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Volumn 1701, Issue 1-2, 2004, Pages 75-87

Solution 1H NMR study of the active site molecular structure and magnetic properties of the cyanomet complex of the isolated, tetrameric β-chain from human adult hemoglobin

Author keywords

; ; Chain; Contact shift; cyanomet complex of the isolated chain of HbA; Dipolar shift; HbA; Hemoglobin A; human adult hemoglobin; isolated chain of HbA; isolated chain of HbA; Magnetic axis; met CN; NMR

Indexed keywords

HEMOGLOBIN; NITRILE; POLYPEPTIDE; TETRAMER; CYANOMETHEMOGLOBIN; DRUG DERIVATIVE; HYDROGEN; METHEMOGLOBIN;

EID: 4344663946     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2004.06.003     Document Type: Article
Times cited : (1)

References (61)
  • 4
    • 0031859481 scopus 로고    scopus 로고
    • The stereochemical mechanism of the cooperative effect in hemoglobin revisited
    • Perutz M.F., Wilkinson A.J., Paoli M., Dodson G.G. The stereochemical mechanism of the cooperative effect in hemoglobin revisited. Annu. Rev. Biophys. 27:1998;1-34
    • (1998) Annu. Rev. Biophys. , vol.27 , pp. 1-34
    • Perutz, M.F.1    Wilkinson, A.J.2    Paoli, M.3    Dodson, G.G.4
  • 5
    • 0018838712 scopus 로고
    • The structure of human carbonmonoxy haemoglobin at 2.7 Å resolution
    • Baldwin J.M. The structure of human carbonmonoxy haemoglobin at 2.7 Å resolution. J. Mol. Biol. 136:1980;103-128
    • (1980) J. Mol. Biol. , vol.136 , pp. 103-128
    • Baldwin, J.M.1
  • 6
    • 0021027685 scopus 로고
    • Structure of human oxyhemoglobin at 2.1 Å resolution
    • Shaanan B. Structure of human oxyhemoglobin at 2.1 Å resolution. J. Mol. Biol. 171:1983;31-59
    • (1983) J. Mol. Biol. , vol.171 , pp. 31-59
    • Shaanan, B.1
  • 7
    • 0021683974 scopus 로고
    • The crystal structure of human deoxyhemoglobin at 1.7 Å resolution
    • Fermi G., Perutz M.F., Shannan B., Fourme R. The crystal structure of human deoxyhemoglobin at 1.7 Å resolution. J. Mol. Biol. 175:1984;159-174
    • (1984) J. Mol. Biol. , vol.175 , pp. 159-174
    • Fermi, G.1    Perutz, M.F.2    Shannan, B.3    Fourme, R.4
  • 8
    • 0031571593 scopus 로고    scopus 로고
    • Tension in haemoglobin revealed by Fe-His(F8) bond rupture in the fully liganded T-state
    • Paoli M., Dodson G., Liddington R.C., Wilkinson A.J. Tension in haemoglobin revealed by Fe-His(F8) bond rupture in the fully liganded T-state. J. Mol. Biol. 271:1997;161-167
    • (1997) J. Mol. Biol. , vol.271 , pp. 161-167
    • Paoli, M.1    Dodson, G.2    Liddington, R.C.3    Wilkinson, A.J.4
  • 9
    • 0026619765 scopus 로고
    • Proton nuclear magnetic resonance studies on hemoglobin: Cooperative interactions and partially ligated intermediates
    • Ho C. Proton nuclear magnetic resonance studies on hemoglobin: cooperative interactions and partially ligated intermediates. Adv. Protein Chem. 43:1992;153-312
    • (1992) Adv. Protein Chem. , vol.43 , pp. 153-312
    • Ho, C.1
  • 10
  • 12
    • 1842483305 scopus 로고    scopus 로고
    • The structure-function relationship of hemoglobin in solution at atomic resolution
    • Lukin J.A., Ho C. The structure-function relationship of hemoglobin in solution at atomic resolution. Chem. Rev. 104:2004;1219-1230
    • (2004) Chem. Rev. , vol.104 , pp. 1219-1230
    • Lukin, J.A.1    Ho, C.2
  • 13
    • 0031585733 scopus 로고    scopus 로고
