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Volumn 79, Issue 4, 2011, Pages 1143-1153

Crystal structure of the carbon monoxide complex of human cytoglobin

Author keywords

Conformational changes; Globin; Heme; Oxygen; X ray crystallography

Indexed keywords

CARBON MONOXIDE; CYTOGLOBIN; DROSOPHILA PROTEIN; FERROUS ION; HEMOGLOBIN; HISTIDINE; IMIDAZOLE; LIGAND; MYOGLOBIN; NEUROGLOBIN;

EID: 79952487366     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22950     Document Type: Article
Times cited : (21)

References (44)
  • 1
    • 0036219963 scopus 로고    scopus 로고
    • Cytoglobin: a novel globin type ubiquitously expressed in vertebrate tissues
    • Burmester T, Ebner B, Weich B, Hankeln T. Cytoglobin: a novel globin type ubiquitously expressed in vertebrate tissues. Mol Biol Evol 2002; 19: 416-421.
    • (2002) Mol Biol Evol , vol.19 , pp. 416-421
    • Burmester, T.1    Ebner, B.2    Weich, B.3    Hankeln, T.4
  • 2
    • 0035816696 scopus 로고    scopus 로고
    • Characterization of a stellate cell activation-associated protein (STAP) with peroxidase activity found in rat hepatic stellate cells
    • Kawada N, Kristensen DB, Asahina K, Nakatani K, Minamiyama Y, Seki S, Yoshizato K. Characterization of a stellate cell activation-associated protein (STAP) with peroxidase activity found in rat hepatic stellate cells. J Biol Chem 2001; 276: 25318-25323.
    • (2001) J Biol Chem , vol.276 , pp. 25318-25323
    • Kawada, N.1    Kristensen, D.2    Asahina, K.3    Nakatani, K.4    Minamiyama, Y.5    Seki, S.6    Yoshizato, K.7
  • 5
    • 0038333244 scopus 로고    scopus 로고
    • Characterization of the heme environmental structure of cytoglobin, a fourth globin in humans
    • Sawai H, Kawada N, Yoshizato K, Nakajima H, Aono S, Shiro Y. Characterization of the heme environmental structure of cytoglobin, a fourth globin in humans. Biochemistry 2003; 42: 5133-5142.
    • (2003) Biochemistry , vol.42 , pp. 5133-5142
    • Sawai, H.1    Kawada, N.2    Yoshizato, K.3    Nakajima, H.4    Aono, S.5    Shiro, Y.6
  • 9
    • 0035909992 scopus 로고    scopus 로고
    • Neuroglobin is up-regulated by and protects neurons from hypoxic-ischemic injury
    • Sun Y, Jin K, Mao XO, Zhu Y, Greenberg DA. Neuroglobin is up-regulated by and protects neurons from hypoxic-ischemic injury. Proc Natl Acad Sci USA 2001; 98: 15306-15311.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 15306-15311
    • Sun, Y.1    Jin, K.2    Mao, X.3    Zhu, Y.4    Greenberg, D.5
  • 12
    • 0037205447 scopus 로고    scopus 로고
    • A ubiquitously expressed human hexacoordinate hemoglobin
    • Trent JT, III, Hargrove MS. A ubiquitously expressed human hexacoordinate hemoglobin. J Biol Chem 2002; 277: 19538-19545.
    • (2002) J Biol Chem , vol.277 , pp. 19538-19545
    • Trent III, J.1    Hargrove, M.2
  • 13
    • 30744469606 scopus 로고    scopus 로고
    • Slow ligand binding kinetics dominate ferrous hexacoordinate hemoglobin reactivities and reveal differences between plants and other species
    • Smagghe BJ, Sarath G, Ross E, Hilbert JL, Hargrove MS. Slow ligand binding kinetics dominate ferrous hexacoordinate hemoglobin reactivities and reveal differences between plants and other species. Biochemistry 2006; 45: 561-570.
    • (2006) Biochemistry , vol.45 , pp. 561-570
    • Smagghe, B.1    Sarath, G.2    Ross, E.3    Hilbert, J.4    Hargrove, M.5
  • 14
    • 10644251786 scopus 로고    scopus 로고
    • The structure of carbonmonoxy neuroglobin reveals a heme-sliding mechanism for control of ligand affinity
    • Vallone B, Nienhaus K, Matthes A, Brunori M, Nienhaus GU. The structure of carbonmonoxy neuroglobin reveals a heme-sliding mechanism for control of ligand affinity. Proc Natl Acad Sci USA 2004; 101: 17351-17356.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 17351-17356
    • Vallone, B.1    Nienhaus, K.2    Matthes, A.3    Brunori, M.4    Nienhaus, G.5
  • 16
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch W. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J Appl Cryst 1993; 26: 795-800.
