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Volumn 136, Issue 2-3, 2008, Pages 115-123

Solution 1H NMR study of the active site structure for the double mutant H64Q/V68F cyanide complex from mouse neuroglobin

Author keywords

Cyanide complex; Double mutant; Mouse neuroglobin; NMR; Solution structure

Indexed keywords

CYANIDE; HEME; IRON; MUTANT PROTEIN; MYOGLOBIN; NEUROGLOBIN; GLOBIN; ISOPROTEIN; NERVE PROTEIN; PROTON;

EID: 46049100358     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bpc.2008.05.003     Document Type: Article
Times cited : (7)

References (59)
  • 1
    • 0034726874 scopus 로고    scopus 로고
    • A vertebrate globin expressed in the brain
    • Burmester T., Weich B., Reinhardt S., and Hankeln T. A vertebrate globin expressed in the brain. Nature 407 (2000) 520-523
    • (2000) Nature , vol.407 , pp. 520-523
    • Burmester, T.1    Weich, B.2    Reinhardt, S.3    Hankeln, T.4
  • 2
    • 34249031561 scopus 로고    scopus 로고
    • Neuroglobin, seven years later
    • Brunori M., and Vallone B. Neuroglobin, seven years later. Cell. Mol. Life Sci. 64 (2007) 1259-1268
    • (2007) Cell. Mol. Life Sci. , vol.64 , pp. 1259-1268
    • Brunori, M.1    Vallone, B.2
  • 3
    • 3042727978 scopus 로고    scopus 로고
    • T. Burmester, T. Hankeln, Neuroglobin: A respiratory protein of the nervous system, News Physiol. Sci. 19(2004) 110-113.
    • T. Burmester, T. Hankeln, Neuroglobin: A respiratory protein of the nervous system, News Physiol. Sci. 19(2004) 110-113.
  • 5
    • 0035909992 scopus 로고    scopus 로고
    • Neuroglobin is upregulated by and protects neurons from hypoxic-ischemic injury
    • Sun Y., Jin K., Mao X.O., and Zhu D.A. Neuroglobin is upregulated by and protects neurons from hypoxic-ischemic injury. Proc. Natl. Acad. Sci. U. S. A. 98 (2001) 15306-15311
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 15306-15311
    • Sun, Y.1    Jin, K.2    Mao, X.O.3    Zhu, D.A.4
  • 6
    • 2142654948 scopus 로고    scopus 로고
    • Human neuroglobin interacts with flotillin-1, a lipid raft microdomain-associated protein
    • Wakasugi K., Nakano T., Kitatsuji C., and Morishima I. Human neuroglobin interacts with flotillin-1, a lipid raft microdomain-associated protein. Biochem. Biophys. Res. Commun. 318 (2004) 453-460
    • (2004) Biochem. Biophys. Res. Commun. , vol.318 , pp. 453-460
    • Wakasugi, K.1    Nakano, T.2    Kitatsuji, C.3    Morishima, I.4
  • 7
    • 37649003389 scopus 로고    scopus 로고
    • Neuroglobin attenuates β-amyloid neurotoxicity in vitro and transgenic Alzheimer phenotype in vivo
    • Khan A.A., Mao X.O., Banwait S., Jin K., and Greenberg D.A. Neuroglobin attenuates β-amyloid neurotoxicity in vitro and transgenic Alzheimer phenotype in vivo. Proc. Natl. Acad. Sci. U. S. A. 104 (2008) 19114-19119
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 19114-19119
    • Khan, A.A.1    Mao, X.O.2    Banwait, S.3    Jin, K.4    Greenberg, D.A.5
  • 9
    • 0035839641 scopus 로고    scopus 로고
    • Human neuroglobin, a hexacoordinate hemoglobin that reversibly binds oxygen
    • Trent J.T.I., Watts R.A., and Hargrove M.S. Human neuroglobin, a hexacoordinate hemoglobin that reversibly binds oxygen. J. Biol. Chem. 276 (2001) 30106-30110
    • (2001) J. Biol. Chem. , vol.276 , pp. 30106-30110
    • Trent, J.T.I.1    Watts, R.A.2    Hargrove, M.S.3
  • 11
    • 0037031325 scopus 로고    scopus 로고
    • NO binding properties of neuroglobin, A characterization by EPR and flash photolysis
    • Nistor V.S., Goovaerts E., van Doorslaer S., Dewilde S., and Moens L. NO binding properties of neuroglobin, A characterization by EPR and flash photolysis. Chem. Phys. Lett. 361 (2002) 355-361
    • (2002) Chem. Phys. Lett. , vol.361 , pp. 355-361
    • Nistor, V.S.1    Goovaerts, E.2    van Doorslaer, S.3    Dewilde, S.4    Moens, L.5
  • 15