    • Approaches to the Solution NMR characterization of active sites for 65 kDa tetrameric hemoglobins in the paramagnetic cyanomet state
    • Kolczak U., Han C., Sylvia L.A., La Mar G.N. Approaches to the Solution NMR characterization of active sites for 65 kDa tetrameric hemoglobins in the paramagnetic cyanomet state. J. Am. Chem. Soc. 119:1997;12643-12654
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 12643-12654
    • Kolczak, U.1    Han, C.2    Sylvia, L.A.3    La Mar, G.N.4
  • 14
    • 0034741014 scopus 로고    scopus 로고
    • 1H NMR characterization of axial interactions of the proximal and distal His in the cyanomet complexes of the isolated chains and 65 kDa intact tetramer of human hemoglobin
    • 1H NMR characterization of axial interactions of the proximal and distal His in the cyanomet complexes of the isolated chains and 65 kDa intact tetramer of human hemoglobin. J. Am. Chem. Soc. 123:2001;4266-4274
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 4266-4274
    • La Mar, G.N.1    Kolczak, U.2    Tran, A.-T.3    Chien, E.4
  • 15
    • 0015527419 scopus 로고
    • High resolution nuclear magnetic resonance spectra of hemoglobin. 3. The half-ligated state and allosteric interactions
    • Ogawa S., Shulman R.G. High resolution nuclear magnetic resonance spectra of hemoglobin. 3. The half-ligated state and allosteric interactions. J. Mol. Biol. 70:1972;315-336
    • (1972) J. Mol. Biol. , vol.70 , pp. 315-336
    • Ogawa, S.1    Shulman, R.G.2
  • 16
    • 0015527426 scopus 로고
    • High resolution nuclear resonance spectra of hemoglobin. II. Ligated tetramers
    • Ogawa S., Shulman R.G., Fujiwara M., Yamane T. High resolution nuclear resonance spectra of hemoglobin. II. Ligated tetramers. J. Mol. Biol. 70:1972;301-313
    • (1972) J. Mol. Biol. , vol.70 , pp. 301-313
    • Ogawa, S.1    Shulman, R.G.2    Fujiwara, M.3    Yamane, T.4
  • 17
    • 0015527453 scopus 로고
    • High resolution nuclear magnetic resonance spectra of hemoglobin. I. The cyanide complexes of α and β chains
    • Ogawa S., Shulman R.G., Yamane T. High resolution nuclear magnetic resonance spectra of hemoglobin. I. The cyanide complexes of α and β chains. J. Mol. Biol. 70:1972;291-300
    • (1972) J. Mol. Biol. , vol.70 , pp. 291-300
    • Ogawa, S.1    Shulman, R.G.2    Yamane, T.3
  • 18
    • 0027993425 scopus 로고
    • Modeling the hemoglobin switchpoint with cyanomet valency hybrids - Raman spectroscopic probes of tertiary and quaternary structure
    • Mukerji I., Spiro T.G. Modeling the hemoglobin switchpoint with cyanomet valency hybrids - Raman spectroscopic probes of tertiary and quaternary structure. Biochemistry. 33:1994;13132-13139
    • (1994) Biochemistry , vol.33 , pp. 13132-13139
    • Mukerji, I.1    Spiro, T.G.2
  • 19
    • 0025141855 scopus 로고
    • NMR determination of the orientation of the magnetic susceptibility tensor in cyano met-myoglobin: A new probe of steric tilt of bound ligand
    • Emerson S.D., La Mar G.N. NMR determination of the orientation of the magnetic susceptibility tensor in cyano met-myoglobin: a new probe of steric tilt of bound ligand. Biochemistry. 29:1990;1556-1566
    • (1990) Biochemistry , vol.29 , pp. 1556-1566
    • Emerson, S.D.1    La Mar, G.N.2
  • 20
    • 0023280145 scopus 로고
    • 1H NMR probe for hydrogen bonding of distal residues to bound ligands in heme proteins: Isotope effect on heme electronic structure of myoglobin
