메뉴 건너뛰기




Volumn 8, Issue 1, 2013, Pages

CO Rebinding Kinetics and Molecular Dynamics Simulations Highlight Dynamic Regulation of Internal Cavities in Human Cytoglobin

Author keywords

[No Author keywords available]

Indexed keywords

CARBON MONOXIDE; CYTOGLOBIN; HEME; HISTIDINE; SILICA GEL;

EID: 84871892340     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0049770     Document Type: Article
Times cited : (29)

References (61)
  • 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, et al. (2001) Characterization of a stellate cell activation-associated protein (STAP) with peroxidase activity found in rat hepatic stellate cells. J Biol Chem 276: 25318-25323.
    • (2001) J Biol Chem , vol.276 , pp. 25318-25323
    • Kawada, N.1    Kristensen, D.B.2    Asahina, K.3    Nakatani, K.4    Minamiyama, Y.5
  • 3
    • 0036219963 scopus 로고    scopus 로고
    • Cytoglobin: A Novel Globin Type Ubiquitously Expressed in Vertebrate Tissues
    • Burmester T, Ebner B, Weich B, Hankeln T, (2002) Cytoglobin: A Novel Globin Type Ubiquitously Expressed in Vertebrate Tissues. Mol Biol Evol 19: 416-421.
    • (2002) Mol Biol Evol , vol.19 , pp. 416-421
    • Burmester, T.1    Ebner, B.2    Weich, B.3    Hankeln, T.4
  • 4
    • 10444267310 scopus 로고    scopus 로고
    • Neuroglobin and cytoglobin in search of their role in the vertebrate globin family
    • Hankeln T, Ebner B, Fuchs C, Gerlach F, Haberkamp M, et al. (2005) Neuroglobin and cytoglobin in search of their role in the vertebrate globin family. J Inorg Biochem 99: 110-119.
    • (2005) J Inorg Biochem , vol.99 , pp. 110-119
    • Hankeln, T.1    Ebner, B.2    Fuchs, C.3    Gerlach, F.4    Haberkamp, M.5
  • 5
    • 0037205447 scopus 로고    scopus 로고
    • A Ubiquitously Expressed Human Hexacoordinate Hemoglobin
    • Trent JI, Hargrove MS, (2002) A Ubiquitously Expressed Human Hexacoordinate Hemoglobin. J Biol Chem 277: 19538-19545.
    • (2002) J Biol Chem , vol.277 , pp. 19538-19545
    • Trent, J.I.1    Hargrove, M.S.2
  • 6
    • 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, et al. (2003) Characterization of the Heme Environmental Structure of Cytoglobin, a Fourth Globin in Humans. Biochemistry 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
  • 7
    • 0037018935 scopus 로고    scopus 로고
    • Truncated Hemoglobin from the Cyanobacterium Synechococcus sp. PCC 7002: Evidence for Hexacoordination and Covalent Adduct Formation in the Ferric Recombinant Protein
    • Scott NL, Falzone CJ, Vuletich DA, Zhao J, Bryant DA, et al. (2002) Truncated Hemoglobin from the Cyanobacterium Synechococcus sp. PCC 7002: Evidence for Hexacoordination and Covalent Adduct Formation in the Ferric Recombinant Protein. Biochemistry 41: 6902-6910.
    • (2002) Biochemistry , vol.41 , pp. 6902-6910
    • Scott, N.L.1    Falzone, C.J.2    Vuletich, D.A.3    Zhao, J.4    Bryant, D.A.5
  • 8
    • 60549094197 scopus 로고    scopus 로고
    • Nonsymbiotic hemoglobins and stress tolerance in plants
    • Dordas C, (2009) Nonsymbiotic hemoglobins and stress tolerance in plants. Plant Science 176: 433-440.
    • (2009) Plant Science , vol.176 , pp. 433-440
    • Dordas, C.1
  • 9
    • 0012231458 scopus 로고    scopus 로고
    • Neuroglobin and cytoglobin Fresh blood for the vertebrate globin family
    • Pesce A, Bolognesi M, Bocedi A, Ascenzi P, Dewilde S, et al. (2002) Neuroglobin and cytoglobin Fresh blood for the vertebrate globin family. EMBO Reports 3: 1146-1151.