    • 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 N.L., Falzone C.J., Vuletich D.A., Zhao J., Bryant D.A., and Lecomte J.T. Truncated hemoglobin from the cyanobacterium Synechococcus sp. PCC 7002: evidence for hexacoordination and covalent adduct formation in the ferric recombinant protein. Biochemistry 41 (2002) 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    Lecomte, J.T.6
  • 16
    • 0036219963 scopus 로고    scopus 로고
    • Cytoglobin: a novel globin type ubiquitously expressed in vertebrate tissues
    • Burmester T., Ebner B., Weich B., and Hankeln T. Cytoglobin: a novel globin type ubiquitously expressed in vertebrate tissues. Mol. Biol. Evol. 19 (2002) 416-421
    • (2002) Mol. Biol. Evol. , vol.19 , pp. 416-421
    • Burmester, T.1    Ebner, B.2    Weich, B.3    Hankeln, T.4
  • 17
    • 1842637797 scopus 로고    scopus 로고
    • Structural change of the heme pocket due to disulfide bridge formation is significantly larger for neuroglobin than for cytoglobin
    • Vinck E., van Doorslaer S., Dewilde S., and Moens L. Structural change of the heme pocket due to disulfide bridge formation is significantly larger for neuroglobin than for cytoglobin. J. Am. Chem. Soc. 126 (2004) 4516-4517
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 4516-4517
    • Vinck, E.1    van Doorslaer, S.2    Dewilde, S.3    Moens, L.4
  • 18
    • 4644261106 scopus 로고    scopus 로고
    • Bis-histidyl hexacoordination in hemoglobins facilitates heme reduction kinetics
    • Weiland T.R., Kundu S., Trent J.T., Hoy J.A., and Hargrove M.S. Bis-histidyl hexacoordination in hemoglobins facilitates heme reduction kinetics. J. Am. Chem. Soc. 126 (2004) 11930-11935
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 11930-11935
    • Weiland, T.R.1    Kundu, S.2    Trent, J.T.3    Hoy, J.A.4    Hargrove, M.S.5
  • 20
    • 7444261414 scopus 로고    scopus 로고
    • Structure-function relationships in unusual nonvertebrate globins
    • Shikama K., and Matsuoka A. Structure-function relationships in unusual nonvertebrate globins. Crit. Rev. Biochem. Mol. Biol. 39 (2004) 217-259
    • (2004) Crit. Rev. Biochem. Mol. Biol. , vol.39 , pp. 217-259
    • Shikama, K.1    Matsuoka, A.2
  • 21
    • 2542460159 scopus 로고    scopus 로고
    • Structural dynamics in the active site of murine neuroglobin and its effects on ligand binding
    • Nienhaus K., Kriegl J.M., and Nienhaus G.U. Structural dynamics in the active site of murine neuroglobin and its effects on ligand binding. J. Biol. Chem. 279 (2004) 22944-22952
    • (2004) J. Biol. Chem. , vol.279 , pp. 22944-22952
    • Nienhaus, K.1    Kriegl, J.M.2    Nienhaus, G.U.3
  • 22
    • 0038682731 scopus 로고    scopus 로고
    • 1H NMR characterization of equilibrium heme orientational disorder with functional consequences in mouse neuroglobin
    • 1H NMR characterization of equilibrium heme orientational disorder with functional consequences in mouse neuroglobin. J. Am. Chem. Soc. 125 (2003) 8080-8081
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 8080-8081
    • Du, W.H.1    Syvitski, R.2    Dewilde, S.3    Moens, L.4    La Mar, G.N.5
  • 24
    • 2642521269 scopus 로고    scopus 로고
    • The structure of murine neuroglobin: Novel pathways for ligand migration and binding
    • Vallone B., Nienhaus K., Brunori M., and Nienhaus G.U. The structure of murine neuroglobin: Novel pathways for ligand migration and binding. Proteins 56 (2004) 85-92
    • (2004) Proteins , vol.56 , pp. 85-92
    • Vallone, B.1    Nienhaus, K.2    Brunori, M.3    Nienhaus, G.U.4
  • 25
    • 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., and Nienhaus G.U. The structure of carbonmonoxy neuroglobin reveals a heme-sliding mechanism for control of ligand affinity. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 17351-17356
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 17351-17356
