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Volumn 436, Issue , 2008, Pages 303-315

Mapping Heme-Ligand Tunnels in Group I Truncated(2/2) Hemoglobins

Author keywords

[No Author keywords available]

Indexed keywords

CYANIDE; HEME; HEMOGLOBIN; HEMOPROTEIN; LIGAND; XENON; BUTYL ISOCYANIDE; NITRILE; TRUNCATED HEMOGLOBIN;

EID: 42949176730     PISSN: 00766879     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0076-6879(08)36017-0     Document Type: Chapter
Times cited : (20)

References (43)
  • 2
    • 23844469133 scopus 로고    scopus 로고
    • A novel thermostable hemoglobin from the actinobacterium Thermobifida fusca
    • Bonamore A., Ilari A., Giangiacomo L., Bellelli A., Morea V., and Boffi A. A novel thermostable hemoglobin from the actinobacterium Thermobifida fusca. FEBS J. 272 (2005) 4189-4201
    • (2005) FEBS J. , vol.272 , pp. 4189-4201
    • Bonamore, A.1    Ilari, A.2    Giangiacomo, L.3    Bellelli, A.4    Morea, V.5    Boffi, A.6
  • 3
    • 0034867130 scopus 로고    scopus 로고
    • Cavities and packing defects in the structural dynamics of myoglobin
    • Brunori M., and Gibson Q.H. Cavities and packing defects in the structural dynamics of myoglobin. EMBO Rep. 2 (2001) 674-679
    • (2001) EMBO Rep. , vol.2 , pp. 674-679
    • Brunori, M.1    Gibson, Q.H.2
  • 5
    • 0037073478 scopus 로고    scopus 로고
    • The solution structure of the recombinant hemoglobin from the cyanobacterium Synechocystis sp. PCC 6803 in its hemichrome state
    • Falzone C.J., Vu B.C., Scott N.L., and Lecomte J.T. The solution structure of the recombinant hemoglobin from the cyanobacterium Synechocystis sp. PCC 6803 in its hemichrome state. J. Mol. Biol. 324 (2002) 1015-1029
    • (2002) J. Mol. Biol. , vol.324 , pp. 1015-1029
    • Falzone, C.J.1    Vu, B.C.2    Scott, N.L.3    Lecomte, J.T.4
  • 6
    • 15744375834 scopus 로고    scopus 로고
    • The truncated oxygen-avid hemoglobin from Bacillus subtilis: X-ray structure and ligand binding properties
    • Giangiacomo L., Ilari A., Boffi A., Morea V., and Chiancone E. The truncated oxygen-avid hemoglobin from Bacillus subtilis: X-ray structure and ligand binding properties. J. Biol. Chem. 280 (2005) 9192-9202
    • (2005) J. Biol. Chem. , vol.280 , pp. 9192-9202
    • Giangiacomo, L.1    Ilari, A.2    Boffi, A.3    Morea, V.4    Chiancone, E.5
  • 7
    • 2142742831 scopus 로고    scopus 로고
    • Overview and new developments in softer X-ray (2 Å < lambda < 5 Å) protein crystallography
    • Helliwell J.R. Overview and new developments in softer X-ray (2 Å < lambda < 5 Å) protein crystallography. J. Synchrotron Radiat. 11 (2004) 1-3
    • (2004) J. Synchrotron Radiat. , vol.11 , pp. 1-3
    • Helliwell, J.R.1
  • 8
    • 0027459747 scopus 로고
    • Structural alignment of globins, phycocyanins and colicin A
    • Holm L., and Sander C. Structural alignment of globins, phycocyanins and colicin A. FEBS Lett. 315 (1993) 301-306
    • (1993) FEBS Lett. , vol.315 , pp. 301-306
    • Holm, L.1    Sander, C.2
  • 9
    • 1942533441 scopus 로고    scopus 로고
    • The crystal structure of Synechocystis hemoglobin with a covalent heme linkage