    • 1H NMR probe for hydrogen bonding of distal residues to bound ligands in heme proteins: isotope effect on heme electronic structure of myoglobin. J. Am. Chem. Soc. 109:1987;7219-7220
    • (1987) J. Am. Chem. Soc. , vol.109 , pp. 7219-7220
    • Lecomte, J.T.J.1    La Mar, G.N.2
  • 21
    • 0021859756 scopus 로고
    • Comparison of the solution and crystal structures of mitochondrial cytochrome c. Analysis of paramagnetic shifts in the nuclear magnetic resonance spectrum of ferricytochrome c
    • Williams G., Clayden N.J., Moore G.R., Williams R.J.P. Comparison of the solution and crystal structures of mitochondrial cytochrome c. Analysis of paramagnetic shifts in the nuclear magnetic resonance spectrum of ferricytochrome c. J. Mol. Biol. 183:1985;447-460
    • (1985) J. Mol. Biol. , vol.183 , pp. 447-460
    • Williams, G.1    Clayden, N.J.2    Moore, G.R.3    Williams, R.J.P.4
  • 22
    • 0141976292 scopus 로고    scopus 로고
    • Solution 1H NMR study of the active site molecular structure and magnetic properties of the cyanomet complex of the isolated a-chain from human hemoglobin a
    • Tran A.-T., Kolczak U., La Mar G.N. Solution 1H NMR study of the active site molecular structure and magnetic properties of the cyanomet complex of the isolated a-chain from human hemoglobin A. BBA-PAP. 1650:2003;59-72
    • (2003) BBA-PAP , vol.1650 , pp. 59-72
    • Tran, A.-T.1    Kolczak, U.2    La Mar, G.N.3
  • 23
    • 0033550490 scopus 로고    scopus 로고
    • Solution NMR determination of the anisotropy and orientation of the paramagnetic susceptibility tensor as a function of temperature for metmyoglobin cyanide; Implications for the population of excited electronic states
    • Nguyen B.D., Xia Z., Yeh D.C., Vyas K., Deaguero H., La Mar G. Solution NMR determination of the anisotropy and orientation of the paramagnetic susceptibility tensor as a function of temperature for metmyoglobin cyanide; implications for the population of excited electronic states. J. Am. Chem. Soc. 121:1999;208-217
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 208-217
    • Nguyen, B.D.1    Xia, Z.2    Yeh, D.C.3    Vyas, K.4    Deaguero, H.5    La Mar, G.6
  • 24
    • 0032507002 scopus 로고    scopus 로고
    • Co- and counterrotation of magnetic axes and axial ligands in low-spin ferriheme systems
    • Shokhirev N.V., Walker F.A. Co- and counterrotation of magnetic axes and axial ligands in low-spin ferriheme systems. J. Am. Chem. Soc. 120:1998;981-990
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 981-990
    • Shokhirev, N.V.1    Walker, F.A.2
  • 25
    • 0011124516 scopus 로고
    • The chemistry of the Bohr effect: II. Some properties of hemoglobin H
    • Benesch R.E., Ranney H.M., Benesch R., Smith G.M. The chemistry of the Bohr effect: II. Some properties of hemoglobin H. J. Biol. Chem. 236:1961;2926-2929
    • (1961) J. Biol. Chem. , vol.236 , pp. 2926-2929
    • Benesch, R.E.1    Ranney, H.M.2    Benesch, R.3    Smith, G.M.4
  • 26
    • 0344724823 scopus 로고
    • The dissociation of hemoglobins a and H in concentrated sodium chloride
    • Benesch R.E., Benesch R., Macduff G. The dissociation of hemoglobins A and H in concentrated sodium chloride. Biochemistry. 3:1964;1132
    • (1964) Biochemistry , vol.3 , pp. 1132
    • Benesch, R.E.1    Benesch, R.2    MacDuff, G.3
  • 28
    • 0026795182 scopus 로고
