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Volumn 53, Issue 15, 2014, Pages 2474-2482

A model for the flexibility of the distal histidine in dehaloperoxidase- hemoglobin A based on X-ray crystal structures of the carbon monoxide adduct

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BIOCHEMISTRY; CARBON MONOXIDE; DESIGN FOR TESTABILITY; HEMOGLOBIN; HYDROGEN BONDS; IRON COMPOUNDS; LIGANDS; MOLECULAR DYNAMICS; PORPHYRINS; PROBABILITY DENSITY FUNCTION; VOLATILE FATTY ACIDS;

EID: 84899437266     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi5001905     Document Type: Article
Times cited : (12)

References (86)
  • 2
    • 0039316844 scopus 로고    scopus 로고
    • An unusual dehalogenating peroxidase from the marine terebellid polychaete Amphitrite ornata
    • Chen, Y. P., Woodin, S. A., Lincoln, D. E., and Lovell, C. R. (1996) An unusual dehalogenating peroxidase from the marine terebellid polychaete Amphitrite ornata J. Biol. Chem. 271, 4609-4612
    • (1996) J. Biol. Chem. , vol.271 , pp. 4609-4612
    • Chen, Y.P.1    Woodin, S.A.2    Lincoln, D.E.3    Lovell, C.R.4
  • 3
    • 0034794637 scopus 로고    scopus 로고
    • Amphitrite ornata, a marine worm, contains two dehaloperoxidase genes
    • Han, K., Woodin, S. A., Lincoln, D. E., Fielman, K. T., and Ely, B. (2001) Amphitrite ornata, a marine worm, contains two dehaloperoxidase genes Mar. Biotechnol. 3, 287-292
    • (2001) Mar. Biotechnol. , vol.3 , pp. 287-292
    • Han, K.1    Woodin, S.A.2    Lincoln, D.E.3    Fielman, K.T.4    Ely, B.5
  • 4
    • 77952040623 scopus 로고    scopus 로고
    • Structure of dehaloperoxidase B at 1.58 angstrom resolution and structural characterization of the AB dimer from Amphitrite ornata
    • de Serrano, V., D'Antonio, J., Franzen, S., and Ghiladi, R. A. (2010) Structure of dehaloperoxidase B at 1.58 angstrom resolution and structural characterization of the AB dimer from Amphitrite ornata Acta Crystallogr., Sect. D: Biol. Crystallogr. 66, 529-538
    • (2010) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.66 , pp. 529-538
    • De Serrano, V.1    D'Antonio, J.2    Franzen, S.3    Ghiladi, R.A.4
  • 5
    • 0032914442 scopus 로고    scopus 로고
    • Oxidative 4-dechlorination of 2,4,6-trichlorophenol catalyzed by horseradish peroxidase
    • Ferrari, R. P., Laurenti, E., and Trotta, F. (1999) Oxidative 4-dechlorination of 2,4,6-trichlorophenol catalyzed by horseradish peroxidase JBIC, J. Biol. Inorg. Chem. 4, 232-237
    • (1999) JBIC, J. Biol. Inorg. Chem. , vol.4 , pp. 232-237
    • Ferrari, R.P.1    Laurenti, E.2    Trotta, F.3
  • 8
    • 79959950550 scopus 로고    scopus 로고
    • Reactivity of Deoxy- and Oxyferrous Dehaloperoxidase B from Amphitrite ornata: Identification of Compound II and Its Ferrous-Hydroperoxide Precursor
    • D'Antonio, J. and Ghiladi, R. A. (2011) Reactivity of Deoxy- and Oxyferrous Dehaloperoxidase B from Amphitrite ornata: Identification of Compound II and Its Ferrous-Hydroperoxide Precursor Biochemistry 50, 5999-6011
    • (2011) Biochemistry , vol.50 , pp. 5999-6011
    • D'Antonio, J.1    Ghiladi, R.A.2
  • 9
    • 84899439157 scopus 로고    scopus 로고
    • X-ray Crystal Structures of Substrate-bound for of DHP
    • 10.1021/bi400627w.
    • Lebioda, L. and Dawson, J. H. X-ray Crystal Structures of Substrate-bound for of DHP, Biochemistry, 10.1021/bi400627w.
