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Volumn 398, Issue 1-2 SPEC. ISS., 2007, Pages 208-223

Transient ligand docking sites in Cerebratulus lacteus mini-hemoglobin

Author keywords

Carbon monoxide; Fourier Transform Infrared Spectroscopy; Ligand migration; Photolysis

Indexed keywords

HEME; HEMOGLOBIN;

EID: 34447524874     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.gene.2007.01.037     Document Type: Article
Times cited : (10)

References (57)
  • 1
    • 0012284110 scopus 로고
    • Infrared spectroscopy of photodissociated carboxymyoglobin at low temperatures
    • Alben J.O., et al. Infrared spectroscopy of photodissociated carboxymyoglobin at low temperatures. Proc. Natl. Acad. Sci. U. S. A. 79 (1982) 3744-3748
    • (1982) Proc. Natl. Acad. Sci. U. S. A. , vol.79 , pp. 3744-3748
    • Alben, J.O.1
  • 2
    • 0025191367 scopus 로고
    • Temperature-derivative spectroscopy: a tool for protein dynamics
    • Berendzen J., and Braunstein D. Temperature-derivative spectroscopy: a tool for protein dynamics. Proc. Natl. Acad. Sci. U. S. A. 87 (1990) 1-5
    • (1990) Proc. Natl. Acad. Sci. U. S. A. , vol.87 , pp. 1-5
    • Berendzen, J.1    Braunstein, D.2
  • 3
    • 0041758430 scopus 로고    scopus 로고
    • Complex landscape of protein structural dynamics unveiled by nanosecond Laue crystallography Watching a protein as it functions with 150-ps time-resolved x-ray crystallography
    • Bourgeois D., et al. Complex landscape of protein structural dynamics unveiled by nanosecond Laue crystallography Watching a protein as it functions with 150-ps time-resolved x-ray crystallography. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 8704-8709
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 8704-8709
    • Bourgeois, D.1
  • 4
    • 0024110777 scopus 로고
    • Ligand binding to synthetic mutant myoglobin (His-E7-Gly): role of the distal histidine
    • Braunstein D., et al. Ligand binding to synthetic mutant myoglobin (His-E7-Gly): role of the distal histidine. Proc. Natl. Acad. Sci. U. S. A. 85 (1988) 8497-8501
    • (1988) Proc. Natl. Acad. Sci. U. S. A. , vol.85 , pp. 8497-8501
    • Braunstein, D.1
  • 5
    • 0027131994 scopus 로고
    • Ligand binding to heme proteins: III. FTIR studies of His-E7 and Val-E11 mutants of carbonmonoxymyoglobin
    • Braunstein D.P., et al. Ligand binding to heme proteins: III. FTIR studies of His-E7 and Val-E11 mutants of carbonmonoxymyoglobin. Biophys. J. 65 (1993) 2447-2454
    • (1993) Biophys. J. , vol.65 , pp. 2447-2454
    • Braunstein, D.P.1
  • 6
    • 35448945261 scopus 로고    scopus 로고
    • Bredenbeck, J., Helbing, J., Nienhaus, K., Nienhaus, G.U., Hamm, P., in press. Protein Ligand Migration Mapped by Nonequilibrium 2D-IR Exchange Spectroscopy. Proc. Natl. Acad. Sci. USA. doi:10.1073/pnas.0607758104.