    • A third quaternary structure of human hemoglobin a at 1.7 Å resolution
    • Silva M.M., Rogers P.H., Arnone A. A third quaternary structure of human hemoglobin A at 1.7 Å resolution. J. Biol. Chem. 267:1992;17248-17256
    • (1992) J. Biol. Chem. , vol.267 , pp. 17248-17256
    • Silva, M.M.1    Rogers, P.H.2    Arnone, A.3
  • 29
    • 0026948866 scopus 로고
    • 1H NMR resonance assignment of hyperfine-shifted residues in the active site of a paramagnetic protein: Application to Aplysia cyano-metmyoglobin
    • 1H NMR resonance assignment of hyperfine-shifted residues in the active site of a paramagnetic protein: application to Aplysia cyano-metmyoglobin. J. Biomol. NMR. 2:1992;597-618
    • (1992) J. Biomol. NMR , vol.2 , pp. 597-618
    • Qin, J.1    La Mar, G.N.2
  • 31
    • 0019753767 scopus 로고
    • Preparation of hybrid hemoglobins with different prosthetic groups
    • Ikedo-Saito M., Inubishi T., Yonetani T. Preparation of hybrid hemoglobins with different prosthetic groups. Methods Enzymol. 76:1981;113-121
    • (1981) Methods Enzymol. , vol.76 , pp. 113-121
    • Ikedo-Saito, M.1    Inubishi, T.2    Yonetani, T.3
  • 32
    • 0024409683 scopus 로고
    • Proton NMR investigation of the influence of subunit assembly on the low-spin reversible high-spin equilibrium of met-azido hemoglobin a
    • Yamamoto Y., La Mar G.N. Proton NMR investigation of the influence of subunit assembly on the low-spin reversible high-spin equilibrium of met-azido hemoglobin A. Biochim. Biophys. Acta. 996:1989;187-194
    • (1989) Biochim. Biophys. Acta , vol.996 , pp. 187-194
    • Yamamoto, Y.1    La Mar, G.N.2
  • 34
    • 0001021790 scopus 로고
    • Dynamic range problem in Fourier transform NMR. Modified WEFT pulse sequence
    • Gupta R.K. Dynamic range problem in Fourier transform NMR. Modified WEFT pulse sequence. J. Magn. Reson. 24:1976;461-465
    • (1976) J. Magn. Reson. , vol.24 , pp. 461-465
    • Gupta, R.K.1
  • 35
    • 0343359244 scopus 로고
    • Investigation of exchange processes by two dimensional NMR spectroscopy
    • Jeener J., Meier B.H., Bachmann P., Ernst R.R. Investigation of exchange processes by two dimensional NMR spectroscopy. J. Chem. Phys. 71:1979;4546-4553
    • (1979) J. Chem. Phys. , vol.71 , pp. 4546-4553
    • Jeener, J.1    Meier, B.H.2    Bachmann, P.3    Ernst, R.R.4
  • 37
    • 0014814578 scopus 로고
    • Nonlinear regression with linear constraints: An extension of the magnified diagonal method
    • Shrager R.I. Nonlinear regression with linear constraints: an extension of the magnified diagonal method. J. Assoc. Comput. Mach. 17:1970;446-452
    • (1970) J. Assoc. Comput. Mach. , vol.17 , pp. 446-452
    • Shrager, R.I.1
  • 39
    • 0023746661 scopus 로고
    • Assignment of proton resonances in the NMR spectrum of carbonmonoxy hemoglobin beta subunit tetramers
    • Craescu C.T., Mispelter J. Assignment of proton resonances in the NMR spectrum of carbonmonoxy hemoglobin beta subunit tetramers. Eur. J. Biochem. 176:1988;171-178
    • (1988) Eur. J. Biochem. , vol.176 , pp. 171-178
    • Craescu, C.T.1    Mispelter, J.2
  • 40
    • 0024605026 scopus 로고
    • 1H NMR spectrum of carbonmonoxy hemoglobin by 2D methods
    • 1H NMR spectrum of carbonmonoxy hemoglobin by 2D methods. Eur. J. Biochem. 181:1989;87-96
    • (1989) Eur. J. Biochem. , vol.181 , pp. 87-96
    • Craescu, C.T.1    Mispelter, J.2