    • Biochemistry
    • Lebioda, L.1    Dawson, J.H.2
  • 10
    • 84875986002 scopus 로고    scopus 로고
    • Structural and Kinetic Study of an Internal Substrate Binding Site in Dehaloperoxidase-Hemoglobin A from Amphitrite ornata
    • Zhao, J., de Serrano, V., Zhao, J. J., Le, P., and Franzen, S. (2013) Structural and Kinetic Study of an Internal Substrate Binding Site in Dehaloperoxidase-Hemoglobin A from Amphitrite ornata Biochemistry 52, 2427-2439
    • (2013) Biochemistry , vol.52 , pp. 2427-2439
    • Zhao, J.1    De Serrano, V.2    Zhao, J.J.3    Le, P.4    Franzen, S.5
  • 11
    • 84872486657 scopus 로고    scopus 로고
    • Catalytic efficiency of dehaloperoxidase A is controlled by electrostatics - Application of the vibrational Stark effect to understand enzyme kinetics
    • Schkolnik, G., Utesch, T., Zhao, J. J., Jiang, S., Thompson, M. K., Mroginski, M. A., Hildebrandt, P., and Franzen, S. (2013) Catalytic efficiency of dehaloperoxidase A is controlled by electrostatics-application of the vibrational Stark effect to understand enzyme kinetics Biochem. Biophys. Res. Commun. 430, 1011-1015
    • (2013) Biochem. Biophys. Res. Commun. , vol.430 , pp. 1011-1015
    • Schkolnik, G.1    Utesch, T.2    Zhao, J.J.3    Jiang, S.4    Thompson, M.K.5    Mroginski, M.A.6    Hildebrandt, P.7    Franzen, S.8
  • 12
    • 84859880405 scopus 로고    scopus 로고
    • Study of the electrostatic effects of mutations on the surface of dehaloperoxidase-hemoglobin A
    • Zhao, J. J., Rowe, J., Franzen, J., He, C., and Franzen, S. (2012) Study of the electrostatic effects of mutations on the surface of dehaloperoxidase- hemoglobin A Biochem. Biophys. Res. Commun. 420, 733-737
    • (2012) Biochem. Biophys. Res. Commun. , vol.420 , pp. 733-737
    • Zhao, J.J.1    Rowe, J.2    Franzen, J.3    He, C.4    Franzen, S.5
  • 13
    • 33746349251 scopus 로고    scopus 로고
    • Spectroscopic Study of Substrate Binding to the Carbonmonoxy Form of Dehaloperoxidase from Amphitrite ornata
    • Nienhaus, K., Deng, P., Belyea, J., Franzen, S., and Nienhaus, G. U. (2006) Spectroscopic Study of Substrate Binding to the Carbonmonoxy Form of Dehaloperoxidase from Amphitrite ornata J. Phys. Chem. B 110, 13264-13276
    • (2006) J. Phys. Chem. B , vol.110 , pp. 13264-13276
    • Nienhaus, K.1    Deng, P.2    Belyea, J.3    Franzen, S.4    Nienhaus, G.U.5
  • 14
    • 55249126699 scopus 로고    scopus 로고
    • Determinants of Substrate Internalization in the Distal Pocket of Dehaloperoxidase Hemoglobin of Amphitrite ornata
    • Nienhaus, K., Nickel, E., Davis, M. F., Franzen, S., and Nienhaus, G. U. (2008) Determinants of Substrate Internalization in the Distal Pocket of Dehaloperoxidase Hemoglobin of Amphitrite ornata Biochemistry 47, 12985-12994
    • (2008) Biochemistry , vol.47 , pp. 12985-12994
    • Nienhaus, K.1    Nickel, E.2    Davis, M.F.3    Franzen, S.4    Nienhaus, G.U.5
  • 15
    • 84887599535 scopus 로고    scopus 로고
    • Functional consequences of the open distal pocket of dehaloperoxidase- hemoglobin observed by time-resolved X-ray crystallography
    • Zhao, J., Srajer, V., and Franzen, S. (2013) Functional consequences of the open distal pocket of dehaloperoxidase-hemoglobin observed by time-resolved X-ray crystallography Biochemistry 52, 7943-7950
    • (2013) Biochemistry , vol.52 , pp. 7943-7950
    • Zhao, J.1    Srajer, V.2    Franzen, S.3
  • 17
    • 77749259052 scopus 로고    scopus 로고
    • New insights into the role of distal histidine flexibility in ligand stabilization of Dehaloperoxidase-hemoglobin from Amphitrite ornata
    • Nicoletti, F. P., Thompson, M. K., Howes, B. D., Franzen, S., and Smulevich, G. (2010) New insights into the role of distal histidine flexibility in ligand stabilization of Dehaloperoxidase-hemoglobin from Amphitrite ornata Biochemistry 49, 1903-1912