  • 7
    • 0033019674 scopus 로고    scopus 로고
    • Structural dynamics of ligand diffusion in the protein matrix: a study on a new myoglobin mutant Y(B10) Q(E7) R(E10)
    • Brunori M., et al. Structural dynamics of ligand diffusion in the protein matrix: a study on a new myoglobin mutant Y(B10) Q(E7) R(E10). Biophys. J. 76 (1999) 1259-1269
    • (1999) Biophys. J. , vol.76 , pp. 1259-1269
    • Brunori, M.1
  • 8
    • 0034091637 scopus 로고    scopus 로고
    • The role of cavities in protein dynamics: crystal structure of a photolytic intermediate of a mutant myoglobin
    • Brunori M., et al. The role of cavities in protein dynamics: crystal structure of a photolytic intermediate of a mutant myoglobin. Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 2058-2063
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 2058-2063
    • Brunori, M.1
  • 9
    • 0000822382 scopus 로고
    • Light-induced and thermal relaxation in a protein
    • Chu K., et al. Light-induced and thermal relaxation in a protein. Phys. Rev. Lett. 74 (1995) 2607-2610
    • (1995) Phys. Rev. Lett. , vol.74 , pp. 2607-2610
    • Chu, K.1
  • 10
    • 0034708201 scopus 로고    scopus 로고
    • Structure of a ligand-binding intermediate in wild-type carbonmonoxy myoglobin
    • Chu K., et al. Structure of a ligand-binding intermediate in wild-type carbonmonoxy myoglobin. Nature 403 (2000) 921-923
    • (2000) Nature , vol.403 , pp. 921-923
    • Chu, K.1
  • 12
    • 0026320866 scopus 로고
    • The energy landscapes and motions of proteins
    • Frauenfelder H., Sligar S.G., and Wolynes P.G. The energy landscapes and motions of proteins. Science 254 (1991) 1598-1603
    • (1991) Science , vol.254 , pp. 1598-1603
    • Frauenfelder, H.1    Sligar, S.G.2    Wolynes, P.G.3
  • 13
    • 0029901733 scopus 로고    scopus 로고
    • X-ray structure determination of a metastable state of carbonmonoxy myoglobin after photodissociation
    • Hartmann H., et al. X-ray structure determination of a metastable state of carbonmonoxy myoglobin after photodissociation. Proc. Natl. Acad. Sci. U. S. A. 93 (1996) 7013-7016
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 7013-7016
    • Hartmann, H.1
  • 15
    • 0029762039 scopus 로고    scopus 로고
    • Ligand binding to heme proteins. VI. Interconversion of taxonomic substates in carbonmonoxymyoglobin
    • Johnson J.B., et al. Ligand binding to heme proteins. VI. Interconversion of taxonomic substates in carbonmonoxymyoglobin. Biophys. J. 71 (1996) 1563-1573
    • (1996) Biophys. J. , vol.71 , pp. 1563-1573
    • Johnson, J.B.1
  • 17
    • 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., et al. Structural dynamics of myoglobin: ligand migration among protein cavities studied by Fourier transform infrared/temperature derivative spectroscopy. J. Biol. Chem. 277 (2002) 11636-11644
    • (2002) J. Biol. Chem. , vol.277 , pp. 11636-11644
    • Lamb, D.C.1
  • 18
    • 1642619052 scopus 로고    scopus 로고
    • Structural dynamics of myoglobin: an infrared kinetic study of ligand migration in mutants YQR and YQRF
    • Lamb D.C., et al. Structural dynamics of myoglobin: an infrared kinetic study of ligand migration in mutants YQR and YQRF. Biophys. Chem. 109 (2004) 41-58
    • (2004) Biophys. Chem. , vol.109 , pp. 41-58
    • Lamb, D.C.1
  • 19
    • 21244460042 scopus 로고    scopus 로고
    • Probing electric fields in protein cavities by using the vibrational Stark effect of carbon monoxide
    • Lehle H., et al. Probing electric fields in protein cavities by using the vibrational Stark effect of carbon monoxide. Biophys. J. 8 (2005) 1978-1990
    • (2005) Biophys. J. , vol.8 , pp. 1978-1990
    • Lehle, H.1
  • 20
    • 0028328331 scopus 로고
    • Structural determinants of the stretching frequency of CO bound to myoglobin
    • Li T., Quillin M.L., Phillips Jr. G.N., and Olson J.S. Structural determinants of the stretching frequency of CO bound to myoglobin. Biochemistry 33 (1994) 1433-1446
    • (1994) Biochemistry , vol.33 , pp. 1433-1446
    • Li, T.1    Quillin, M.L.2    Phillips Jr., G.N.3    Olson, J.S.4
  • 21
    • 0031054657 scopus 로고    scopus 로고
