (1990) Annu. Rev. Phys. Chem , vol.41 , pp. 647-681
    • Mukamel, S.1
  • 40
    • 0011136305 scopus 로고
    • Femtosecond time-resolved observation of coherent molecular vibrational motion
    • Nelson, K. A., and L. R. Williams. 1987. Femtosecond time-resolved observation of coherent molecular vibrational motion. Phys. Rev. Lett. 58:745.
    • (1987) Phys. Rev. Lett , vol.58 , pp. 745
    • Nelson, K.A.1    Williams, L.R.2
  • 41
    • 85050201686 scopus 로고
    • Femtosecond coherent spectroscopy
    • Nelson, K. A., and E. P. Ippen. 1989. Femtosecond coherent spectroscopy. Adv. Chem. Phys. 75:1-35.
    • (1989) Adv. Chem. Phys , vol.75 , pp. 1-35
    • Nelson, K.A.1    Ippen, E.P.2
  • 43
    • 0032964843 scopus 로고    scopus 로고
    • Femtosecond processes in proteins
    • Vos, M. H., and J. L. Martin. 1999. Femtosecond processes in proteins. Biochim. Biophys. Acta. 1411:1-20.
    • (1999) Biochim. Biophys. Acta , vol.1411 , pp. 1-20
    • Vos, M.H.1    Martin, J.L.2
  • 44
    • 0028519152 scopus 로고
    • Vibrationally coherent photochemistry in the femtosecond primary event of vision
    • Wang, Q., R. W. Schoenlein, L. A. Peteanu, R. A. Mathies, and C. V. Shank. 1994. Vibrationally coherent photochemistry in the femtosecond primary event of vision. Science. 266:422-425.
    • (1994) Science , vol.266 , pp. 422-425
    • Wang, Q.1    Schoenlein, R.W.2    Peteanu, L.A.3    Mathies, R.A.4    Shank, C.V.5
  • 45
    • 0031210745 scopus 로고    scopus 로고
    • A multidimensional Landau-Zener description of chemical reaction dynamics and vibrational coherence
    • Zhu, L. Y., A. Widom, and P. M. Champion. 1997. A multidimensional Landau-Zener description of chemical reaction dynamics and vibrational coherence. J. Chem. Phys. 107:2859-2871.
    • (1997) J. Chem. Phys , vol.107 , pp. 2859-2871
    • Zhu, L.Y.1    Widom, A.2    Champion, P.M.3
  • 46
    • 36449006690 scopus 로고
    • Femtosecond polarization spectroscopy: A density-matrix description
    • Ziegler, L. D., R. Fan, A. E. Desrosiers, and N. F. Scherer. 1994. Femtosecond polarization spectroscopy: a density-matrix description. J. Chem. Phys. 100:1823-1839.
    • (1994) J. Chem. Phys , vol.100 , pp. 1823-1839
    • Ziegler, L.D.1    Fan, R.2    Desrosiers, A.E.3    Scherer, N.F.4
  • 47
    • 84988189520 scopus 로고
    • Raman and kinetic-studies of myoglobin structure and dynamics
    • Champion, P. M. 1992. Raman and kinetic-studies of myoglobin structure and dynamics. J. Raman Spectrosc. 23:557-567.
    • (1992) J. Raman Spectrosc , vol.23 , pp. 557-567
    • Champion, P.M.1
  • 48
    • 0344730727 scopus 로고
    • Protein fluctuations, distributed coupling, and the binding of ligands to heme-proteins
    • Srajer, V., L. Reinisch, and P. M. Champion. 1988. Protein fluctuations, distributed coupling, and the binding of ligands to heme-proteins. J. Am. Chem. Soc. 110:6656-6670.
    • (1988) J. Am. Chem. Soc , vol.110 , pp. 6656-6670
    • Srajer, V.1    Reinisch, L.2    Champion, P.M.3
  • 49
    • 0025718720 scopus 로고
    • Investigations of optical-line shapes and kinetic hole burning in myoglobin
    • Srajer, V., and P. M. Champion. 1991. Investigations of optical-line shapes and kinetic hole burning in myoglobin. Biochemistry. 30:7390-7402.