    • (2010) Biochemistry , vol.49 , pp. 1903-1912
    • Nicoletti, F.P.1    Thompson, M.K.2    Howes, B.D.3    Franzen, S.4    Smulevich, G.5
  • 19
    • 0035831479 scopus 로고    scopus 로고
    • Flavohemoglobin, a globin with a peroxidase-like catalytic site
    • Mukai, M., Mills, C. E., Poole, R. K., and Yeh, S. R. (2001) Flavohemoglobin, a globin with a peroxidase-like catalytic site J. Biol. Chem. 276, 7272-7277
    • (2001) J. Biol. Chem. , vol.276 , pp. 7272-7277
    • Mukai, M.1    Mills, C.E.2    Poole, R.K.3    Yeh, S.R.4
  • 21
    • 0029646104 scopus 로고
    • The crystal structure of chloroperoxidase: A heme peroxidase-cytochrome P450 functional hybrid
    • Sundaramoorthy, M., Terner, J., and Poulos, T. L. (1995) The crystal structure of chloroperoxidase: A heme peroxidase-cytochrome P450 functional hybrid Structure 3, 1367-1377
    • (1995) Structure , vol.3 , pp. 1367-1377
    • Sundaramoorthy, M.1    Terner, J.2    Poulos, T.L.3
  • 24
    • 84875796365 scopus 로고    scopus 로고
    • Role of Polarity of the Distal Pocket in the Control of Inhibitor Binding in Dehaloperoxidase-Hemoglobin
    • Plummer, A., Thompson, M. K., and Franzen, S. (2013) Role of Polarity of the Distal Pocket in the Control of Inhibitor Binding in Dehaloperoxidase- Hemoglobin Biochemistry 52, 2218-2227
    • (2013) Biochemistry , vol.52 , pp. 2218-2227
    • Plummer, A.1    Thompson, M.K.2    Franzen, S.3
  • 25
    • 0019321508 scopus 로고
    • The stereochemistry of peroxidase catalysis
    • Poulos, T. L. and Kraut, J. (1980) The stereochemistry of peroxidase catalysis J. Biol. Chem. 255, 8199-8205
    • (1980) J. Biol. Chem. , vol.255 , pp. 8199-8205
    • Poulos, T.L.1    Kraut, J.2
  • 26
    • 0027424783 scopus 로고
    • Effect of Arginine-48 Replacement on the Reaction between Cytochrome-C Peroxidase and Hydrogen-Peroxide
    • Vitello, L. B., Erman, J. E., Miller, M. A., Wang, J., and Kraut, J. (1993) Effect of Arginine-48 Replacement on the Reaction between Cytochrome-C Peroxidase and Hydrogen-Peroxide Biochemistry 32, 9807-9818
    • (1993) Biochemistry , vol.32 , pp. 9807-9818
    • Vitello, L.B.1    Erman, J.E.2    Miller, M.A.3    Wang, J.4    Kraut, J.5
  • 27
    • 0029986887 scopus 로고    scopus 로고
    • Crystal structures of CO-, deoxy- and Met-myoglobins at various pH values
    • Yang, F. and Phillips, G. N., Jr. (1996) Crystal structures of CO-, deoxy- and Met-myoglobins at various pH values J. Mol. Biol. 256, 762-774
    • (1996) J. Mol. Biol. , vol.256 , pp. 762-774
    • Yang, F.1    Phillips Jr., G.N.2
  • 28
    • 0000379278 scopus 로고    scopus 로고
    • Probing Heme Protein Conformational Equilibration Rates with Kinetic Selection
    • Tian, W. D., Sage, J. T., Champion, P. M., Chien, E., and Sligar, S. G. (1996) Probing Heme Protein Conformational Equilibration Rates with Kinetic Selection Biochemistry 35, 3487-3502
    • (1996) Biochemistry , vol.35 , pp. 3487-3502
    • Tian, W.D.1    Sage, J.T.2    Champion, P.M.3    Chien, E.4    Sligar, S.G.5
  • 29
    • 78650347504 scopus 로고    scopus 로고
    • An Investigation of the Distal Histidyl Hydrogen Bonds in Oxyhemoglobin: Effects of Temperature, pH, and Inositol Hexaphosphate
    • Yuan, Y., Simplaceanu, V., Ho, N. T., and Ho, C. (2010) An Investigation of the Distal Histidyl Hydrogen Bonds in Oxyhemoglobin: Effects of Temperature, pH, and Inositol Hexaphosphate Biochemistry 49, 10606-10615
    • (2010) Biochemistry , vol.49 , pp. 10606-10615
    • Yuan, Y.1    Simplaceanu, V.2    Ho, N.T.3    Ho, C.4
  • 30
    • 76749095979 scopus 로고    scopus 로고