    • Hoy J.A., Kundu S., Trent III J.T., Ramaswamy S., and Hargrove M.S. The crystal structure of Synechocystis hemoglobin with a covalent heme linkage. J. Biol. Chem. 279 (2004) 16535-16542
    • (2004) J. Biol. Chem. , vol.279 , pp. 16535-16542
    • Hoy, J.A.1    Kundu, S.2    Trent III, J.T.3    Ramaswamy, S.4    Hargrove, M.S.5
  • 10
    • 0034919604 scopus 로고    scopus 로고
    • Channeling of substrates and intermediates in enzyme-catalyzed reactions
    • Huang X., Holden H.M., and Raushel F.M. Channeling of substrates and intermediates in enzyme-catalyzed reactions. Annu. Rev. Biochem. 70 (2001) 149-180
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 149-180
    • Huang, X.1    Holden, H.M.2    Raushel, F.M.3
  • 11
    • 33845699407 scopus 로고    scopus 로고
    • Crystal structure and ligand binding properties of the truncated hemoglobin from Geobacillus stearothermophilus
    • Ilari A., Kjelgaard P., von Wachenfeldt C., Catacchio B., Chiancone E., and Boffi A. Crystal structure and ligand binding properties of the truncated hemoglobin from Geobacillus stearothermophilus. Arch. Biochem. Biophys. 457 (2007) 85-94
    • (2007) Arch. Biochem. Biophys. , vol.457 , pp. 85-94
    • Ilari, A.1    Kjelgaard, P.2    von Wachenfeldt, C.3    Catacchio, B.4    Chiancone, E.5    Boffi, A.6
  • 12
    • 33745664787 scopus 로고    scopus 로고
    • Solution of protein crystallographic structures by high-pressure cryocooling and noble-gas phasing
    • Kim C.U., Hao Q., and Gruner S.M. Solution of protein crystallographic structures by high-pressure cryocooling and noble-gas phasing. Acta Crystallogr. D 62 (2006) 687-694
    • (2006) Acta Crystallogr. D , vol.62 , pp. 687-694
    • Kim, C.U.1    Hao, Q.2    Gruner, S.M.3
  • 13
    • 0027995683 scopus 로고
    • Detection, delineation, measurement and display of cavities in macromolecular structures
    • Kleywegt G.J., and Jones T.A. Detection, delineation, measurement and display of cavities in macromolecular structures. Acta Crystallogr. D 50 (1994) 178-185
    • (1994) Acta Crystallogr. D , vol.50 , pp. 178-185
    • Kleywegt, G.J.1    Jones, T.A.2
  • 14
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P.J. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24 (1991) 946-950
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 15
    • 0028881975 scopus 로고
    • SURFNET: A program for visualizing molecular surfaces, cavities and intermolecular interactions
    • Laskowski R.A. SURFNET: A program for visualizing molecular surfaces, cavities and intermolecular interactions. J. Mol. Graph. 13 (1995) 323-330
    • (1995) J. Mol. Graph. , vol.13 , pp. 323-330
    • Laskowski, R.A.1
  • 16
    • 0035814893 scopus 로고    scopus 로고
    • Structural characterization of n-butyl-isocyanide complexes of cytochrome P450nor and P450cam
    • Lee D.S., Park S.Y., Yamane K., Obayashi E., Hori H., and Shiro Y. Structural characterization of n-butyl-isocyanide complexes of cytochrome P450nor and P450cam. Biochemistry 40 (2001) 2669-2677
    • (2001) Biochemistry , vol.40 , pp. 2669-2677
    • Lee, D.S.1    Park, S.Y.2    Yamane, K.3    Obayashi, E.4    Hori, H.5    Shiro, Y.6
  • 20
    • 0038624089 scopus 로고    scopus 로고
