메뉴 건너뛰기




Volumn 91, Issue 9, 2006, Pages 3529-3541

Structure-function relationship in a variant hemoglobin: A combined computational-experimental approach

Author keywords

[No Author keywords available]

Indexed keywords

HEMOGLOBIN VARIANT; PROLINE;

EID: 33751342723     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.106.083170     Document Type: Article
Times cited : (12)

References (59)
  • 1
    • 1842483305 scopus 로고    scopus 로고
    • The structure-function relationship of hemoglobin in solution at atomic resolution
    • Lukin, J. A., and C. Ho. 2004. The structure-function relationship of hemoglobin in solution at atomic resolution. Chem. Rev. 104:1219-1230.
    • (2004) Chem. Rev. , vol.104 , pp. 1219-1230
    • Lukin, J.A.1    Ho, C.2
  • 2
    • 0001793063 scopus 로고
    • Preparation of haemoglobin crystals
    • Perutz, M. F. 1968. Preparation of haemoglobin crystals. J. Cryst. Growth. 2:54-56.
    • (1968) J. Cryst. Growth. , vol.2 , pp. 54-56
    • Perutz, M.F.1
  • 6
    • 0026619765 scopus 로고
    • Proton nuclear magnetic resonance studies on hemoglobin cooperative interactions and partially ligated intermediates
    • Ho, C. 1992. Proton nuclear magnetic resonance studies on hemoglobin cooperative interactions and partially ligated intermediates. Adv. Protein Chem. 43:153-312.
    • (1992) Adv. Protein Chem. , vol.43 , pp. 153-312
    • Ho, C.1
  • 7
    • 0028360904 scopus 로고
    • Proton nuclear magnetic resonance studies of hemoglobin
    • Ho, C., and J. R. Perussi. 1994. Proton nuclear magnetic resonance studies of hemoglobin. Methods Enzymol. 232:97-139.
    • (1994) Methods Enzymol , vol.232 , pp. 97-139
    • Ho, C.1    Perussi, J.R.2
  • 8
    • 0032834006 scopus 로고    scopus 로고
    • Recombinant hemoglobin (αα29leucine→ phenylalanine, α96valine→tryptophan, β108asparagine→lysine) exhibits low oxygen affinity and high cooperativity combined with resistance to autoxidation
    • Jeong, S. T., N. T. Ho, M. P. Hendrich, and C. Ho. 1999. Recombinant hemoglobin (αα29leucine→ phenylalanine, α96valine→ tryptophan, β108asparagine→lysine) exhibits low oxygen affinity and high cooperativity combined with resistance to autoxidation. Biochemistry. 38:13433-13442.
    • (1999) Biochemistry , vol.38 , pp. 13433-13442
    • Jeong, S.T.1    Ho, N.T.2    Hendrich, M.P.3    Ho, C.4
  • 9
    • 0037438352 scopus 로고    scopus 로고
    • Site mutations disrupt inter-helical H-bonds (α14W-α67T and β15W-β72s) involved in kinetic steps in the hemoglobin R→T transition without altering the free energies of oxygenation
    • Tsai, C. H., V. Simplaceanu, N. T. Ho, T. J. Shen, D. Wang, T. G. Spiro, and C. Ho. 2003. Site mutations disrupt inter-helical H-bonds (α14W-α67T and β15W-β72s) involved in kinetic steps in the hemoglobin R→T transition without altering the free energies of oxygenation. Biophys. Chem. 100:131-142.
    • (2003) Biophys. Chem. , vol.100 , pp. 131-142
    • Tsai, C.H.1    Simplaceanu, V.2    Ho, N.T.3    Shen, T.J.4    Wang, D.5    Spiro, T.G.6    Ho, C.7
  • 10
    • 0034649341 scopus 로고    scopus 로고
    • An additional H-Bond in the α1β2 interface as the structural basis for the low oxygen affinity and high cooperativity of a novel recombinant hemoglobin (βL105W)
    • Fang, T. Y., V. Simplaceanu, C. H. Tsai, N. T. Ho, and C. Ho. 2000. An additional H-Bond in the α1β2 interface as the structural basis for the low oxygen affinity and high cooperativity of a novel recombinant hemoglobin (βL105W). Biochemistry. 30:13708-13718.