    • Determination of Separate Inhibitor and Substrate Binding Sites in the Dehaloperoxidase-Hemoglobin from Amphitrite ornata
    • Davis, M. F., Bobay, B. G., and Franzen, S. (2010) Determination of Separate Inhibitor and Substrate Binding Sites in the Dehaloperoxidase- Hemoglobin from Amphitrite ornata Biochemistry 49, 1199-1206
    • (2010) Biochemistry , vol.49 , pp. 1199-1206
    • Davis, M.F.1    Bobay, B.G.2    Franzen, S.3
  • 31
    • 64349114283 scopus 로고    scopus 로고
    • Different Modes of Binding of Mono-, Di-, and Trihalogenated Phenols to the Hemoglobin Dehaloperoxidase from Amphitrite ornata
    • Davis, M. F., Gracz, H., Vendeix, F. A. P., de Serrano, V., Somasundaram, A., Decatur, S. M., and Franzen, S. (2009) Different Modes of Binding of Mono-, Di-, and Trihalogenated Phenols to the Hemoglobin Dehaloperoxidase from Amphitrite ornata Biochemistry 48, 2164-2172
    • (2009) Biochemistry , vol.48 , pp. 2164-2172
    • Davis, M.F.1    Gracz, H.2    Vendeix, F.A.P.3    De Serrano, V.4    Somasundaram, A.5    Decatur, S.M.6    Franzen, S.7
  • 32
    • 34748844557 scopus 로고    scopus 로고
    • X-ray Crystal Structural Analysis of the Binding Site in the Ferric and Oxyferrous forms of the Recombinant Heme Dehaloperoxidase Cloned from Amphitrite ornata
    • de Serrano, V., Chen, Z., Davis, M. F., and Franzen, S. (2007) X-ray Crystal Structural Analysis of the Binding Site in the Ferric and Oxyferrous forms of the Recombinant Heme Dehaloperoxidase Cloned from Amphitrite ornata Acta Crystallogr., Sect. D: Biol. Crystallogr. D63, 1094-1101
    • (2007) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.63 , pp. 1094-1101
    • De Serrano, V.1    Chen, Z.2    Davis, M.F.3    Franzen, S.4
  • 33
    • 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. (1999) Crystal structures of myoglobin-ligand complexes at near-atomic resolution Biophys. J. 77, 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
  • 34
    • 0000348848 scopus 로고    scopus 로고
    • Bound CO Is A Molecular Probe of Electrostatic Potential in the Distal Pocket of Myoglobin
    • Phillips, G. N., Jr., Teodoro, M. L., Li, T., Smith, B., and Olson, J. S. (1999) Bound CO Is A Molecular Probe of Electrostatic Potential in the Distal Pocket of Myoglobin J. Phys. Chem. B 103, 8817-8829
    • (1999) J. Phys. Chem. B , vol.103 , pp. 8817-8829
    • Phillips Jr., G.N.1    Teodoro, M.L.2    Li, T.3    Smith, B.4    Olson, J.S.5
  • 35
    • 0014030651 scopus 로고
    • An X-ray Study of Azide Methaemoglobin
    • Perutz, M. F. and Mathews, F. S. (1966) An X-ray Study of Azide Methaemoglobin J. Mol. Biol. 21, 199-&
    • (1966) J. Mol. Biol. , vol.21 , pp. 199
    • Perutz, M.F.1    Mathews, F.S.2
  • 37
    • 79953185359 scopus 로고    scopus 로고
    • Blocking the Gate to Ligand Entry in Human Hemoglobin
    • Birukou, I., Soman, J., and Olson, J. S. (2011) Blocking the Gate to Ligand Entry in Human Hemoglobin J. Biol. Chem. 286, 10515-10529
    • (2011) J. Biol. Chem. , vol.286 , pp. 10515-10529
    • Birukou, I.1    Soman, J.2    Olson, J.S.3
  • 38
    • 0027768729 scopus 로고
    • Distal pocket polarity in ligand binding to myoglobin: Deoxy and carbonmonoxy forms of a threonine68(E11) mutant investigated by x-ray crystallography and infrared spectroscopy
    • Cameron, A. D., Smerdon, S. J., Wilkinson, A. J., Habash, J., Helliwell, J. R., Li, T., and Olson, J. S. (1993) Distal pocket polarity in ligand binding to myoglobin: Deoxy and carbonmonoxy forms of a threonine68(E11) mutant investigated by x-ray crystallography and infrared spectroscopy Biochemistry 32, 13061-13070
    • (1993) Biochemistry , vol.32 , pp. 13061-13070
    • Cameron, A.D.1    Smerdon, S.J.2    Wilkinson, A.J.3    Habash, J.4    Helliwell, J.R.5    Li, T.6    Olson, J.S.7