    • (2002) EMBO Reports , vol.3 , pp. 1146-1151
    • Pesce, A.1    Bolognesi, M.2    Bocedi, A.3    Ascenzi, P.4    Dewilde, S.5
  • 10
    • 71749112436 scopus 로고    scopus 로고
    • Correlations between oxygen affinity and sequence classifications of plant hemoglobins
    • Smagghe BJ, Hoy JA, Percifield R, Kundu S, Hargrove MS, et al. (2009) Correlations between oxygen affinity and sequence classifications of plant hemoglobins. Biopolymers 91: 1083-1096.
    • (2009) Biopolymers , vol.91 , pp. 1083-1096
    • Smagghe, B.J.1    Hoy, J.A.2    Percifield, R.3    Kundu, S.4    Hargrove, M.S.5
  • 11
    • 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, (2004) The structure of carbonmonoxy neuroglobin reveals a heme-sliding mechanism for control of ligand affinity. Proc Natl Acad Sci USA 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.U.5
  • 12
    • 34447108659 scopus 로고    scopus 로고
    • Plant hemoglobins: A molecular fossil record for the evolution of oxygen transport
    • Hoy JA, Robinson H, Trent JT, Kakar S, Smagge BJ, et al. (2007) Plant hemoglobins: A molecular fossil record for the evolution of oxygen transport. J Mol Biol 371: 168-179.
    • (2007) J Mol Biol , vol.371 , pp. 168-179
    • Hoy, J.A.1    Robinson, H.2    Trent, J.T.3    Kakar, S.4    Smagge, B.J.5
  • 13
    • 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, (2001) Neuroglobin is up-regulated by and protects neurons from hypoxic-ischemic injury. Proc Natl Acad Sci USA 98: 15306-15311.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 15306-15311
    • Sun, Y.1    Jin, K.2    Mao, X.O.3    Zhu, Y.4    Greenberg, D.A.5
  • 15
    • 84862845350 scopus 로고    scopus 로고
    • Characterization of the Function of Cytoglobin as an Oxygen-Dependent Regulator of Nitric Oxide Concentration
    • Liu X, Follmer D, Zweier JR, Huang X, Hemann C, et al. (2012) Characterization of the Function of Cytoglobin as an Oxygen-Dependent Regulator of Nitric Oxide Concentration. Biochemistry 51: 5072-5082.
    • (2012) Biochemistry , vol.51 , pp. 5072-5082
    • Liu, X.1    Follmer, D.2    Zweier, J.R.3    Huang, X.4    Hemann, C.5
  • 16
    • 1642377942 scopus 로고    scopus 로고
    • Mapping protein matrix cavities in human cytoglobin through Xe atom binding
    • deSanctis D, Dewilde S, Pesce A, Moens L, Ascenzi P, et al. (2004) Mapping protein matrix cavities in human cytoglobin through Xe atom binding. Bioch Bioph Res Com 316: 1217-1221.
    • (2004) Bioch Bioph Res Com , vol.316 , pp. 1217-1221
    • deSanctis, D.1    Dewilde, S.2    Pesce, A.3    Moens, L.4    Ascenzi, P.5
  • 17
    • 34447518537 scopus 로고    scopus 로고
    • Anoxia or oxygen and glucose deprivation in SH-SY5Y cells: A step closer to the unraveling of neuroglobin and cytoglobin functions
    • Fordel E, Thijs L, Martinet W, Schrijvers D, Moens L, et al. (2007) Anoxia or oxygen and glucose deprivation in SH-SY5Y cells: A step closer to the unraveling of neuroglobin and cytoglobin functions. Gene 398: 114-122.
    • (2007) Gene , vol.398 , pp. 114-122
    • Fordel, E.1    Thijs, L.2    Martinet, W.3    Schrijvers, D.4    Moens, L.5
  • 18
    • 10744220623 scopus 로고    scopus 로고
    • Cytoglobin is a respiratory protein in connective tissue and neurons, which is up-regulated by hypoxia
    • Schmidt M, Gerlach F, Avivi A, Laufs T, Wystub S, et al. (2004) Cytoglobin is a respiratory protein in connective tissue and neurons, which is up-regulated by hypoxia. J Biol Chem 279: 8063-8069.