    • Vallone, B.1    Nienhaus, K.2    Matthes, A.3    Brunori, M.4    Nienhaus, G.U.5
  • 26
    • 0021766921 scopus 로고
    • Cavities in proteins: structure of a metmyoglobin xenon complex solved to 1.9 ANG
    • 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 ANG. 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
  • 27
    • 0032540246 scopus 로고    scopus 로고
    • Solution and crystal structures of a sperm whale myoglobin triple mutant that mimics the sulfide-binding hemoglobin from Lucina pectinata
    • Nguyen B.D., Zhao X.F., Vyas K., La Mar G.N., Lile R.A., Bruker E.A., Philips Jr. G.N., Olson J.S., and Wittenberg J.B. Solution and crystal structures of a sperm whale myoglobin triple mutant that mimics the sulfide-binding hemoglobin from Lucina pectinata. J. Biol. Chem. 273 (1998) 9517-9526
    • (1998) J. Biol. Chem. , vol.273 , pp. 9517-9526
    • Nguyen, B.D.1    Zhao, X.F.2    Vyas, K.3    La Mar, G.N.4    Lile, R.A.5    Bruker, E.A.6    Philips Jr., G.N.7    Olson, J.S.8    Wittenberg, J.B.9
  • 28
    • 0028303641 scopus 로고
    • Correlation between the steric bulk of the distal E7 and E11 residues and the tilt of the FeCN unit in cyanometmyoglobin as determined by NMR from the orientation of the magnetic axes in single and double point mutants
    • Rajarathnam K., Qin J., La Mar G.N., Chiu M.L., and Sligar S.G. Correlation between the steric bulk of the distal E7 and E11 residues and the tilt of the FeCN unit in cyanometmyoglobin as determined by NMR from the orientation of the magnetic axes in single and double point mutants. Biochemistry 33 (1994) 5493-5501
    • (1994) Biochemistry , vol.33 , pp. 5493-5501
    • Rajarathnam, K.1    Qin, J.2    La Mar, G.N.3    Chiu, M.L.4    Sligar, S.G.5
  • 30
    • 1242316981 scopus 로고    scopus 로고
    • Residues in the distal heme pocket of neuroglobin: implications for the multiple ligand binding steps
    • Uno T., Ryu D., Tsutsumi H., Tomisugi Y., Ishikawa Y., Wilkson A.J., Sato H., and Hayashi T. Residues in the distal heme pocket of neuroglobin: implications for the multiple ligand binding steps. J. Biol. Chem. 279 (2004) 5886-5893
    • (2004) J. Biol. Chem. , vol.279 , pp. 5886-5893
    • Uno, T.1    Ryu, D.2    Tsutsumi, H.3    Tomisugi, Y.4    Ishikawa, Y.5    Wilkson, A.J.6    Sato, H.7    Hayashi, T.8
  • 33
    • 0024519403 scopus 로고
    • Discrimination between oxygen and carbon monoxide and inhibition of autooxidation by myoglobin. Site-directed mutagenesis of the distal histidine
    • Springer B.A., Egeberg K.D., Sligar S.G., Rohlfs R.J., Mathews A.J., and Olson J.S. Discrimination between oxygen and carbon monoxide and inhibition of autooxidation by myoglobin. Site-directed mutagenesis of the distal histidine. J. Biol. Chem. 264 (1989) 3057-3060
    • (1989) J. Biol. Chem. , vol.264 , pp. 3057-3060
    • Springer, B.A.1    Egeberg, K.D.2    Sligar, S.G.3    Rohlfs, R.J.4    Mathews, A.J.5    Olson, J.S.6
  • 34
    • 0028035164 scopus 로고
    • Structure of the sulfide-reactive hemoglobin from the clam Lucina pectinata. Crystallographic analysis at 1.5 A resolution
    • Rizzi M., Wittenberg J.B., Coda A., Fasano M., Ascenzi P., and Bolognesi M. Structure of the sulfide-reactive hemoglobin from the clam Lucina pectinata. Crystallographic analysis at 1.5 A resolution. J. Mol. Biol. 244 (1994) 86-99
    • (1994) J. Mol. Biol. , vol.244 , pp. 86-99
    • Rizzi, M.1    Wittenberg, J.B.2    Coda, A.3    Fasano, M.4    Ascenzi, P.5    Bolognesi, M.6
  • 37
    • 0001021790 scopus 로고
    • Dynamic range problem in Fourier transform NMR. Modified WEFT pulse sequence
    • Gupta P.K. Dynamic range problem in Fourier transform NMR. Modified WEFT pulse sequence. J. Magn. Reson. 24 (1976) 461-465
    • (1976) J. Magn. Reson. , vol.24 , pp. 461-465
    • Gupta, P.K.1
  • 38
    • 0343359244 scopus 로고
    • Investigation of exchange processes by two-dimensional NMR spectroscopy