  • 39
    • 0028223077 scopus 로고
    • How Far Can Protein Bend the FeCO Unit? Distal Polar and Steric Effects in Heme Proteins and Models
    • Ray, G. B., Li, X.-Y., Ibers, J. A., Sessler, J. L., and Spiro, T. G. (1994) How Far Can Protein Bend the FeCO Unit? Distal Polar and Steric Effects in Heme Proteins and Models J. Am. Chem. Soc. 116, 162-176
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 162-176
    • Ray, G.B.1    Li, X.-Y.2    Ibers, J.A.3    Sessler, J.L.4    Spiro, T.G.5
  • 40
    • 0032550647 scopus 로고    scopus 로고
    • The Unusual Reactivities of Amphitrite ornata Dehaloperoxidase and Notomastus lobatus Chloroperoxidase Do Not Arise from a Histidine Imidazolate Proximal Heme Iron Ligand
    • Franzen, S., Roach, M. P., Chen, Y.-P., Dyer, R. B., Woodruff, W. H., and Dawson, J. H. (1998) The Unusual Reactivities of Amphitrite ornata Dehaloperoxidase and Notomastus lobatus Chloroperoxidase Do Not Arise from a Histidine Imidazolate Proximal Heme Iron Ligand J. Am. Chem. Soc. 120, 4658-4661
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 4658-4661
    • Franzen, S.1    Roach, M.P.2    Chen, Y.-P.3    Dyer, R.B.4    Woodruff, W.H.5    Dawson, J.H.6
  • 41
    • 84857247266 scopus 로고    scopus 로고
    • Insights into the anomalous heme pocket of rainbow trout myoglobin
    • Howes, B. D., Helbo, S., Fago, A., and Smulevich, G. (2012) Insights into the anomalous heme pocket of rainbow trout myoglobin J. Inorg. Biochem. 109, 1-8
    • (2012) J. Inorg. Biochem. , vol.109 , pp. 1-8
    • Howes, B.D.1    Helbo, S.2    Fago, A.3    Smulevich, G.4
  • 42
  • 43
    • 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. (1989) Discrimination Between Oxygen and Carbon Monoxide and Inhibition of Autooxidation by Myoglobin-Site-Directed Mutagenesis of the Distal Histidine J. Biol. Chem. 264, 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
  • 45
    • 84857324414 scopus 로고    scopus 로고
    • An Atomistic View on Human Hemoglobin Carbon Monoxide Migration Processes
    • Lucas, M. F. and Guallar, V. (2012) An Atomistic View on Human Hemoglobin Carbon Monoxide Migration Processes Biophys. J. 102, 887-896
    • (2012) Biophys. J. , vol.102 , pp. 887-896
    • Lucas, M.F.1    Guallar, V.2
  • 47
    • 84884497354 scopus 로고    scopus 로고
    • The role of T56 in controlling the flexibility of the distal histidine in dehaloperoxidase-hemoglobin from Amphitrite ornata
    • Jiang, S., Wright, I., Swartz, P., and Franzen, S. (2013) The role of T56 in controlling the flexibility of the distal histidine in dehaloperoxidase- hemoglobin from Amphitrite ornata Biochim. Biophys. Acta, Proteins Proteomics 1834, 2020-2029
    • (2013) Biochim. Biophys. Acta, Proteins Proteomics , vol.1834 , pp. 2020-2029
    • Jiang, S.1    Wright, I.2    Swartz, P.3    Franzen, S.4
  • 48
    • 80053039198 scopus 로고    scopus 로고
    • Amphitrite ornata Dehaloperoxidase (DHP): Investigations of Structural Factors That Influence the Mechanism of Halophenol Dehalogenation Using "peroxidase-like" Myoglobin Mutants and "myoglobin-like" DHP Mutants
    • Du, J., Huang, X., Sun, S. F., Wang, C. X., Lebioda, L., and Dawson, J. H. (2011) Amphitrite ornata Dehaloperoxidase (DHP): Investigations of Structural Factors That Influence the Mechanism of Halophenol Dehalogenation Using "Peroxidase-like" Myoglobin Mutants and "Myoglobin-like" DHP Mutants Biochemistry 50, 8172-8180
    • (2011) Biochemistry , vol.50 , pp. 8172-8180
    • Du, J.1    Huang, X.2    Sun, S.F.3    Wang, C.X.4    Lebioda, L.5    Dawson, J.H.6
  • 49
    • 0035110522 scopus 로고    scopus 로고
    • Is the CO adduct of myoglobin bent, and does it matter?