    • (2004) J Biol Chem , vol.279 , pp. 8063-8069
    • Schmidt, M.1    Gerlach, F.2    Avivi, A.3    Laufs, T.4    Wystub, S.5
  • 19
    • 7244245630 scopus 로고    scopus 로고
    • Allosteric Regulation and Temperature Dependence of Oxygen Binding in Human Neuroglobin and Cytoglobin: MOLECULAR MECHANISMS AND PHYSIOLOGICAL SIGNIFICANCE
    • Fago A, Hundahl C, Dewilde S, Gilany K, Moens L, et al. (2004) Allosteric Regulation and Temperature Dependence of Oxygen Binding in Human Neuroglobin and Cytoglobin: MOLECULAR MECHANISMS AND PHYSIOLOGICAL SIGNIFICANCE. J Biol Chem 279: 44417-44426.
    • (2004) J Biol Chem , vol.279 , pp. 44417-44426
    • Fago, A.1    Hundahl, C.2    Dewilde, S.3    Gilany, K.4    Moens, L.5
  • 20
    • 54749135818 scopus 로고    scopus 로고
    • Cytoglobin, the Newest Member of the Globin Family, Functions as a Tumor Suppressor Gene
    • Shivapurkar N, Stastny V, Okumura N, Girard L, Xie Y, et al. (2008) Cytoglobin, the Newest Member of the Globin Family, Functions as a Tumor Suppressor Gene. Cancer Research 78: 7448-7456.
    • (2008) Cancer Research , vol.78 , pp. 7448-7456
    • Shivapurkar, N.1    Stastny, V.2    Okumura, N.3    Girard, L.4    Xie, Y.5
  • 22
    • 36048936331 scopus 로고    scopus 로고
    • Ligand migration in non symbiotic hemoglobin AHb1 from Arabidopsis thaliana
    • Abbruzzetti S, Grandi E, Bruno S, Faggiano S, Spyrakis F, et al. (2007) Ligand migration in non symbiotic hemoglobin AHb1 from Arabidopsis thaliana. J Phys Chem B 111: 12582-12590.
    • (2007) J Phys Chem B , vol.111 , pp. 12582-12590
    • Abbruzzetti, S.1    Grandi, E.2    Bruno, S.3    Faggiano, S.4    Spyrakis, F.5
  • 24
    • 27544515467 scopus 로고    scopus 로고
    • Determination of microscopic rate constants for CO binding and migration in myoglobin encapsulated in silica gels
    • Sottini S, Abbruzzetti S, Viappiani C, Ronda L, Mozzarelli A, (2005) Determination of microscopic rate constants for CO binding and migration in myoglobin encapsulated in silica gels. J Phys Chem B 109: 19523-19528.
    • (2005) J Phys Chem B , vol.109 , pp. 19523-19528
    • Sottini, S.1    Abbruzzetti, S.2    Viappiani, C.3    Ronda, L.4    Mozzarelli, A.5
  • 25
    • 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, Abbruzzetti S, Viappiani C, Bettati S, Ronda L, et al. (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
  • 26
    • 5144223974 scopus 로고    scopus 로고
    • New insights into allosteric mechanisms from trapping unstable protein conformations in silica gels
    • Viappiani C, Bettati S, Bruno S, Ronda L, Abbruzzetti S, et al. (2004) New insights into allosteric mechanisms from trapping unstable protein conformations in silica gels. Proc Natl Acad Sci USA 101: 14414-14419.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 14414-14419
    • Viappiani, C.1    Bettati, S.2    Bruno, S.3    Ronda, L.4    Abbruzzetti, S.5
  • 27
    • 42949103602 scopus 로고    scopus 로고
    • Expression, Purification, and Crystallization of Neuro- and Cytoglobin Methods in Enzymology - Globins and other NO-reactive Proteins in Microbes,
    • Dewilde S, Mees K, Kiger L, Lechauve C, Marden MC, et al. (2008) Expression, Purification, and Crystallization of Neuro- and Cytoglobin Methods in Enzymology- Globins and other NO-reactive Proteins in Microbes,. Plants and Invertebrates 436: 341-357.