    • (1991) Biochemistry , vol.30 , pp. 7390-7402
    • Srajer, V.1    Champion, P.M.2
  • 52
    • 0016400375 scopus 로고
    • Resonance Raman spectra of heme proteins. Effects of oxidation and spin states
    • Spiro, T. G., and T. C. Strekas. 1974. Resonance Raman spectra of heme proteins. Effects of oxidation and spin states. 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
  • 53
    • 33847085258 scopus 로고
    • Iron-ligand stretching band in the resonance Raman spectra of ferrous iron porphyrin derivatives. Importance as a probe band for quaternary structure of hemoglobin
    • Hori, H., and T. Kitagawa. 1980. Iron-ligand stretching band in the resonance Raman spectra of ferrous iron porphyrin derivatives. Importance as a probe band for quaternary structure of hemoglobin. J. Am. Chem. Soc. 102:3608-3613.
    • (1980) J. Am. Chem. Soc , vol.102 , pp. 3608-3613
    • Hori, H.1    Kitagawa, T.2
  • 54
    • 0001244916 scopus 로고
    • Differences in Fe(II)-N epsilon(His-F8) stretching frequencies between deoxyhemoglobins in the two alternative quaternary structures
    • Nagai, K., and T. Kitagawa. 1980. Differences in Fe(II)-N epsilon(His-F8) stretching frequencies between deoxyhemoglobins in the two alternative quaternary structures. Proc. Natl. Acad. Sci. USA. 77:2033-2037.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 2033-2037
    • Nagai, K.1    Kitagawa, T.2
  • 55
    • 35548977602 scopus 로고    scopus 로고
    • Temperature dependent dynamics of protoheme: Non-exponential CO rebinding and relaxation in the absence of protein conformational substates
    • Ye, X., D. Ionascu, F. Gruia, A. Yu, and P. Champion. 2007. Temperature dependent dynamics of protoheme: non-exponential CO rebinding and relaxation in the absence of protein conformational substates. Proc. Natl. Acad. Sci. USA. 104:14682-14687.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 14682-14687
    • Ye, X.1    Ionascu, D.2    Gruia, F.3    Yu, A.4    Champion, P.5
  • 56
    • 0029986887 scopus 로고    scopus 로고
    • Crystal structures of CO-, deoxyand met-myoglobins at various pH values
    • Yang, F., and G. N. J. Phillips. 1996. Crystal structures of CO-, deoxyand met-myoglobins at various pH values. J. Mol. Biol. 256:762-774.
    • (1996) J. Mol. Biol , vol.256 , pp. 762-774
    • Yang, F.1    Phillips, G.N.J.2
  • 57
    • 0037007797 scopus 로고    scopus 로고
    • Carbonmonoxy rebinding kinetics in H93G myoglobin: Separation of proximal and distal side effects
    • Franzen, S. 2002. Carbonmonoxy rebinding kinetics in H93G myoglobin: separation of proximal and distal side effects. J. Phys. Chem. B. 106:4533-4542.
    • (2002) J. Phys. Chem. B , vol.106 , pp. 4533-4542
    • Franzen, S.1
  • 61
    • 0035949448 scopus 로고    scopus 로고
    • Ligand-induced heme ruffling and bent NO geometry in ultra-high resolution structures of nitrophorin 4
    • Roberts, S. A., A. Weichsel, Y. Qiu, J. A. Shelnutt, F. A. Walker, and W. R. Montfort. 2001. Ligand-induced heme ruffling and bent NO geometry in ultra-high resolution structures of nitrophorin 4. Biochemistry. 40:11327-11337.
    • (2001) Biochemistry , vol.40 , pp. 11327-11337
    • Roberts, S.A.1    Weichsel, A.2    Qiu, Y.3    Shelnutt, J.A.4    Walker, F.A.5    Montfort, W.R.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.