    • (2000) Biochemistry , vol.30 , pp. 13708-13718
    • Fang, T.Y.1    Simplaceanu, V.2    Tsai, C.H.3    Ho, N.T.4    Ho, C.5
  • 11
    • 0038713404 scopus 로고    scopus 로고
    • Mechanisms of selectivity in channels and enzymes studied with interactive molecular dynamics
    • Grayson, P., E. Tajkhorshid, and K. Schulten. 2003. Mechanisms of selectivity in channels and enzymes studied with interactive molecular dynamics. Biophys. J. 85:36-48.
    • (2003) Biophys. J. , vol.85 , pp. 36-48
    • Grayson, P.1    Tajkhorshid, E.2    Schulten, K.3
  • 13
    • 1842481352 scopus 로고    scopus 로고
    • Extending the molecular modeling methodology to study insertion of membrane nanopores
    • Aksimentiev, A., and K. Schulten. 2004. Extending the molecular modeling methodology to study insertion of membrane nanopores. Proc. Natl. Acad. Sci. USA. 101:4337-4338.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 4337-4338
    • Aksimentiev, A.1    Schulten, K.2
  • 14
    • 3042772813 scopus 로고    scopus 로고
    • Microscopic mechanism of antibiotics translocation through a porin
    • Ceccarelli, M., C. Danelon, A. Laio, and M. Parrinello. 2004. Microscopic mechanism of antibiotics translocation through a porin. Biophys. J. 87:58-64.
    • (2004) Biophys. J. , vol.87 , pp. 58-64
    • Ceccarelli, M.1    Danelon, C.2    Laio, A.3    Parrinello, M.4
  • 15
    • 0029024086 scopus 로고
    • A novel low oxygen affinity recombinant hemoglobin (α96Val→ Trp): Switching quaternary structure without changing the ligation state
    • Kim, H. W., T. J. Shen, D. P. Sun, N. T. Ho, M. Madrid, M. F. Tam, and C. Ho. 1995. A novel low oxygen affinity recombinant hemoglobin (α96Val→Trp): switching quaternary structure without changing the ligation state. J. Mol. Biol. 248:867-882.
    • (1995) J. Mol. Biol. , vol.248 , pp. 867-882
    • Kim, H.W.1    Shen, T.J.2    Sun, D.P.3    Ho, N.T.4    Madrid, M.5    Tam, M.F.6    Ho, C.7
  • 16
    • 0032580999 scopus 로고    scopus 로고
    • Novel water-mediated hydrogen bonds as the structural basis for the low oxygen affinity of the blood substitute candidate rHb (α96Val→Trp)
    • Puius, Y. A., M. Zou, N. T. Ho, C. Ho, and S. C. Almo. 1998. Novel water-mediated hydrogen bonds as the structural basis for the low oxygen affinity of the blood substitute candidate rHb (α96Val→Trp). Biochemistry. 37:9258-9265.
    • (1998) Biochemistry , vol.37 , pp. 9258-9265
    • Puius, Y.A.1    Zou, M.2    Ho, N.T.3    Ho, C.4    Almo, S.C.5
  • 17
    • 18844436222 scopus 로고    scopus 로고
    • Hemoglobins with high oxygen affinity leading to erythrocytosis. New variants and new concepts
    • Wajcman, H., and F. Galacteros. 2005. Hemoglobins with high oxygen affinity leading to erythrocytosis. New variants and new concepts. Hemoglobin. 29:91-106.
    • (2005) Hemoglobin , vol.29 , pp. 91-106
    • Wajcman, H.1    Galacteros, F.2
  • 19
    • 0036799444 scopus 로고    scopus 로고
    • Identification and functional characterization of a new hemoglobin variant in Sardinia: Hb Muravera [β47GAT→GTT, (CD6)Asp→Val]
    • Corda, M., A. Fais, L. Perseu, L. Cipollina, S. Barella, and R. Galanello. 2002. Identification and functional characterization of a new hemoglobin variant in Sardinia: Hb Muravera [β47GAT→GTT, (CD6)Asp→Val]. Haematologica. 87:1111-1112.