    • (2008) Plants and Invertebrates , vol.436 , pp. 341-357
    • Dewilde, S.1    Mees, K.2    Kiger, L.3    Lechauve, C.4    Marden, M.C.5
  • 28
    • 0031463937 scopus 로고    scopus 로고
    • T state hemoglobin binds oxygen noncooperatively with allosteric effects of protons, inositol hexaphosphate and chloride
    • Bettati S, Mozzarelli A, (1997) T state hemoglobin binds oxygen noncooperatively with allosteric effects of protons, inositol hexaphosphate and chloride. J Biol Chem 272: 32050-32055.
    • (1997) J Biol Chem , vol.272 , pp. 32050-32055
    • Bettati, S.1    Mozzarelli, A.2
  • 29
    • 0036212631 scopus 로고    scopus 로고
    • Analysis of Kinetics Using a Hybrid Maximum-Entropy/Nonlinear-Least-Squares Method: Application to Protein Folding
    • Steinbach PJ, Ionescu R, Matthews CR, (2002) Analysis of Kinetics Using a Hybrid Maximum-Entropy/Nonlinear-Least-Squares Method: Application to Protein Folding. Biophys J 82: 2244-2255.
    • (2002) Biophys J , vol.82 , pp. 2244-2255
    • Steinbach, P.J.1    Ionescu, R.2    Matthews, C.R.3
  • 31
    • 33748518255 scopus 로고    scopus 로고
    • Comparison of multiple Amber force fields and development of improved protein backbone parameters
    • Hornak V, Abel R, Okur A, Strockbine B, Roitberg A, et al. (2006) Comparison of multiple Amber force fields and development of improved protein backbone parameters. Proteins 65: 712-725.
    • (2006) Proteins , vol.65 , pp. 712-725
    • Hornak, V.1    Abel, R.2    Okur, A.3    Strockbine, B.4    Roitberg, A.5
  • 33
    • 1042286374 scopus 로고    scopus 로고
    • Crystal Structure of Cytoglobin: The Fourth Globin Type Discovered in Man Displays Heme Hexa-coordination
    • deSanctis D, Dewilde S, Pesce A, Moens L, Ascenzi P, et al. (2004) Crystal Structure of Cytoglobin: The Fourth Globin Type Discovered in Man Displays Heme Hexa-coordination. J Mol Biol 336: 917-927.
    • (2004) J Mol Biol , vol.336 , pp. 917-927
    • deSanctis, D.1    Dewilde, S.2    Pesce, A.3    Moens, L.4    Ascenzi, P.5
  • 34
    • 79952487366 scopus 로고    scopus 로고
    • Crystal structure of the carbon monoxide complex of human cytoglobin
    • Makino M, Sawai H, Shiro Y, Sugimoto H, (2011) Crystal structure of the carbon monoxide complex of human cytoglobin. Proteins 79: 1143-1153.
    • (2011) Proteins , vol.79 , pp. 1143-1153
    • Makino, M.1    Sawai, H.2    Shiro, Y.3    Sugimoto, H.4
  • 36
    • 0000577041 scopus 로고
    • Large-amplitude nonlinear motions in proteins
    • García A, (1992) Large-amplitude nonlinear motions in proteins. Phys Rev Lett 68: 2696-2699.
    • (1992) Phys Rev Lett , vol.68 , pp. 2696-2699
    • García, A.1
  • 38
    • 82255164267 scopus 로고    scopus 로고
    • MDpocket: open-source cavity detection and characterization on molecular dynamics trajectories
    • Schmidtke P, Bidon-Chanal A, Luque FJ, Barril X, (2011) MDpocket: open-source cavity detection and characterization on molecular dynamics trajectories. Bioinformatics 27: 3276-3285.
    • (2011) Bioinformatics , vol.27 , pp. 3276-3285
    • Schmidtke, P.1    Bidon-Chanal, A.2    Luque, F.J.3    Barril, X.4
  • 39
    • 33748460871 scopus 로고    scopus 로고
    • Imaging the migration pathways for O2, CO, NO, and Xe inside myoglobin
    • Cohen J, Arkhipov A, Braun R, Schulten K, (2006) Imaging the migration pathways for O2, CO, NO, and Xe inside myoglobin. Biophys J 91: 1844-1857.