    • A TyrCD1/TrpG8 hydrogen bond network and a TyrB10-TyrCD1 covalent link shape the heme distal site of Mycobacterium tuberculosis hemoglobin O
    • Milani M., Savard P.Y., Ouellet H., Ascenzi P., Guertin M., and Bolognesi M. A TyrCD1/TrpG8 hydrogen bond network and a TyrB10-TyrCD1 covalent link shape the heme distal site of Mycobacterium tuberculosis hemoglobin O. Proc. Natl. Acad. Sci. USA 100 (2003) 5766-5771
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 5766-5771
    • Milani, M.1    Savard, P.Y.2    Ouellet, H.3    Ascenzi, P.4    Guertin, M.5    Bolognesi, M.6
  • 22
    • 32944456529 scopus 로고    scopus 로고
    • On the routine use of soft X-rays in macromolecular crystallography. Part III. The optimal data-collection wavelength
    • Mueller-Dieckmann C., Panjikar S., Tucker P.A., and Weiss M.S. On the routine use of soft X-rays in macromolecular crystallography. Part III. The optimal data-collection wavelength. Acta Crystallogr. D 61 (2005) 1263-1272
    • (2005) Acta Crystallogr. D , vol.61 , pp. 1263-1272
    • Mueller-Dieckmann, C.1    Panjikar, S.2    Tucker, P.A.3    Weiss, M.S.4
  • 24
    • 34447530237 scopus 로고    scopus 로고
    • Protein fold and structure in the truncated (2/2) globin family
    • Nardini M., Pesce A., Milani M., and Bolognesi M. Protein fold and structure in the truncated (2/2) globin family. Gene 398 (2007) 2-11
    • (2007) Gene , vol.398 , pp. 2-11
    • Nardini, M.1    Pesce, A.2    Milani, M.3    Bolognesi, M.4
  • 26
    • 0018654083 scopus 로고
    • Regulation of oxygen affinity of hemoglobin: Influence of structure of the globin on the heme iron
    • Perutz M.F. Regulation of oxygen affinity of hemoglobin: Influence of structure of the globin on the heme iron. Annu. Rev. Biochem. 48 (1979) 327-386
    • (1979) Annu. Rev. Biochem. , vol.48 , pp. 327-386
    • Perutz, M.F.1
  • 27
    • 0034213366 scopus 로고    scopus 로고
    • A novel two-over-two α-helical sandwich fold is characteristic of the truncated hemoglobin family
    • Pesce A., Couture M., Dewilde S., Guertin M., Yamauchi K., Ascenzi P., Moens L., and Bolognesi M. A novel two-over-two α-helical sandwich fold is characteristic of the truncated hemoglobin family. EMBO J. 19 (2000) 2424-2434
    • (2000) EMBO J. , vol.19 , pp. 2424-2434
    • Pesce, A.1    Couture, M.2    Dewilde, S.3    Guertin, M.4    Yamauchi, K.5    Ascenzi, P.6    Moens, L.7    Bolognesi, M.8
  • 28
    • 0242663437 scopus 로고    scopus 로고
    • Selling candles in a post-Edison world: Phasing with noble gases bound engineered sites
    • Quillin M.L., and Matthews B.W. Selling candles in a post-Edison world: Phasing with noble gases bound engineered sites. Acta Crystallogr. D 59 (2003) 1930-1934
    • (2003) Acta Crystallogr. D , vol.59 , pp. 1930-1934
    • Quillin, M.L.1    Matthews, B.W.2
  • 30
    • 0019223598 scopus 로고
    • Equilibrium binding of alkyl isocyanides to human hemoglobin
    • Reisberg P.I., and Olson J.S. Equilibrium binding of alkyl isocyanides to human hemoglobin. J. Biol. Chem. 255 (1980) 4144-4150
    • (1980) J. Biol. Chem. , vol.255 , pp. 4144-4150
    • Reisberg, P.I.1    Olson, J.S.2
  • 31
    • 0019154562 scopus 로고
    • Rates of isonitrile binding to the isolated α and β subunits of human hemoglobin