  • 41
    • 0027198105 scopus 로고
    • Solution NMR determination of active site structure for a paramagnetic protein: Cyano-met Aplysia Mb
    • Qin J., La Mar G.N., Ascoli F., Brunori M. Solution NMR determination of active site structure for a paramagnetic protein: cyano-met Aplysia Mb. J. Mol. Biol. 231:1993;1009-1023
    • (1993) J. Mol. Biol. , vol.231 , pp. 1009-1023
    • Qin, J.1    La Mar, G.N.2    Ascoli, F.3    Brunori, M.4
  • 42
    • 84985733652 scopus 로고
    • 1H NMR parameters of the common amino acid residues measured in aqueous solutions of the linear tetrapeptides H-Gly-Gly-X-L-Ala-OH
    • 1H NMR parameters of the common amino acid residues measured in aqueous solutions of the linear tetrapeptides H-Gly-Gly-X-L-Ala-OH. Biopolymers. 18:1979;285-297
    • (1979) Biopolymers , vol.18 , pp. 285-297
    • Bundi, A.1    Wüthrich, K.2
  • 43
    • 0026410969 scopus 로고
    • Relationship between nuclear magnetic resonance chemical shift and protein secondary structure
    • Wishart D.S., Sykes B.D., Richards F.M. Relationship between nuclear magnetic resonance chemical shift and protein secondary structure. J. Mol. Biol. 222:1991;311-333
    • (1991) J. Mol. Biol. , vol.222 , pp. 311-333
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 45
    • 0000895627 scopus 로고
    • Calibration of ring-current models for the Heme ring
    • Cross K.J., Wright P.E. Calibration of ring-current models for the Heme ring. J. Magn. Reson. 64:1985;220-231
    • (1985) J. Magn. Reson. , vol.64 , pp. 220-231
    • Cross, K.J.1    Wright, P.E.2
  • 46
    • 0008413559 scopus 로고    scopus 로고
    • M.W.W. Adams, & R.M. Kelly. San Diego: Academic Press
    • La Mar G.N. Adams M.W.W., Kelly R.M. Methods in Enzymology. 2001;351-389 Academic Press, San Diego
    • (2001) Methods in Enzymology , pp. 351-389
    • La Mar, G.N.1
  • 48
    • 0026611311 scopus 로고
    • 1H NMR determination of hydrogen bonding of the E10(66) arg side chain to the bound ligand in Aplysia cyano-met myoglobin
    • 1H NMR determination of hydrogen bonding of the E10(66) arg side chain to the bound ligand in Aplysia cyano-met myoglobin. J. Mol. Biol. 224:1992;891-897
    • (1992) J. Mol. Biol. , vol.224 , pp. 891-897
    • Qin, J.1    La Mar, G.N.2    Ascoli, F.3    Bolognesi, M.4    Brunori, M.5
  • 49
    • 0028303641 scopus 로고
    • Correlation between the steric bulk of the distal E7 and E11 residues and the tilt of the Fe-CN unit in cyanometmyoglobin as determined by NMR from the orientation of the magnetic axes in single and double point mutants
    • Rajarathnam K., Qin J., La Mar G.N., Chiu M.L., Sligar S.G. Correlation between the steric bulk of the distal E7 and E11 residues and the tilt of the Fe-CN unit in cyanometmyoglobin as determined by NMR from the orientation of the magnetic axes in single and double point mutants. Biochemistry. 33:1994;5493-5501
    • (1994) Biochemistry , vol.33 , pp. 5493-5501
    • Rajarathnam, K.1    Qin, J.2    La Mar, G.N.3    Chiu, M.L.4    Sligar, S.G.5
  • 52
    • 0033527447 scopus 로고    scopus 로고
    • 1H NMR investigation of the distal hydrogen bonding network and ligand tilt in the cyanomet complex of oxygen-avid Ascaris hemoglobin
    • 1H NMR investigation of the distal hydrogen bonding network and ligand tilt in the cyanomet complex of oxygen-avid Ascaris hemoglobin. J. Biol. Chem. 274:1999;31819-31826