    • (2006) Biophys J , vol.91 , pp. 1844-1857
    • Cohen, J.1    Arkhipov, A.2    Braun, R.3    Schulten, K.4
  • 40
    • 9144247276 scopus 로고    scopus 로고
    • The redox state of the cell regulates the ligand binding affinity of human neuroglobin and cytoglobin
    • Hamdane D, Kiger L, Dewilde S, Green BN, Pesce A, et al. (2003) The redox state of the cell regulates the ligand binding affinity of human neuroglobin and cytoglobin. J Biol Chem 278: 51713-51721.
    • (2003) J Biol Chem , vol.278 , pp. 51713-51721
    • Hamdane, D.1    Kiger, L.2    Dewilde, S.3    Green, B.N.4    Pesce, A.5
  • 41
    • 0001485759 scopus 로고    scopus 로고
    • Functional Characterization of Heme Proteins Encapsulated in Wet Nanoporous Silica Gels
    • Abbruzzetti S, Viappiani C, Bruno S, Bettati S, Bonaccio M, et al. (2001) Functional Characterization of Heme Proteins Encapsulated in Wet Nanoporous Silica Gels. J Nanosci Nanotech 1: 407-415.
    • (2001) J Nanosci Nanotech , vol.1 , pp. 407-415
    • Abbruzzetti, S.1    Viappiani, C.2    Bruno, S.3    Bettati, S.4    Bonaccio, M.5
  • 42
    • 0029163340 scopus 로고
    • Fixation of the Quaternary Structures of Human Adult Haemoglobin by Encapsulation in Transparent Porous Silica Gels
    • Shibayama N, Saigo S, (1995) Fixation of the Quaternary Structures of Human Adult Haemoglobin by Encapsulation in Transparent Porous Silica Gels. J Mol Biol 251: 203-209.
    • (1995) J Mol Biol , vol.251 , pp. 203-209
    • Shibayama, N.1    Saigo, S.2
  • 43
    • 0034769437 scopus 로고    scopus 로고
    • High and low oxygen affinity conformations of T state hemoglobin
    • Bruno S, Bonaccio M, Bettati S, Rivetti C, Viappiani C, et al. (2001) High and low oxygen affinity conformations of T state hemoglobin. Protein Sci 10: 2401-2407.
    • (2001) Protein Sci , vol.10 , pp. 2401-2407
    • Bruno, S.1    Bonaccio, M.2    Bettati, S.3    Rivetti, C.4    Viappiani, C.5
  • 45
    • 0035839641 scopus 로고    scopus 로고
    • Human Neuroglobin, a Hexacoordinate Hemoglobin That Reversibly Binds Oxygen
    • Trent JT, Watts RA, Hargrove MS, (2001) Human Neuroglobin, a Hexacoordinate Hemoglobin That Reversibly Binds Oxygen. J Biol Chem 276: 30106-30110.
    • (2001) J Biol Chem , vol.276 , pp. 30106-30110
    • Trent, J.T.1    Watts, R.A.2    Hargrove, M.S.3
  • 46
    • 0035914459 scopus 로고    scopus 로고
    • Biochemical characterization and ligand binding properties of neuroglobin, a novel member of the globin family
    • Dewilde S, Kiger L, Burmester T, Hankeln T, Baudin-Creuza V, et al. (2001) Biochemical characterization and ligand binding properties of neuroglobin, a novel member of the globin family. J Biol Chem 276: 38949-38955.
    • (2001) J Biol Chem , vol.276 , pp. 38949-38955
    • Dewilde, S.1    Kiger, L.2    Burmester, T.3    Hankeln, T.4    Baudin-Creuza, V.5
  • 48
    • 2542460159 scopus 로고    scopus 로고
    • Structural Dynamics in the Active Site of Murine Neuroglobin and Its Effects on Ligand Binding
    • Nienhaus K, Kriegl JM, Nienhaus GU, (2004) Structural Dynamics in the Active Site of Murine Neuroglobin and Its Effects on Ligand Binding. J Biol Chem 279: 22944-22952.