    • Ultrafast rotation and trapping of carbon monoxide dissociated from myoglobin
    • Lim M., Jackson T.A., and Anfinrud P.A. Ultrafast rotation and trapping of carbon monoxide dissociated from myoglobin. Nat. Struct. Biol. 4 (1997) 209-214
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 209-214
    • Lim, M.1    Jackson, T.A.2    Anfinrud, P.A.3
  • 22
    • 31944447153 scopus 로고    scopus 로고
    • Two distinct heme distal site states define Cerebratulus lacteus mini-hemoglobin oxygen affinity
    • Marti M.A., et al. Two distinct heme distal site states define Cerebratulus lacteus mini-hemoglobin oxygen affinity. Proteins 62 (2006) 641-648
    • (2006) Proteins , vol.62 , pp. 641-648
    • Marti, M.A.1
  • 23
    • 0035423114 scopus 로고    scopus 로고
    • 2 diffusion to the heme
    • 2 diffusion to the heme. EMBO J. 20 (2001) 3902-3909
    • (2001) EMBO J. , vol.20 , pp. 3902-3909
    • Milani, M.1
  • 24
    • 0036005629 scopus 로고    scopus 로고
    • Structural plasticity in the eight-helix fold of a trematode haemoglobin
    • Milani M., et al. Structural plasticity in the eight-helix fold of a trematode haemoglobin. Acta Crystallogr., D Biol. Crystallogr. 58 (2002) 719-722
    • (2002) Acta Crystallogr., D Biol. Crystallogr. , vol.58 , pp. 719-722
    • Milani, M.1
  • 25
    • 2442705539 scopus 로고    scopus 로고
    • Heme-ligand tunneling in group I truncated hemoglobins
    • Milani M., et al. Heme-ligand tunneling in group I truncated hemoglobins. J. Biol. Chem. 279 (2004) 21520-21525
    • (2004) J. Biol. Chem. , vol.279 , pp. 21520-21525
    • Milani, M.1
  • 26
    • 10444229578 scopus 로고    scopus 로고
    • Structural bases for heme binding and diatomic ligand recognition in truncated hemoglobins
    • Milani M., et al. Structural bases for heme binding and diatomic ligand recognition in truncated hemoglobins. J. Inorg. Biochem. 99 (2005) 97-109
    • (2005) J. Inorg. Biochem. , vol.99 , pp. 97-109
    • Milani, M.1
  • 27
    • 0027482810 scopus 로고
    • Ligand binding to heme proteins: II. Transitions in the heme pocket of myoglobin
    • Mourant J.R., et al. Ligand binding to heme proteins: II. Transitions in the heme pocket of myoglobin. Biophys. J. 65 (1993) 1496-1507
    • (1993) Biophys. J. , vol.65 , pp. 1496-1507
    • Mourant, J.R.1
  • 28
    • 0042030751 scopus 로고    scopus 로고
    • Connection between the taxonomic substates and protonation of histidines 64 and 97 in carbonmonoxy myoglobin
    • Müller J.D., McMahon B.H., Chien E.Y., Sligar S.G., and Nienhaus G.U. Connection between the taxonomic substates and protonation of histidines 64 and 97 in carbonmonoxy myoglobin. Biophys. J. 77 (1999) 1036-1051
    • (1999) Biophys. J. , vol.77 , pp. 1036-1051
    • Müller, J.D.1    McMahon, B.H.2    Chien, E.Y.3    Sligar, S.G.4    Nienhaus, G.U.5
  • 30
    • 0027992932 scopus 로고
    • Ligand binding to heme proteins: the effect of light on ligand binding in myoglobin
    • Nienhaus G.U., Mourant J.R., Chu K., and Frauenfelder H. Ligand binding to heme proteins: the effect of light on ligand binding in myoglobin. Biochemistry 33 (1994) 13413-13430
    • (1994) Biochemistry , vol.33 , pp. 13413-13430
    • Nienhaus, G.U.1    Mourant, J.R.2    Chu, K.3    Frauenfelder, H.4
  • 31
    • 0042242570 scopus 로고    scopus 로고
    • Structural dynamics of myoglobin: spectroscopic and structural characterization of ligand docking sites in myoglobin mutant L29W
    • Nienhaus K., Deng P., Kriegl J.M., and Nienhaus G.U. Structural dynamics of myoglobin: spectroscopic and structural characterization of ligand docking sites in myoglobin mutant L29W. Biochemistry 42 (2003) 9633-9646
    • (2003) Biochemistry , vol.42 , pp. 9633-9646
    • Nienhaus, K.1    Deng, P.2    Kriegl, J.M.3    Nienhaus, G.U.4
  • 32
    • 0041742184 scopus 로고    scopus 로고
    • Structural dynamics of myoglobin: the effect of internal cavities on ligand migration and binding
    • Nienhaus K., Deng P., Kriegl J.M., and Nienhaus G.U. Structural dynamics of myoglobin: the effect of internal cavities on ligand migration and binding. Biochemistry 42 (2003) 9647-9658