    • Spiro, T. G. and Kozlowski, P. M. (2001) Is the CO adduct of myoglobin bent, and does it matter? Acc. Chem. Res. 34, 137-144
    • (2001) Acc. Chem. Res. , vol.34 , pp. 137-144
    • Spiro, T.G.1    Kozlowski, P.M.2
  • 50
    • 0028086944 scopus 로고
    • Determinatino of CO Orientation in Myoglobin by Single-crystal Linear Dichroism
    • Ivanov, D., Sage, J. T., Keim, M., Powell, J. R., Asher, S. A., and Champion, P. M. (1994) Determinatino of CO Orientation in Myoglobin by Single-crystal Linear Dichroism J. Am. Chem. Soc. 116, 4139-4140
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 4139-4140
    • Ivanov, D.1    Sage, J.T.2    Keim, M.3    Powell, J.R.4    Asher, S.A.5    Champion, P.M.6
  • 51
    • 0030773396 scopus 로고    scopus 로고
    • Myoglobin discriminates between O-2, NO, and CO by electrostatic interactions with the bound ligand
    • Olson, J. S. and Phillips, G. N. (1997) Myoglobin discriminates between O-2, NO, and CO by electrostatic interactions with the bound ligand J. Biol. Inorg. Chem. 2, 544-552
    • (1997) J. Biol. Inorg. Chem. , vol.2 , pp. 544-552
    • Olson, J.S.1    Phillips, G.N.2
  • 53
    • 0019827532 scopus 로고
    • Neutron Diffraction Reveals Oxygen-Histidine Hydrogen Bond in Oxymyoglobin
    • Phillips, S. E. V. and Schoenborn, B. P. (1981) Neutron Diffraction Reveals Oxygen-Histidine Hydrogen Bond in Oxymyoglobin Nature 292, 81-82
    • (1981) Nature , vol.292 , pp. 81-82
    • Phillips, S.E.V.1    Schoenborn, B.P.2
  • 54
    • 0030827765 scopus 로고    scopus 로고
    • Myoglobin models and steric origins of the discrimination between O-2 and CO
    • Slebodnick, C. and Ibers, J. A. (1997) Myoglobin models and steric origins of the discrimination between O-2 and CO J. Bioinorg. Chem. 2, 521-525
    • (1997) J. Bioinorg. Chem. , vol.2 , pp. 521-525
    • Slebodnick, C.1    Ibers, J.A.2
  • 55
    • 0035023569 scopus 로고    scopus 로고
    • How the CO in myoglobin acquired its bend: Lessons in interpretation of crystallographic data
    • Stec, B. and Phillips, G. N. (2001) How the CO in myoglobin acquired its bend: lessons in interpretation of crystallographic data Acta Crystallogr., Sect. D: Biol. Crystal 57, 751-754
    • (2001) Acta Crystallogr., Sect. D: Biol. Crystal , vol.57 , pp. 751-754
    • Stec, B.1    Phillips, G.N.2
  • 56
    • 0037032263 scopus 로고    scopus 로고
    • An Electrostatic Model for the Frequency Shifts in the Carbonmonoxy Stretching Band of Myoglobin: Correlation of Hydrogen Bonding and the Stark Tuning Rate
    • Franzen, S. (2002) An Electrostatic Model for the Frequency Shifts in the Carbonmonoxy Stretching Band of Myoglobin: Correlation of Hydrogen Bonding and the Stark Tuning Rate J. Am. Chem. Soc. 124, 13271-13281
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 13271-13281
    • Franzen, S.1
  • 57
    • 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. (1999) Determinants of the FeXO (X = C, N, O) vibrational frequencies in heme adducts from experiment and density functional theory J. Am. Chem. Soc. 121, 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
  • 58
    • 0033806397 scopus 로고    scopus 로고
    • Role of the axial ligand in heme-CO backbonding; DFT analysis of vibrational data
    • Vogel, K. M., Kozlowski, P. M., Zgierski, M. Z., and Spiro, T. G. (2000) Role of the axial ligand in heme-CO backbonding; DFT analysis of vibrational data Inorg. Chim. Acta 297, 11-17
    • (2000) Inorg. Chim. Acta , vol.297 , pp. 11-17
    • Vogel, K.M.1    Kozlowski, P.M.2    Zgierski, M.Z.3    Spiro, T.G.4
  • 59
    • 84880770397 scopus 로고    scopus 로고
    • Effects of local protein environment on the binding of diatomic molecules to heme in myoglobins. DFT and dispersion-corrected DFT studies