    • (2002) Haematologica , vol.87 , pp. 1111-1112
    • Corda, M.1    Fais, A.2    Perseu, L.3    Cipollina, L.4    Barella, S.5    Galanello, R.6
  • 20
  • 21
    • 0016364150 scopus 로고
    • Hemoglobin Duarte: (α2β2 62(E6)Ala leads to Pro): A new unstable hemoglobin with increased oxygen affinity
    • Beutler, E., A. Lang, and H. Lehmann. 1974. Hemoglobin Duarte: (α2β2 62(E6)Ala leads to Pro): a new unstable hemoglobin with increased oxygen affinity. Blood. 43:527-535.
    • (1974) Blood , vol.43 , pp. 527-535
    • Beutler, E.1    Lang, A.2    Lehmann, H.3
  • 23
    • 0029769272 scopus 로고    scopus 로고
    • Hb J-Europa [β 62(E6)Ala→Asp]: Normal oxygen binding properties in a new variant involving a residue located distal to the heme
    • Kiger, L., J. Kister, P. Groff, G. Kalmes, D. Promé, F. Galactéros, and H. Wajcman. 1996. Hb J-Europa [β 62(E6)Ala→Asp]: normal oxygen binding properties in a new variant involving a residue located distal to the heme. Hemoglobin. 20:135-140.
    • (1996) Hemoglobin , vol.20 , pp. 135-140
    • Kiger, L.1    Kister, J.2    Groff, P.3    Kalmes, G.4    Promé, D.5    Galactéros, F.6    Wajcman, H.7
  • 25
    • 0025760401 scopus 로고
    • Detection of the common Hb F Sardinia [A γ(E19)Ile - Thr] variant by isoelectric focusing in normal newborns and in adults affected by elevated fetal hemoglobin syndromes
    • Masala, B., and L. Manca. 1991. Detection of the common Hb F Sardinia [A γ(E19)Ile - Thr] variant by isoelectric focusing in normal newborns and in adults affected by elevated fetal hemoglobin syndromes. Clin. Chim. Acta. 198:195-202.
    • (1991) Clin. Chim. Acta , vol.198 , pp. 195-202
    • Masala, B.1    Manca, L.2
  • 26
    • 0019751816 scopus 로고
    • Measurement of binding of gaseous and nongaseous ligands to hemoglobins by conventional spectrophotometric procedures
    • Giardina, B., and G. Amiconi. 1981. Measurement of binding of gaseous and nongaseous ligands to hemoglobins by conventional spectrophotometric procedures. Methods Enzymol. 76:417-427.
    • (1981) Methods Enzymol , vol.76 , pp. 417-427
    • Giardina, B.1    Amiconi, G.2
  • 27
    • 0010262629 scopus 로고    scopus 로고
    • ORAC: A molecular dynamics program to simulate complex molecular systems with realistic electrostatic interactions
    • Procacci, P., E. Paci, T. Darden, and M. Marchi. 1997. ORAC: a molecular dynamics program to simulate complex molecular systems with realistic electrostatic interactions. J. Comput. Chem. 18:1848-1862.
    • (1997) J. Comput. Chem. , vol.18 , pp. 1848-1862
    • Procacci, P.1    Paci, E.2    Darden, T.3    Marchi, M.4
  • 31
    • 0013603851 scopus 로고    scopus 로고
    • Taming the Ewald sum in molecular dynamics simulations of solvated proteins via a multiple time step algorithm
    • Procacci, P., and M. Marchi. 1996. Taming the Ewald sum in molecular dynamics simulations of solvated proteins via a multiple time step algorithm. J. Chem. Phys. 104:3003-3012.
    • (1996) J. Chem. Phys. , vol.104 , pp. 3003-3012
    • Procacci, P.1    Marchi, M.2
  • 32
    • 0033891899 scopus 로고    scopus 로고
    • Chain-selective isotopic labeling for NMR studies of large multimeric proteins: Application to hemoglobin
    • Simplaceanu, V., J. A. Lukin, T.-Y. Fang, M. Zou, N. T. Ho, and C. Ho. 2000. Chain-selective isotopic labeling for NMR studies of large multimeric proteins: application to hemoglobin. Biophys. J. 79:1146-1154.