    • (2003) Biochemistry , vol.42 , pp. 9647-9658
    • Nienhaus, K.1    Deng, P.2    Kriegl, J.M.3    Nienhaus, G.U.4
  • 33
    • 0142242162 scopus 로고    scopus 로고
    • Structural dynamics of myoglobin: ligand migration and binding in valine 68 mutants
    • Nienhaus K., Deng P., Olson J.S., Warren J.J., and Nienhaus G.U. Structural dynamics of myoglobin: ligand migration and binding in valine 68 mutants. J. Biol. Chem. 278 (2003) 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
  • 35
    • 11844258850 scopus 로고    scopus 로고
    • The origin of Stark splitting in the initial photoproduct state of MbCO
    • Nienhaus K., Olson J.S., Franzen S., and Nienhaus G.U. The origin of Stark splitting in the initial photoproduct state of MbCO. J. Am .Chem. Soc. 127 (2005) 40-41
    • (2005) J. Am .Chem. Soc. , vol.127 , pp. 40-41
    • Nienhaus, K.1    Olson, J.S.2    Franzen, S.3    Nienhaus, G.U.4
  • 36
    • 0019765115 scopus 로고
    • Stopped-flow, rapid mixing measurements of ligand binding to hemoglobin and red cells
    • Olson J.S. Stopped-flow, rapid mixing measurements of ligand binding to hemoglobin and red cells. Methods Enzymol. 76 (1981) 631-651
    • (1981) Methods Enzymol. , vol.76 , pp. 631-651
    • Olson, J.S.1
  • 38
    • 0034624691 scopus 로고    scopus 로고
    • Ligand binding and conformational motions in myoglobin
    • Ostermann A., Waschipky R., Parak F.G., and Nienhaus G.U. Ligand binding and conformational motions in myoglobin. Nature 404 (2000) 205-208
    • (2000) Nature , vol.404 , pp. 205-208
    • Ostermann, A.1    Waschipky, R.2    Parak, F.G.3    Nienhaus, G.U.4
  • 39
    • 0001257322 scopus 로고    scopus 로고
    • Vibrational Stark spectroscopy in proteins: a probe and calibration fro electrostatic fields
    • Park E.S., Andrews S.S., Hu R.B., and Boxer S.G. Vibrational Stark spectroscopy in proteins: a probe and calibration fro electrostatic fields. J. Phys. Chem. B 103 (1999) 9813-9817
    • (1999) J. Phys. Chem. B , vol.103 , pp. 9813-9817
    • Park, E.S.1    Andrews, S.S.2    Hu, R.B.3    Boxer, S.G.4
  • 40
    • 0034213366 scopus 로고    scopus 로고
    • Pesce A., et al. EMBO J. 19 (2000) 2424-2434
    • (2000) EMBO J. , vol.19 , pp. 2424-2434
    • Pesce, A.1
  • 41
    • 0035207970 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray analysis of neural haemoglobin from the nemertean worm Cerebratulus lacteus
    • Pesce A., et al. Crystallization and preliminary X-ray analysis of neural haemoglobin from the nemertean worm Cerebratulus lacteus. Acta Crystallogr., D Biol. Crystallogr. 57 (2001) 1897-1899
    • (2001) Acta Crystallogr., D Biol. Crystallogr. , vol.57 , pp. 1897-1899
    • Pesce, A.1
  • 42
    • 0036098845 scopus 로고    scopus 로고
    • The 109 residue nerve tissue minihemoglobin from Cerebratulus lacteus highlights striking structural plasticity of the alpha-helical globin fold
    • Pesce A., et al. The 109 residue nerve tissue minihemoglobin from Cerebratulus lacteus highlights striking structural plasticity of the alpha-helical globin fold. Structure (Camb) 10 (2002) 725-735
    • (2002) Structure (Camb) , vol.10 , pp. 725-735
    • Pesce, A.1
  • 43
    • 4043170589 scopus 로고    scopus 로고
    • 2 affinity in Cerebratulus lacteus mini-hemoglobin
    • 2 affinity in Cerebratulus lacteus mini-hemoglobin. J. Biol. Chem. 279 (2004) 33662-33672
    • (2004) J. Biol. Chem. , vol.279 , pp. 33662-33672
    • Pesce, A.1
  • 45
    • 0025216601 scopus 로고
    • The effects of amino acid substitution at position E7 (residue 64) on the kinetics of ligand binding to sperm whale myoglobin
    • Rohlfs R.J., et al. The effects of amino acid substitution at position E7 (residue 64) on the kinetics of ligand binding to sperm whale myoglobin. J. Biol. Chem. 265 (1990) 3168-3176
    • (1990) J. Biol. Chem. , vol.265 , pp. 3168-3176
    • Rohlfs, R.J.1
  • 47
    • 23844539617 scopus 로고    scopus 로고
    • Ligand migration pathway and protein dynamics in myoglobin: a time-resolved crystallographic study on L29W MbCO