    • Liao, M. S., Huang, M. J., and Watts, J. D. (2013) Effects of local protein environment on the binding of diatomic molecules to heme in myoglobins. DFT and dispersion-corrected DFT studies J. Mol. Model. 19, 3307-3323
    • (2013) J. Mol. Model. , vol.19 , pp. 3307-3323
    • Liao, M.S.1    Huang, M.J.2    Watts, J.D.3
  • 60
    • 33747202720 scopus 로고    scopus 로고
    • A DFT study on the relative affinity for oxygen of the alpha and beta subunits of hemoglobin
    • Marechal, J. D., Maseras, F., Lledos, A., Mouawad, L., and Perahia, D. (2006) A DFT study on the relative affinity for oxygen of the alpha and beta subunits of hemoglobin J. Comput. Chem. 27, 1446-1453
    • (2006) J. Comput. Chem. , vol.27 , pp. 1446-1453
    • Marechal, J.D.1    Maseras, F.2    Lledos, A.3    Mouawad, L.4    Perahia, D.5
  • 61
    • 39749136203 scopus 로고    scopus 로고
    • DFT analysis of axial and equatorial effects on Heme-CO vibrational modes: Applications to CooA and H-NOX heme sensor proteins
    • Xu, C. L., Ibrahim, M., and Spiro, T. G. (2008) DFT analysis of axial and equatorial effects on Heme-CO vibrational modes: Applications to CooA and H-NOX heme sensor proteins Biochemistry 47, 2379-2387
    • (2008) Biochemistry , vol.47 , pp. 2379-2387
    • Xu, C.L.1    Ibrahim, M.2    Spiro, T.G.3
  • 62
    • 0035107645 scopus 로고    scopus 로고
    • Steric contributions to CO binding in heme proteins: A density functional analysis of FeCO vibrations and deformability
    • Kozlowski, P. M., Vogel, K. M., Zgierski, M. Z., and Spiro, T. G. (2001) Steric contributions to CO binding in heme proteins: a density functional analysis of FeCO vibrations and deformability J. Porphyrins Phthalocyanines 5, 312-322
    • (2001) J. Porphyrins Phthalocyanines , vol.5 , pp. 312-322
    • Kozlowski, P.M.1    Vogel, K.M.2    Zgierski, M.Z.3    Spiro, T.G.4
  • 63
    • 14644398597 scopus 로고    scopus 로고
    • Quantum chemical evaluation of protein control over heme ligation: CO/O-2 discrimination in myoglobin
    • De Angelis, F., Jarzecki, A. A., Car, R., and Spiro, T. G. (2005) Quantum chemical evaluation of protein control over heme ligation: CO/O-2 discrimination in myoglobin J. Phys. Chem. B 109, 3065-3070
    • (2005) J. Phys. Chem. B , vol.109 , pp. 3065-3070
    • De Angelis, F.1    Jarzecki, A.A.2    Car, R.3    Spiro, T.G.4
  • 65
    • 0031059866 scopus 로고    scopus 로고
    • Processing of x-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. and Minor, W. (1997) Processing of x-ray diffraction data collected in oscillation mode Methods Enzymol. 276, 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 69
    • 34447260582 scopus 로고
    • An all-electron numerical method for solving the local density functional for polyatomic molecules
    • Delley, B. (1990) An all-electron numerical method for solving the local density functional for polyatomic molecules J. Chem. Phys. 92, 508-517
    • (1990) J. Chem. Phys. , vol.92 , pp. 508-517
    • Delley, B.1
  • 70
    • 0034319689 scopus 로고    scopus 로고
    • From molecules to solids with the DMol3 approach
    • Delley, B. (2000) From molecules to solids with the DMol3 approach J. Chem. Phys. 113, 7756-7764
    • (2000) J. Chem. Phys. , vol.113 , pp. 7756-7764
    • Delley, B.1
  • 71
    • 2842565972 scopus 로고    scopus 로고
    • Generalized gradient approximation for the exchange-correlation hole of a many-electron system
    • Perdew, J. P., Burke, K., and Wang, Y. (1996) Generalized gradient approximation for the exchange-correlation hole of a many-electron system Phys. Rev. B: Condens. Matter 54, 16533-16539
    • (1996) Phys. Rev. B: Condens. Matter , vol.54 , pp. 16533-16539
    • Perdew, J.P.1    Burke, K.2    Wang, Y.3
  • 72
    • 36049046910 scopus 로고
    • Thermal properties of a homogeneous electron gas
    • Mermin, N. D. (1965) Thermal properties of a homogeneous electron gas Phys. Rev. A 137, 1441-1443