    • (1999) J. Biol. Chem. , vol.274 , pp. 31819-31826
    • Xia, Z.1    Zhang, W.2    Nguyen, B.D.3    Kloek, A.P.4    Goldberg, D.E.5    La Mar, G.N.6
  • 53
    • 0038682731 scopus 로고    scopus 로고
    • 1H NMR characterization by equilibrium heme orientational disorder with functional consequence in mouse neuroglobin
    • 1H NMR characterization by equilibrium heme orientational disorder with functional consequence in mouse neuroglobin. J. Am. Chem. Soc. 125:2003;8080-8081
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 8080-8081
    • Du, W.1    Syvitski, R.T.2    Dewilde, S.3    Moens, L.4    La Mar, G.N.5
  • 54
    • 0015803280 scopus 로고
    • Evaluation of dipolar nuclear magnetic resonance shifts in low-spin hemin systems: Ferricytochrome c and metmyoglobin cyanide
    • Horrocks W.D. Jr., Greenberg E.S. Evaluation of dipolar nuclear magnetic resonance shifts in low-spin hemin systems: ferricytochrome c and metmyoglobin cyanide. Biochim. Biophys. Acta. 322:1973;38-44
    • (1973) Biochim. Biophys. Acta , vol.322 , pp. 38-44
    • Horrocks Jr., W.D.1    Greenberg, E.S.2
  • 55
    • 0342945169 scopus 로고
    • Isotropic nuclear magnetic resonance shifts in low-spin iron(III) porphyrin and hemin systems. Theoretical interpretation of temperature dependencies
    • Horrocks W.D. Jr., Greenberg E.S. Isotropic nuclear magnetic resonance shifts in low-spin iron(III) porphyrin and hemin systems. Theoretical interpretation of temperature dependencies. Mol. Phys. 27:1974;993-999
    • (1974) Mol. Phys. , vol.27 , pp. 993-999
    • Horrocks Jr., W.D.1    Greenberg, E.S.2
  • 56
    • 0028851121 scopus 로고
    • 13C-NMR: The effect of the axial ligands
    • 13C-NMR: the effect of the axial ligands. Eur. J. Biochem. 227:1995;829-837
    • (1995) Eur. J. Biochem. , vol.227 , pp. 829-837
    • Turner, D.L.1
  • 57
    • 33751154489 scopus 로고
    • 1H contact shifts in low-spin Fe(III) model hemes and heme proteins: Explanation of "curie" and "anti-Curie" behavior within the same molecule
    • 1H contact shifts in low-spin Fe(III) model hemes and heme proteins: explanation of "Curie" and "anti-Curie" behavior within the same molecule. J. Phys. Chem. 99:1995;17795-17804
    • (1995) J. Phys. Chem. , vol.99 , pp. 17795-17804
    • Shokhirev, N.V.1    Walker, F.A.2
  • 58
    • 0035834045 scopus 로고    scopus 로고
    • Probing the importance of the amino terminal sequence of the beta- and the gamma-chains to the properties of normal adult and fetal hemoglobins
    • Tsai C.-H., Larson S.C., Shen T.J., Ho N.T., Fisher G.W., Tam M.F., Ho C. Probing the importance of the amino terminal sequence of the beta- and the gamma-chains to the properties of normal adult and fetal hemoglobins. Biochemistry. 40:2001;12169-12177
    • (2001) Biochemistry , vol.40 , pp. 12169-12177
    • Tsai, C.-H.1    Larson, S.C.2    Shen, T.J.3    Ho, N.T.4    Fisher, G.W.5    Tam, M.F.6    Ho, C.7
  • 59
    • 0028167480 scopus 로고
    • 4 hemoglobin. Analysis of the partitioning of quaternary-associated and ligand-induced changes in tertiary structure
    • 4 hemoglobin. Analysis of the partitioning of quaternary-associated and ligand-induced changes in tertiary structure. J. Mol. Biol. 236:1994;831-843
    • (1994) J. Mol. Biol. , vol.236 , pp. 831-843
    • Borgstahl, G.E.O.1    Rogers, P.H.2    Arnone, A.3


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