    • (1993) J Appl Cryst , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 20
    • 79952490740 scopus 로고    scopus 로고
    • The PyMOL molecular graphics system. San Carlos, CA: DeLano Scientific.
    • DeLano WL. The PyMOL molecular graphics system. San Carlos, CA: DeLano Scientific; 2002.
    • (2002)
    • Delano, W.1
  • 21
    • 0028881975 scopus 로고
    • SURFNET: a program for visualizing molecular surfaces, cavities, and intermolecular interactions
    • 307-328.
    • Laskowski RA. SURFNET: a program for visualizing molecular surfaces, cavities, and intermolecular interactions. J Mol Graph 1995; 13: 323-330, 307-328.
    • (1995) J Mol Graph , vol.13 , pp. 323-330
    • Laskowski, R.1
  • 22
    • 0029986887 scopus 로고    scopus 로고
    • Crystal structures of CO-, deoxy- and met-myoglobins at various pH values
    • Yang F, Phillips GN, Jr. Crystal structures of CO-, deoxy- and met-myoglobins at various pH values. J Mol Biol 1996; 256: 762-774.
    • (1996) J Mol Biol , vol.256 , pp. 762-774
    • Yang, F.1    Phillips Jr, G.2
  • 23
    • 0033574735 scopus 로고    scopus 로고
    • A steric mechanism for inhibition of CO binding to heme proteins
    • Kachalova GS, Popov AN, Bartunik HD. A steric mechanism for inhibition of CO binding to heme proteins. Science 1999; 284: 473-476.
    • (1999) Science , vol.284 , pp. 473-476
    • Kachalova, G.1    Popov, A.2    Bartunik, H.3
  • 24
    • 0038853525 scopus 로고    scopus 로고
    • Crystal structures of myoglobin-ligand complexes at near-atomic resolution
    • Vojtechovsky J, Chu K, Berendzen J, Sweet RM, Schlichting I. Crystal structures of myoglobin-ligand complexes at near-atomic resolution. Biophys J 1999; 77: 2153-2174.
    • (1999) Biophys J , vol.77 , pp. 2153-2174
    • Vojtechovsky, J.1    Chu, K.2    Berendzen, J.3    Sweet, R.4    Schlichting, I.5
  • 27
    • 2642521269 scopus 로고    scopus 로고
    • The structure of murine neuroglobin: novel pathways for ligand migration and binding
    • Vallone B, Nienhaus K, Brunori M, Nienhaus GU. The structure of murine neuroglobin: novel pathways for ligand migration and binding. Proteins 2004; 56: 85-92.
    • (2004) Proteins , vol.56 , pp. 85-92
    • Vallone, B.1    Nienhaus, K.2    Brunori, M.3    Nienhaus, G.4
  • 29
    • 34447108659 scopus 로고    scopus 로고
    • Plant hemoglobins: a molecular fossil record for the evolution of oxygen transport
    • Hoy JA, Robinson H, Trent JT, III, Kakar S, Smagghe BJ, Hargrove MS. Plant hemoglobins: a molecular fossil record for the evolution of oxygen transport. J Mol Biol 2007; 371: 168-179.
    • (2007) J Mol Biol , vol.371 , pp. 168-179
    • Hoy, J.1    Robinson, H.2    Trent III, J.3    Kakar, S.4    Smagghe, B.5    Hargrove, M.6
  • 30
    • 3843100441 scopus 로고    scopus 로고
    • Crystallographic analysis of Synechocystis cyanoglobin reveals the structural changes accompanying ligand binding in a hexacoordinate hemoglobin
    • Trent JT, III, Kundu S, Hoy JA, Hargrove MS. Crystallographic analysis of Synechocystis cyanoglobin reveals the structural changes accompanying ligand binding in a hexacoordinate hemoglobin. J Mol Biol 2004; 341: 1097-1108.
    • (2004) J Mol Biol , vol.341 , pp. 1097-1108
    • Trent III, J.1    Kundu, S.2    Hoy, J.3    Hargrove, M.4
  • 31
    • 0028328331 scopus 로고
    • Structural determinants of the stretching frequency of CO bound to myoglobin
    • Li T, Quillin ML, Phillips GN, Jr, Olson JS. Structural determinants of the stretching frequency of CO bound to myoglobin. Biochemistry 1994; 33: 1433-1446.
    • (1994) Biochemistry , vol.33 , pp. 1433-1446
    • Li, T.1    Quillin, M.2    Phillips Jr, G.3    Olson, J.4
  • 32
    • 0018589604 scopus 로고
    • Structure of carboxymyoglobin in crystals and in solution
    • Makinen MW, Houtchens RA, Caughey WS. Structure of carboxymyoglobin in crystals and in solution. Proc Natl Acad Sci USA 1979; 76: 6042-6046.
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 6042-6046
    • Makinen, M.1    Houtchens, R.2    Caughey, W.3
  • 33
    • 0001341970 scopus 로고