    • (2000) Biophys. J. , vol.79 , pp. 1146-1154
    • Simplaceanu, V.1    Lukin, J.A.2    Fang, T.-Y.3    Zou, M.4    Ho, N.T.5    Ho, C.6
  • 33
    • 0034538248 scopus 로고    scopus 로고
    • First-principles molecular dynamics simulations of models for the myoglobins active center
    • Rovira, C., and M. Parrinello. 2000. First-principles molecular dynamics simulations of models for the myoglobins active center. Int. J. Quantum. Chem. 80:1172-1180.
    • (2000) Int. J. Quantum. Chem. , vol.80 , pp. 1172-1180
    • Rovira, C.1    Parrinello, M.2
  • 34
    • 0034951055 scopus 로고    scopus 로고
    • Influence of the heme pocket conformation on the structure and vibrations of the Fe-CO bond in myoglobins: A QM/MM density functional study
    • Rovira, C., B. Schulze, M. Eichinger, J. D. Evanseck, and M. Parrinello. 2001. Influence of the heme pocket conformation on the structure and vibrations of the Fe-CO bond in myoglobins: a QM/MM density functional study. Biophys. J. 81:435-445.
    • (2001) Biophys. J. , vol.81 , pp. 435-445
    • Rovira, C.1    Schulze, B.2    Eichinger, M.3    Evanseck, J.D.4    Parrinello, M.5
  • 35
    • 0019707626 scopus 로고
    • Polymorphic transitions in single crystals: A new molecular dynamics method
    • Parrinello, M., and A. Rahman. 1981. Polymorphic transitions in single crystals: a new molecular dynamics method. J. Appl. Phys. 52:7182-7190.
    • (1981) J. Appl. Phys. , vol.52 , pp. 7182-7190
    • Parrinello, M.1    Rahman, A.2
  • 36
    • 0002906346 scopus 로고    scopus 로고
    • Vol. F. M. G. Rossman and E. Arnold, editors. Kluwer Academic Publishers, Dordrecht, The Netherlands. Chapter 17.1
    • Kleywegt, G. J., J. Y. Zou, M. Kjeldgaard, and T. A. Jones. 2001. In International Tables for Crystallography, Vol. F. M. G. Rossman and E. Arnold, editors. Kluwer Academic Publishers, Dordrecht, The Netherlands. 353-356. Chapter 17.1.
    • (2001) International Tables for Crystallography , pp. 353-356
    • Kleywegt, G.J.1    Zou, J.Y.2    Kjeldgaard, M.3    Jones, T.A.4
  • 37
    • 0027995683 scopus 로고
    • Detection, delineation, measurement and display of cavities in macromolecular structures
    • Kleywegt, G. J., and T. A. Jones. 1994. Detection, delineation, measurement and display of cavities in macromolecular structures. Acta Crystallogr. D50:178-185.
    • (1994) Acta Crystallogr. , vol.D50 , pp. 178-185
    • Kleywegt, G.J.1    Jones, T.A.2
  • 38
    • 0027159949 scopus 로고
    • The molecular surface package
    • Connolly, M. L. 1993. The molecular surface package. J. Mol. Graph. 11:139-143.
    • (1993) J. Mol. Graph. , vol.11 , pp. 139-143
    • Connolly, M.L.1
  • 41
    • 0030941242 scopus 로고    scopus 로고
    • Contribution of surface histidyl residues in the alpha-chain to the Bohr effect of human normal adult hemoglobin: Roles of global electrostatic effect
    • Sun, D. P., M. Zou, N. T. Ho, and C. Ho. 1997. Contribution of surface histidyl residues in the alpha-chain to the Bohr effect of human normal adult hemoglobin: roles of global electrostatic effect. Biochemistry. 36:6663-6673.