    • (2004) J Biol Chem , vol.279 , pp. 22944-22952
    • Nienhaus, K.1    Kriegl, J.M.2    Nienhaus, G.U.3
  • 50
    • 0032774244 scopus 로고    scopus 로고
    • Cyanide binding to Lucina pectinata hemoglobin I and to sperm whale myoglobin: an x-ray crystallographic study
    • Bolognesi M, Rosano C, Losso R, Borassi A, Rizzi M, et al. (1999) Cyanide binding to Lucina pectinata hemoglobin I and to sperm whale myoglobin: an x-ray crystallographic study. Biophys J 77: 1093-1099.
    • (1999) Biophys J , vol.77 , pp. 1093-1099
    • Bolognesi, M.1    Rosano, C.2    Losso, R.3    Borassi, A.4    Rizzi, M.5
  • 52
    • 0035146934 scopus 로고    scopus 로고
    • Nitric oxide, cytochrome-c oxidase, and myoglobin
    • Brunori M, (2001) Nitric oxide, cytochrome-c oxidase, and myoglobin. TIBS 26: 21-23.
    • (2001) TIBS , vol.26 , pp. 21-23
    • Brunori, M.1
  • 53
    • 0035312317 scopus 로고    scopus 로고
    • Nitric oxide moves myoglobin centre stage
    • Brunori M, (2001) Nitric oxide moves myoglobin centre stage. TIBS 26: 209-210.
    • (2001) TIBS , vol.26 , pp. 209-210
    • Brunori, M.1
  • 55
    • 34347382940 scopus 로고    scopus 로고
    • Locally enhanced sampling molecular dynamics study of the dioxygen transport in human cytoglobin
    • Orlowski S, Nowak W, (2007) Locally enhanced sampling molecular dynamics study of the dioxygen transport in human cytoglobin. J Mol Model 13: 715-723.
    • (2007) J Mol Model , vol.13 , pp. 715-723
    • Orlowski, S.1    Nowak, W.2
  • 56
    • 34547953953 scopus 로고    scopus 로고
    • Ligand Pathways in Myoglobin: A Review of Trp Cavity Mutations
    • Olson JS, Soman J, Phillips GN Jr, (2007) Ligand Pathways in Myoglobin: A Review of Trp Cavity Mutations. IUBMB Life 59: 552-562.
    • (2007) IUBMB Life , vol.59 , pp. 552-562
    • Olson, J.S.1    Soman, J.2    Phillips Jr., G.N.3
  • 57
    • 0346057931 scopus 로고    scopus 로고
    • Competition with Xenon Elicits Ligand Migration and Escape Pathways in Myoglobin
    • Tetreau C, Blouquit Y, Novikov E, Quiniou E, Lavalette D, (2004) Competition with Xenon Elicits Ligand Migration and Escape Pathways in Myoglobin. Biophys J 86: 435-447.
    • (2004) Biophys J , vol.86 , pp. 435-447
    • Tetreau, C.1    Blouquit, Y.2    Novikov, E.3    Quiniou, E.4    Lavalette, D.5
  • 58
    • 4644277323 scopus 로고    scopus 로고
    • The Escape Process of Carbon Monoxide from Myoglobin to Solution at Physiological Temperature
    • Nishihara Y, Sakakura M, Kimura Y, Terazima M, (2004) The Escape Process of Carbon Monoxide from Myoglobin to Solution at Physiological Temperature. J Am Chem Soc 126: 11877-11888.
    • (2004) J Am Chem Soc , vol.126 , pp. 11877-11888
    • Nishihara, Y.1    Sakakura, M.2    Kimura, Y.3    Terazima, M.4
  • 60
    • 34249819653 scopus 로고    scopus 로고
    • Dynamical regulation of ligand migration by a gate-opening molecular switch in truncated hemoglobin-N from Mycobacterium tuberculosis
    • Bidon-Chanal A, Marti MA, Estrin DA, Luque FJ, (2007) Dynamical regulation of ligand migration by a gate-opening molecular switch in truncated hemoglobin-N from Mycobacterium tuberculosis. J Am Chem Soc 129: 6782-6788.
    • (2007) J Am Chem Soc , vol.129 , pp. 6782-6788
    • Bidon-Chanal, A.1    Marti, M.A.2    Estrin, D.A.3    Luque, F.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.