    • Reisberg P.I., and Olson J.S. Rates of isonitrile binding to the isolated α and β subunits of human hemoglobin. J. Biol. Chem. 255 (1980) 4151-4158
    • (1980) J. Biol. Chem. , vol.255 , pp. 4151-4158
    • Reisberg, P.I.1    Olson, J.S.2
  • 33
    • 0346753473 scopus 로고    scopus 로고
    • Use of noble gases xenon and krypton as heavy atoms in protein structure determination
    • Schiltz M., Fourme R., and Prange T. Use of noble gases xenon and krypton as heavy atoms in protein structure determination. Methods Enzymol. 374 (2003) 83-119
    • (2003) Methods Enzymol. , vol.374 , pp. 83-119
    • Schiltz, M.1    Fourme, R.2    Prange, T.3
  • 36
    • 0035923445 scopus 로고    scopus 로고
    • Protein conformational relaxation and ligand migration in myoglobin: A nanosecond to millisecond molecular movie from time-resolved Laue X-ray diffraction
    • Srajer V., Ren Z., Teng T.Y., Schmidt M., Ursby T., Bourgeois D., Pradervand C., Schildkamp W., Wulff M., and Moffat K. Protein conformational relaxation and ligand migration in myoglobin: A nanosecond to millisecond molecular movie from time-resolved Laue X-ray diffraction. Biochemistry 40 (2001) 13802-13815
    • (2001) Biochemistry , vol.40 , pp. 13802-13815
    • Srajer, V.1    Ren, Z.2    Teng, T.Y.3    Schmidt, M.4    Ursby, T.5    Bourgeois, D.6    Pradervand, C.7    Schildkamp, W.8    Wulff, M.9    Moffat, K.10
  • 37
    • 0021766921 scopus 로고
    • Cavities in proteins: Structure of a metmyoglobin-xenon complex solved to 1.9 Å
    • Tilton Jr. R.F., Kuntz Jr. I.D., and Petsko G.A. Cavities in proteins: Structure of a metmyoglobin-xenon complex solved to 1.9 Å. Biochemistry 23 (1984) 2849-2857
    • (1984) Biochemistry , vol.23 , pp. 2849-2857
    • Tilton Jr., R.F.1    Kuntz Jr., I.D.2    Petsko, G.A.3
  • 38
    • 3843100441 scopus 로고    scopus 로고
    • Crystallographic analysis of Synechocystis cyanoglobin reveals the structural changes accompanying ligand binding in a hexacoordinate hemoglobin
    • Trent III J.T., Kundu S., Hoy J.A., and Hargrove M.S. Crystallographic analysis of Synechocystis cyanoglobin reveals the structural changes accompanying ligand binding in a hexacoordinate hemoglobin. J. Mol. Biol. 341 (2004) 1097-1108
    • (2004) J. Mol. Biol. , vol.341 , pp. 1097-1108
    • Trent III, J.T.1    Kundu, S.2    Hoy, J.A.3    Hargrove, M.S.4
  • 40
    • 33646341657 scopus 로고    scopus 로고
    • A phylogenetic and structural analysis of truncated hemoglobins
    • Vuletich D.A., and Lecomte J.T. A phylogenetic and structural analysis of truncated hemoglobins. J. Mol. Evol. 62 (2006) 196-210
    • (2006) J. Mol. Evol. , vol.62 , pp. 196-210
    • Vuletich, D.A.1    Lecomte, J.T.2
  • 41
    • 33748598228 scopus 로고    scopus 로고
    • Tunneling of intermediates in enzyme-catalyzed reactions
    • Weeks A., Lund L., and Raushel F.M. Tunneling of intermediates in enzyme-catalyzed reactions. Curr. Opin. Struct. Biol. 10 (2006) 465-472
    • (2006) Curr. Opin. Struct. Biol. , vol.10 , pp. 465-472
    • Weeks, A.1    Lund, L.2    Raushel, F.M.3
  • 43
    • 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


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