    • Schmidt M., et al. Ligand migration pathway and protein dynamics in myoglobin: a time-resolved crystallographic study on L29W MbCO. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 11704-11709
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 11704-11709
    • Schmidt, M.1
  • 48
    • 0038047431 scopus 로고    scopus 로고
    • Watching a protein as it functions with 150-ps time-resolved x-ray crystallography
    • Schotte F., et al. Watching a protein as it functions with 150-ps time-resolved x-ray crystallography. Science 300 (2003) 1944-1947
    • (2003) Science , vol.300 , pp. 1944-1947
    • Schotte, F.1
  • 49
    • 0030768765 scopus 로고    scopus 로고
    • Ligand migration in sperm whale myoglobin
    • Scott E.E., and Gibson Q.H. Ligand migration in sperm whale myoglobin. Biochemistry 36 (1997) 11909-11917
    • (1997) Biochemistry , vol.36 , pp. 11909-11917
    • Scott, E.E.1    Gibson, Q.H.2
  • 51
    • 0028519126 scopus 로고
    • Photolysis-induced structural changes in single crystals of carbonmonoxy myoglobin at 40 K
    • Teng T.Y., Srajer V., and Moffat K. Photolysis-induced structural changes in single crystals of carbonmonoxy myoglobin at 40 K. Nat. Struct. Biol. 1 (1994) 701-705
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 701-705
    • Teng, T.Y.1    Srajer, V.2    Moffat, K.3
  • 52
    • 0027453672 scopus 로고
    • Investigations of ligand association and dissociation rates in the "open" and "closed" states of myoglobin
    • Tian W.D., Sage J.T., and Champion P.M. Investigations of ligand association and dissociation rates in the "open" and "closed" states of myoglobin. J. Mol. Biol. 233 (1993) 155-166
    • (1993) J. Mol. Biol. , vol.233 , pp. 155-166
    • Tian, W.D.1    Sage, J.T.2    Champion, P.M.3
  • 53
    • 0032479053 scopus 로고    scopus 로고
    • The mini-hemoglobins in neural and body wall tissue of the nemertean worm, Cerebratulus lacteus
    • Vandergon T.L., Riggs C.K., Gorr T.A., Colacino J.M., and Riggs A.F. The mini-hemoglobins in neural and body wall tissue of the nemertean worm, Cerebratulus lacteus. J. Biol. Chem. 273 (1998) 16998-17011
    • (1998) J. Biol. Chem. , vol.273 , pp. 16998-17011
    • Vandergon, T.L.1    Riggs, C.K.2    Gorr, T.A.3    Colacino, J.M.4    Riggs, A.F.5
  • 54
    • 0033520701 scopus 로고    scopus 로고
    • Determinants of the FeXO (X= C, N, O) vibrational frequencies in heme adducts from experiment and density functional theory
    • Vogel K.M., Kozlowski P.M., Zgierski M.Z., and Spiro T.G. Determinants of the FeXO (X= C, N, O) vibrational frequencies in heme adducts from experiment and density functional theory. J. Am. Chem. Soc. 121 (1999) 9915-9921
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 9915-9921
    • Vogel, K.M.1    Kozlowski, P.M.2    Zgierski, M.Z.3    Spiro, T.G.4
  • 55
    • 0038853525 scopus 로고    scopus 로고
    • Crystal structures of myoglobin-ligand complexes at near-atomic resolution
    • Vojtechovsky J., Chu K., Berendzen J., Sweet R.M., and Schlichting I. Crystal structures of myoglobin-ligand complexes at near-atomic resolution. Biophys. J. 77 (1999) 2153-2174
    • (1999) Biophys. J. , vol.77 , pp. 2153-2174
    • Vojtechovsky, J.1    Chu, K.2    Berendzen, J.3    Sweet, R.M.4    Schlichting, I.5
  • 56
    • 0037059826 scopus 로고    scopus 로고
    • Truncated hemoglobins: a new family of hemoglobins widely distributed in bacteria, unicellular eukaryotes, and plants
    • Wittenberg J.B., Bolognesi M., Wittenberg B.A., and Guertin M. Truncated hemoglobins: a new family of hemoglobins widely distributed in bacteria, unicellular eukaryotes, and plants. J. Biol. Chem. 277 (2002) 871-874
    • (2002) J. Biol. Chem. , vol.277 , pp. 871-874
    • Wittenberg, J.B.1    Bolognesi, M.2    Wittenberg, B.A.3    Guertin, M.4
  • 57
    • 0029986887 scopus 로고    scopus 로고
    • Crystal structures of CO-, deoxy- and met-myoglobins at various pH values
    • Yang F., and Phillips Jr. G.N. Crystal structures of CO-, deoxy- and met-myoglobins at various pH values. J. Mol. Biol. 256 (1996) 762-774
    • (1996) J. Mol. Biol. , vol.256 , pp. 762-774
    • Yang, F.1    Phillips Jr., G.N.2


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