    • Jeener J., Meier B.H., Bachmann P., and Ernst R.R. Investigation of exchange processes by two-dimensional NMR spectroscopy. J. Chem. Phys. 71 (1979) 4546-4553
    • (1979) J. Chem. Phys. , vol.71 , pp. 4546-4553
    • Jeener, J.1    Meier, B.H.2    Bachmann, P.3    Ernst, R.R.4
  • 39
    • 0024282849 scopus 로고
    • Clean TOCSY for proton spin system identification in macromolecules
    • Griesinger C., Otting G., Wuthrich K., and Ernst R.R. Clean TOCSY for proton spin system identification in macromolecules. J. Am. Chem. Soc. 110 (1988) 7870-7872
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 7870-7872
    • Griesinger, C.1    Otting, G.2    Wuthrich, K.3    Ernst, R.R.4
  • 40
    • 0033922153 scopus 로고    scopus 로고
    • The use of chemical shift temperature gradients to establish the paramagnetic susceptibility tensor orientation: implication for structure determination/refinement in paramagnetic metalloproteins
    • Xia Z.C., Nguyen B., and La Mar G.N. The use of chemical shift temperature gradients to establish the paramagnetic susceptibility tensor orientation: implication for structure determination/refinement in paramagnetic metalloproteins. J. Biomol. NMR 17 (2000) 167-174
    • (2000) J. Biomol. NMR , vol.17 , pp. 167-174
    • Xia, Z.C.1    Nguyen, B.2    La Mar, G.N.3
  • 42
    • 84985733652 scopus 로고
    • 1H-NMR parameters of the common amino acid residues measured in aqueous solutions of the linear tetrapeptides H-Gly-Gly-X-L-Ala-OH
    • 1H-NMR parameters of the common amino acid residues measured in aqueous solutions of the linear tetrapeptides H-Gly-Gly-X-L-Ala-OH. Biopolymers 18 (1979) 285-297
    • (1979) Biopolymers , vol.18 , pp. 285-297
    • Bundi, A.1    Wuthrich, K.2
  • 43
    • 0026410969 scopus 로고
    • Relationship between nuclear magnetic resonance chemical shift and protein secondary structure
    • Wishart D.S., Sykes B.D., and Richard F.M. Relationship between nuclear magnetic resonance chemical shift and protein secondary structure. J. Mol. Biol. 222 (1991) 311-333
    • (1991) J. Mol. Biol. , vol.222 , pp. 311-333
    • Wishart, D.S.1    Sykes, B.D.2    Richard, F.M.3
  • 44
    • 0000895627 scopus 로고
    • Calibration of ring-current models for the heme ring
    • Cross K.J., and Wright P.E. Calibration of ring-current models for the heme ring. J. Magn. Reson. 64 (1985) 231-240
    • (1985) J. Magn. Reson. , vol.64 , pp. 231-240
    • Cross, K.J.1    Wright, P.E.2
  • 45
    • 0025141855 scopus 로고
    • NMR determination of the orientation of the magnetic susceptibility tensor in cyanometmyoglobin: a new probe of steric tilt of bound ligand
    • Emerson S.D., and La Mar G.N. NMR determination of the orientation of the magnetic susceptibility tensor in cyanometmyoglobin: a new probe of steric tilt of bound ligand. Biochemistry 29 (1990) 1556-1566
    • (1990) Biochemistry , vol.29 , pp. 1556-1566
    • Emerson, S.D.1    La Mar, G.N.2
  • 46
  • 47
    • 0027198105 scopus 로고
    • Solution NMR determination of active site structure for a paramagnetic protein: cyano-met Aplysia Mb
    • Qin J., La Mar G.N., Ascoli F., and Brunori M. Solution NMR determination of active site structure for a paramagnetic protein: cyano-met Aplysia Mb. J. Mol. Biol. 231 (1993) 1009-1023
    • (1993) J. Mol. Biol. , vol.231 , pp. 1009-1023
    • Qin, J.1    La Mar, G.N.2    Ascoli, F.3    Brunori, M.4
  • 48
    • 28444481048 scopus 로고    scopus 로고
    • H-1-NMR study of the effect of temperature through reversible unfolding on the heme pocket molecular structure and magnetic properties of Aplysia limacina cyano-metmyoglobin
    • Xia Z.C., Bao D.N.Y., Brunori M., Cutruzzola F., and La Mar G.N. H-1-NMR study of the effect of temperature through reversible unfolding on the heme pocket molecular structure and magnetic properties of Aplysia limacina cyano-metmyoglobin. Biophys. J. 89 (2005) 4149-4158