    • (1997) Biochemistry , vol.36 , pp. 6663-6673
    • Sun, D.P.1    Zou, M.2    Ho, N.T.3    Ho, C.4
  • 42
    • 0019174818 scopus 로고
    • Proton nuclear magnetic resonance studies of hemoglobins M Boston (α58E7His→Tyr) and M Milwaukee (β67E11 Val→Glu): Spectral assignments of hyperfine-shifted proton resonances and of proximal histidine (E7) NH resonances to the α and β chains of normal adult hemoglobin
    • Takahashi, S., A. K. C. Lin, and C. Ho. 1980. Proton nuclear magnetic resonance studies of hemoglobins M Boston (α58E7His→Tyr) and M Milwaukee (β67E11 Val→Glu): spectral assignments of hyperfine-shifted proton resonances and of proximal histidine (E7) NH resonances to the α and β chains of normal adult hemoglobin. Biochemistry. 19:5196-5202.
    • (1980) Biochemistry , vol.19 , pp. 5196-5202
    • Takahashi, S.1    Lin, A.K.C.2    Ho, C.3
  • 43
    • 0019161187 scopus 로고
    • Assignment of proximal histidyl imidazole exchangeable proton NMR resonances to individual subunits in hemoglobins A, Boston, Iwate and Milwaukee. Biochem Biophys
    • La Mar, G. N., K. Nagai, T. Jue, D. L. Budd, K. Gersonde, H. Sick, T. Kagimoto, A. Hayashi, and F. Takeda. 1980. Assignment of proximal histidyl imidazole exchangeable proton NMR resonances to individual subunits in hemoglobins A, Boston, Iwate and Milwaukee. Biochem Biophys. Res. Commun. 96:1172-1177.
    • (1980) Res. Commun. , vol.96 , pp. 1172-1177
    • La Mar, G.N.1    Nagai, K.2    Jue, T.3    Budd, D.L.4    Gersonde, K.5    Sick, H.6    Kagimoto, T.7    Hayashi, A.8    Takeda, F.9
  • 44
    • 0016273084 scopus 로고
    • Effects of ligands and organic phosphates on functional properties of human adult hemoglobin
    • Johnson, M. E., and C. Ho. 1974. Effects of ligands and organic phosphates on functional properties of human adult hemoglobin. Biochemistry. 13:3653-3661.
    • (1974) Biochemistry , vol.13 , pp. 3653-3661
    • Johnson, M.E.1    Ho, C.2
  • 45
    • 0001018129 scopus 로고
    • Isotropic NMR shifts in transition metal complexes: The calculation of the Fermi contact and pseudocontact terms
    • Kurland, R. J., and B. R. McGarvey. 1970. Isotropic NMR shifts in transition metal complexes: the calculation of the Fermi contact and pseudocontact terms. J. Magn. Reson. 2:286-301.
    • (1970) J. Magn. Reson. , vol.2 , pp. 286-301
    • Kurland, R.J.1    McGarvey, B.R.2
  • 46
    • 0014958182 scopus 로고
    • Stereochemistry of cooperative effects in haemoglobin
    • Perutz, M. F. 1970. Stereochemistry of cooperative effects in haemoglobin. Nature. 228:226-233.
    • (1970) Nature , vol.228 , pp. 226-233
    • Perutz, M.F.1
  • 47
    • 0016756387 scopus 로고
    • A proton nuclear magnetic resonance study of the quaternary structure of human hemoglobins in water
    • Fung, L. W.-M., and C. Ho. 1975. A proton nuclear magnetic resonance study of the quaternary structure of human hemoglobins in water. Biochemistry. 14:2526-2535.
    • (1975) Biochemistry , vol.14 , pp. 2526-2535
    • Fung, L.W.-M.1    Ho, C.2
  • 48
    • 0026748898 scopus 로고
    • Site-directed mutagenesis in hemoglobin: Functional and structural role of inter- and intrasubunit hydrogen bonds as studied with 37β and 145β mutations
    • Ishimori, K., K. Imai, G. Miyazaki, T. Kitagawa, Y. Wada, H. Morimoto, and I. Morishima. 1992. Site-directed mutagenesis in hemoglobin: functional and structural role of inter- and intrasubunit hydrogen bonds as studied with 37β and 145β mutations. Biochemistry. 31:3256-3264.