    • (1965) Phys. Rev. A , vol.137 , pp. 1441-1443
    • Mermin, N.D.1
  • 76
    • 0023042853 scopus 로고
    • X-ray Structure and Refinement of Carbon Monoxy (Fe-II)-Myoglobin at 1.5 Å Resolution
    • Kuriyan, J., Wilz, S., Karplus, M., and Petsko, G. A. (1986) X-ray Structure and Refinement of Carbon Monoxy (Fe-II)-Myoglobin at 1.5 Å Resolution J. Mol. Biol. 192, 133-154
    • (1986) J. Mol. Biol. , vol.192 , pp. 133-154
    • Kuriyan, J.1    Wilz, S.2    Karplus, M.3    Petsko, G.A.4
  • 78
    • 39549115043 scopus 로고    scopus 로고
    • Substrate Binding Triggers a Switch in the Iron Coordination in Dehaloperoxidase from Amphitrite ornata: HYSCORE Experiments
    • Smirnova, T. I., Weber, R. T., Davis, M. F., and Franzen, S. (2008) Substrate Binding Triggers a Switch in the Iron Coordination in Dehaloperoxidase from Amphitrite ornata: HYSCORE Experiments J. Am. Chem. Soc. 130, 2128-2129
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 2128-2129
    • Smirnova, T.I.1    Weber, R.T.2    Davis, M.F.3    Franzen, S.4
  • 79
    • 0034705539 scopus 로고    scopus 로고
    • The crystal structure and amino acid sequence of dehaloperoxidase from Amphitrite ornata indicate common ancestry with globins
    • LaCount, M. W., Zhang, E., Chen, Y. P., Han, K., Whitton, M. M., Lincoln, D. E., Woodin, S. A., and Lebioda, L. (2000) The crystal structure and amino acid sequence of dehaloperoxidase from Amphitrite ornata indicate common ancestry with globins J. Biol. Chem. 275, 18712-18716
    • (2000) J. Biol. Chem. , vol.275 , pp. 18712-18716
    • Lacount, M.W.1    Zhang, E.2    Chen, Y.P.3    Han, K.4    Whitton, M.M.5    Lincoln, D.E.6    Woodin, S.A.7    Lebioda, L.8
  • 80
    • 0019888621 scopus 로고
    • Real Space Refinement of Neutron Diffraction Data from Sperm Whale Carbonmonoxy Myoglobin
    • Hanson, J. C. and Schoenborn, B. P. (1981) Real Space Refinement of Neutron Diffraction Data from Sperm Whale Carbonmonoxy Myoglobin J. Mol. Biol. 153, 117-146
    • (1981) J. Mol. Biol. , vol.153 , pp. 117-146
    • Hanson, J.C.1    Schoenborn, B.P.2
  • 82
    • 84875793959 scopus 로고    scopus 로고
    • Structural Evidence for Stabilization of Inhibitor Binding by a Protein Cavity in the Dehaloperoxidase-Hemoglobin from Amphitrite ornata
    • De Serrano, V. and Franzen, S. (2012) Structural Evidence for Stabilization of Inhibitor Binding by a Protein Cavity in the Dehaloperoxidase-Hemoglobin from Amphitrite ornata Peptide Sci. 98, 27-35
    • (2012) Peptide Sci. , vol.98 , pp. 27-35
    • De Serrano, V.1    Franzen, S.2
  • 85
    • 70350705724 scopus 로고    scopus 로고
    • Ligand Migration and Cavities within Scapharca Dimeric Hbl: Studies by Time-Resolved Crystallography, Xe Binding, and Computational Analysis
    • Knapp, J. E., Pahl, R., Cohen, J., Nichols, J. C., Schulten, K., Gibson, Q. H., Srajer, V., and Royer, W. E. (2009) Ligand Migration and Cavities within Scapharca Dimeric Hbl: Studies by Time-Resolved Crystallography, Xe Binding, and Computational Analysis Structure 17, 1494-1504
    • (2009) Structure , vol.17 , pp. 1494-1504
    • Knapp, J.E.1    Pahl, R.2    Cohen, J.3    Nichols, J.C.4    Schulten, K.5    Gibson, Q.H.6    Srajer, V.7    Royer, W.E.8
  • 86
    • 33646755415 scopus 로고    scopus 로고
    • Allosteric action in real time: Time-resolved crystallographic studies of a cooperative dimeric hemoglobin
    • Knapp, J. E., Pahl, R., Srajer, V., and Royer, W. E. (2006) Allosteric action in real time: Time-resolved crystallographic studies of a cooperative dimeric hemoglobin Proc. Natl. Acad. Sci. U. S. A. 103, 7649-7654
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 7649-7654
    • Knapp, J.E.1    Pahl, R.2    Srajer, V.3    Royer, W.E.4


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