    • (2005) Biophys. J. , vol.89 , pp. 4149-4158
    • Xia, Z.C.1    Bao, D.N.Y.2    Brunori, M.3    Cutruzzola, F.4    La Mar, G.N.5
  • 51
    • 0026948866 scopus 로고
    • Complete sequence-specific assignment of hyperfine-shifted residues in the active site of a paramagnetic protein: cyano-met Aplysia myoglobin
    • Qin J., and La Mar G.N. Complete sequence-specific assignment of hyperfine-shifted residues in the active site of a paramagnetic protein: cyano-met Aplysia myoglobin. J. Biomol. NMR 2 (1992) 597-618
    • (1992) J. Biomol. NMR , vol.2 , pp. 597-618
    • Qin, J.1    La Mar, G.N.2
  • 52
    • 0027245807 scopus 로고
    • Solution structure determination of the heme cavity in the His (E7)Val cyano-met myoglobin point mutant based on the proton NMR detected dipolar field of the iron: evidence for contraction of the heme pocket
    • Rajarathnam K., Qin J., La Mar G.N., Chiu M.L., and Sligar S.G. Solution structure determination of the heme cavity in the His (E7)Val cyano-met myoglobin point mutant based on the proton NMR detected dipolar field of the iron: evidence for contraction of the heme pocket. Biochemistry 32 (1993) 5670-5680
    • (1993) Biochemistry , vol.32 , pp. 5670-5680
    • Rajarathnam, K.1    Qin, J.2    La Mar, G.N.3    Chiu, M.L.4    Sligar, S.G.5
  • 53
    • 0001165867 scopus 로고    scopus 로고
    • Kadish K.M., Guilard R., and Smith K.M. (Eds), Academic Press, San Diego, USA
    • La Mar G.N., Satterlee J.D., and de Ropp J.S. In: Kadish K.M., Guilard R., and Smith K.M. (Eds). The Porphyrins Handbook (1999), Academic Press, San Diego, USA 185-298
    • (1999) The Porphyrins Handbook , pp. 185-298
    • La Mar, G.N.1    Satterlee, J.D.2    de Ropp, J.S.3
  • 54
    • 0033550490 scopus 로고    scopus 로고
    • Solution NMR determination of the anisotropy and orientation of the paramagnetic susceptibility tensor as a function of temperature for metmyoglobin cyanide: implications for the population of excited electronic states
    • Nguyen B.D., Xia Z.C., Yeh D.C., Vyas K., Deaguero H., and La Mar G.N. Solution NMR determination of the anisotropy and orientation of the paramagnetic susceptibility tensor as a function of temperature for metmyoglobin cyanide: implications for the population of excited electronic states. J. Am. Chem. Soc. 121 (1999) 208-217
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 208-217
    • Nguyen, B.D.1    Xia, Z.C.2    Yeh, D.C.3    Vyas, K.4    Deaguero, H.5    La Mar, G.N.6
  • 56
    • 33745758066 scopus 로고    scopus 로고
    • The heme environment of mouse neuroglobin: histidine imidazole plane orientations obtained from solution NMR and EPR spectroscopy as compared with X-ray crystrallography
    • Walker F.A. The heme environment of mouse neuroglobin: histidine imidazole plane orientations obtained from solution NMR and EPR spectroscopy as compared with X-ray crystrallography. J. Biol. Inorg. Chem. 11 (2006) 391-397
    • (2006) J. Biol. Inorg. Chem. , vol.11 , pp. 391-397
    • Walker, F.A.1
  • 57
    • 33749537264 scopus 로고    scopus 로고
    • 1H NMR characterization of the axial bonding of the two his in oxidized human cytoglobin
    • 1H NMR characterization of the axial bonding of the two his in oxidized human cytoglobin. J. Am. Chem. Soc. 128 (2006) 12988-12999
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 12988-12999
    • Bondarenko, V.1    Dewilde, S.2    Moens, L.3    La Mar, G.N.4
  • 59
    • 33846968462 scopus 로고    scopus 로고
    • Neuroglobin and cytoglobin expression in mice
    • Fordel S., Thijs L., Moens L., and Dewilde S. Neuroglobin and cytoglobin expression in mice. FEBS J. 274 (2007) 1312-1317
    • (2007) FEBS J. , vol.274 , pp. 1312-1317
    • Fordel, S.1    Thijs, L.2    Moens, L.3    Dewilde, S.4


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