    • (1992) Biochemistry , vol.31 , pp. 3256-3264
    • Ishimori, K.1    Imai, K.2    Miyazaki, G.3    Kitagawa, T.4    Wada, Y.5    Morimoto, H.6    Morishima, I.7
  • 49
    • 0037197658 scopus 로고    scopus 로고
    • Effects of amino acid substitution at β131 on the structure and properties of hemoglobin: Evidence for communication between α1β1 and α1β2 subunit interfaces
    • Chang, C. K., V. Simplaceanu, and C. Ho. 2002. Effects of amino acid substitution at β131 on the structure and properties of hemoglobin: evidence for communication between α1β1 and α1β2 subunit interfaces. Biochemistry. 41:5644-5655.
    • (2002) Biochemistry , vol.41 , pp. 5644-5655
    • Chang, C.K.1    Simplaceanu, V.2    Ho, C.3
  • 50
    • 0023243939 scopus 로고
    • A proton nuclear magnetic Overhauser effect investigation of the subunit interfaces in human normal adult hemoglobin
    • Russu, I. M., N. T. Ho, and C. Ho. 1987. A proton nuclear magnetic Overhauser effect investigation of the subunit interfaces in human normal adult hemoglobin. Biochim. Biophys. Acta. 914:40-48.
    • (1987) Biochim. Biophys. Acta , vol.914 , pp. 40-48
    • Russu, I.M.1    Ho, N.T.2    Ho, C.3
  • 51
    • 0036786309 scopus 로고    scopus 로고
    • Ligand binding properties and structural studies of recombinant and chemically modified hemoglobins altered at β93 cysteine
    • Cheng, Y., T.-J. Shen, V. Simplaceanu, and C. Ho. 2002. Ligand binding properties and structural studies of recombinant and chemically modified hemoglobins altered at β93 cysteine. Biochemistry. 41:11901-11913.
    • (2002) Biochemistry , vol.41 , pp. 11901-11913
    • Cheng, Y.1    Shen, T.-J.2    Simplaceanu, V.3    Ho, C.4
  • 52
    • 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
  • 55
    • 21644452454 scopus 로고    scopus 로고
    • Evidence for two geminate rebinding states following laser photolysis of R state hemoglobin encapsulated in wet silica gels
    • Sottini, S., S. Abbruzzetti, C. Viappiani, S. Bettati, L. Ronda, and A. Mozzarelli. 2005. Evidence for two geminate rebinding states following laser photolysis of R state hemoglobin encapsulated in wet silica gels. J. Phys. Chem. B. 109:11411-11413.
    • (2005) J. Phys. Chem. B , vol.109 , pp. 11411-11413
    • Sottini, S.1    Abbruzzetti, S.2    Viappiani, C.3    Bettati, S.4    Ronda, L.5    Mozzarelli, A.6
  • 56
    • 1042299970 scopus 로고    scopus 로고
    • A kinetic description of dioxygen motion within α- and β-subunits of human hemoglobin in the R-state: Geminate and bimolecular stages of the oxygenation reaction
    • Lepeshkevich, S. V., J. Karpiuk, I. V. Sazanovich, and B. M. Dzhagarov. 2004. A kinetic description of dioxygen motion within α- and β-subunits of human hemoglobin in the R-state: geminate and bimolecular stages of the oxygenation reaction. Biochemistry. 43:1675-1684.
    • (2004) Biochemistry , vol.43 , pp. 1675-1684
    • Lepeshkevich, S.V.1    Karpiuk, J.2    Sazanovich, I.V.3    Dzhagarov, B.M.4
  • 57
    • 0034867130 scopus 로고    scopus 로고
    • Cavities and packing defects in the structural dynamics of myoglobins
    • Brunori, M., and Q. H. Gibson. 2001. Cavities and packing defects in the structural dynamics of myoglobins. EMBO Rep. 2:674-679.
    • (2001) EMBO Rep. , vol.2 , pp. 674-679
    • Brunori, M.1    Gibson, Q.H.2
  • 58
    • 4444253708 scopus 로고    scopus 로고
    • Coupling of protein relaxation to ligand binding and migration in myoglobins
    • Agmon, N. 2004. Coupling of protein relaxation to ligand binding and migration in myoglobins. Biophys. J. 87:1537-1543.
    • (2004) Biophys. J. , vol.87 , pp. 1537-1543
    • Agmon, N.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.