    • A molecular model for the major conformational substates in heme proteins
    • Oldfield E, Guo K, Augspurger JD, Dykstra CE. A molecular model for the major conformational substates in heme proteins. J Am Chem Soc 1991; 113: 7537-7541.
    • (1991) J Am Chem Soc , vol.113 , pp. 7537-7541
    • Oldfield, E.1    Guo, K.2    Augspurger, J.3    Dykstra, C.4
  • 34
    • 0024601864 scopus 로고
    • Resonance Raman evidence that distal histidine protonation removes the steric hindrance to upright binding of carbon monoxide by myoglobin
    • Ramsden J, Spiro TG. Resonance Raman evidence that distal histidine protonation removes the steric hindrance to upright binding of carbon monoxide by myoglobin. Biochemistry 1989; 28: 3125-3128.
    • (1989) Biochemistry , vol.28 , pp. 3125-3128
    • Ramsden, J.1    Spiro, T.2
  • 35
    • 0020484765 scopus 로고
    • Resonance Raman investigation of carbon monoxide bonding in (carbon monoxy)hemoglobin and -myoglobin: detection of Fe-CO stretching and Fe-C-O bending vibrations and influence of the quaternary structure change
    • Tsubaki M, Srivastava RB, Yu NT. Resonance Raman investigation of carbon monoxide bonding in (carbon monoxy)hemoglobin and -myoglobin: detection of Fe-CO stretching and Fe-C-O bending vibrations and influence of the quaternary structure change. Biochemistry 1982; 21: 1132-1140.
    • (1982) Biochemistry , vol.21 , pp. 1132-1140
    • Tsubaki, M.1    Srivastava, R.2    Yu, N.3
  • 36
    • 0018332324 scopus 로고
    • 2 complexes of myoglobin and hemoglobin
    • 2 complexes of myoglobin and hemoglobin. Biochemistry 1979; 18: 1309-1321.
    • (1979) Biochemistry , vol.18 , pp. 1309-1321
    • Fuchsman, W.1    Appleby, C.2
  • 37
    • 0024334934 scopus 로고
    • Resonance raman investigations of site-directed mutants of myoglobin: effects of distal histidine replacement
    • Morikis D, Champion PM, Springer BA, Sligar SG. Resonance raman investigations of site-directed mutants of myoglobin: effects of distal histidine replacement. Biochemistry 1989; 28: 4791-4800.
    • (1989) Biochemistry , vol.28 , pp. 4791-4800
    • Morikis, D.1    Champion, P.2    Springer, B.3    Sligar, S.4
  • 39
    • 0003506579 scopus 로고
    • Hemoglobin and myoglobin in their reactions whith ligands
    • Amsterdam: North-Holland Publishing Company.
    • Antonini E, Brunori M. Hemoglobin and myoglobin in their reactions whith ligands. Amsterdam: North-Holland Publishing Company; 1971. 436 p.
    • (1971) , pp. 436
    • Antonini, E.1    Brunori, M.2
  • 40
    • 0035965286 scopus 로고    scopus 로고
    • The heme environment of mouse neuroglobin. Evidence for the presence of two conformations of the heme pocket
    • Couture M, Burmester T, Hankeln T, Rousseau DL. The heme environment of mouse neuroglobin. Evidence for the presence of two conformations of the heme pocket. J Biol Chem 2001; 276: 36377-36382.
    • (2001) J Biol Chem , vol.276 , pp. 36377-36382
    • Couture, M.1    Burmester, T.2    Hankeln, T.3    Rousseau, D.4
  • 41
    • 4143067901 scopus 로고    scopus 로고
    • Neuroglobin and other hexacoordinated hemoglobins show a weak temperature dependence of oxygen binding
    • Uzan J, Dewilde S, Burmester T, Hankeln T, Moens L, Hamdane D, Marden MC, Kiger L. Neuroglobin and other hexacoordinated hemoglobins show a weak temperature dependence of oxygen binding. Biophys J 2004; 87: 1196-1204.
    • (2004) Biophys J , vol.87 , pp. 1196-1204
    • Uzan, J.1    Dewilde, S.2    Burmester, T.3    Hankeln, T.4    Moens, L.5    Hamdane, D.6    Marden, M.7    Kiger, L.8
  • 43
    • 0141704224 scopus 로고    scopus 로고
    • Oxidized human neuroglobin acts as a heterotrimeric Galpha protein guanine nucleotide dissociation inhibitor
    • Wakasugi K, Nakano T, Morishima I. Oxidized human neuroglobin acts as a heterotrimeric Galpha protein guanine nucleotide dissociation inhibitor. J Biol Chem 2003; 278: 36505-36512.
    • (2003) J Biol Chem , vol.278 , pp. 36505-36512
    • Wakasugi, K.1    Nakano, T.2    Morishima, I.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.