메뉴 건너뛰기




Volumn 48, Issue 48, 2009, Pages 11412-11420

Kinetic characterization of xenobiotic reductase A from Pseudomonas putida 86

Author keywords

[No Author keywords available]

Indexed keywords

BINDING AFFINITIES; CONCENTRATION-DEPENDENT; ELECTROSTATIC ENERGIES; KINETIC CHARACTERIZATION; PHOSPHATE GROUP; PSEUDOMONAS PUTIDA; SECOND-ORDER RATE CONSTANTS; THERMO DYNAMIC ANALYSIS; VARIOUS SUBSTRATES;

EID: 73149096726     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi901370u     Document Type: Article
Times cited : (16)

References (48)
  • 1
    • 0029878360 scopus 로고    scopus 로고
    • Degradation of pentaerythritol tetranitrate by Enterobacter cloacae PB2
    • Binks, P. R., French, C. E., Nicklin, S., and Bruce, N. C. (1996) Degradation of pentaerythritol tetranitrate by Enterobacter cloacae PB2. Appl. Environ. Microbiol. 62, 1214-1219.
    • (1996) Appl. Environ. Microbiol , vol.62 , pp. 1214-1219
    • Binks, P.R.1    French, C.E.2    Nicklin, S.3    Bruce, N.C.4
  • 2
    • 0038820069 scopus 로고    scopus 로고
    • Characterization of YqjM, an Old Yellow Enzyme homolog from Bacillus subtilis involved in the oxidative stress response
    • Fitzpatrick, T. B., Amrhein, N., and Macheroux, P. (2003) Characterization of YqjM, an Old Yellow Enzyme homolog from Bacillus subtilis involved in the oxidative stress response. J. Biol. Chem. 278, 19891-19897.
    • (2003) J. Biol. Chem , vol.278 , pp. 19891-19897
    • Fitzpatrick, T.B.1    Amrhein, N.2    Macheroux, P.3
  • 3
    • 0030731165 scopus 로고    scopus 로고
    • Regioselectivity of nitroglycerin denitration by flavoprotein nitroester reductases purified from two Pseudomonas species
    • Blehert, D. S., Knoke, K. L., Fox, B. G., and Chambliss, G. H. (1997) Regioselectivity of nitroglycerin denitration by flavoprotein nitroester reductases purified from two Pseudomonas species. J. Bacteriol. 179, 6912-6920.
    • (1997) J. Bacteriol , vol.179 , pp. 6912-6920
    • Blehert, D.S.1    Knoke, K.L.2    Fox, B.G.3    Chambliss, G.H.4
  • 4
    • 0030867134 scopus 로고    scopus 로고
    • Purification, properties, and sequence of glycerol trinitrate reductase from Agrobacterium radiobacter
    • Snape, J. R., Walkley, N. A., Morby, A. P., Nicklin, S., and White, G. F. (1997) Purification, properties, and sequence of glycerol trinitrate reductase from Agrobacterium radiobacter. J. Bacteriol. 179, 7796-7802.
    • (1997) J. Bacteriol , vol.179 , pp. 7796-7802
    • Snape, J.R.1    Walkley, N.A.2    Morby, A.P.3    Nicklin, S.4    White, G.F.5
  • 5
    • 0031021921 scopus 로고    scopus 로고
    • Molecular cloning of the nemA gene encoding N-ethylmaleimide reductase from Escherichia coli
    • Miura, K., Tomioka, Y., Suzuki, H., Yonezawa, M., Hishinuma, T., and Mizugaki, M. (1997) Molecular cloning of the nemA gene encoding N-ethylmaleimide reductase from Escherichia coli. Biol. Pharm. Bull. 20, 110-112.
    • (1997) Biol. Pharm. Bull , vol.20 , pp. 110-112
    • Miura, K.1    Tomioka, Y.2    Suzuki, H.3    Yonezawa, M.4    Hishinuma, T.5    Mizugaki, M.6
  • 6
    • 0028200297 scopus 로고
    • Purification and characterization of morphinone reductase from Pseudomonas putida M10
    • French, C. E., and Bruce, N. C. (1994) Purification and characterization of morphinone reductase from Pseudomonas putida M10. Biochem. J. 301 (Part 1), 97-103.
    • (1994) Biochem. J , vol.301 , Issue.PART 1 , pp. 97-103
    • French, C.E.1    Bruce, N.C.2
  • 7
    • 0032891449 scopus 로고    scopus 로고
    • Thermoregulated expression and characterization of an NAD(P)H-dependent 2-cyclohexen-1-one reductase in the plant pathogenic bacterium
    • Rohde, B. H., Schmid, R., and Ullrich, M. S. (1999) Thermoregulated expression and characterization of an NAD(P)H-dependent 2-cyclohexen-1-one reductase in the plant pathogenic bacterium Pseudomonas syringae pv. glycinea. J. Bacteriol. 181, 814-822.
    • (1999) Pseudomonas syringae pv. glycinea. J. Bacteriol , vol.181 , pp. 814-822
    • Rohde, B.H.1    Schmid, R.2    Ullrich, M.S.3
  • 8
    • 0032738032 scopus 로고    scopus 로고
    • Cloning and sequence analysis of two Pseudomonas flavoprotein xenobiotic reductases
    • Blehert, D. S., Fox, B. G., and Chambliss, G. H. (1999) Cloning and sequence analysis of two Pseudomonas flavoprotein xenobiotic reductases. J. Bacteriol. 181, 6254-6263.
    • (1999) J. Bacteriol , vol.181 , pp. 6254-6263
    • Blehert, D.S.1    Fox, B.G.2    Chambliss, G.H.3
  • 9
    • 0031949286 scopus 로고    scopus 로고
    • Bacterial degradation of quinoline and derivatives: Pathways and their biocatalysts
    • Fetzner, S., Tshisuaka, B., Lingens, F., Kappl, R., and Hüttermann, J. (1998) Bacterial degradation of quinoline and derivatives: Pathways and their biocatalysts. Angew. Chem., Int. Ed. 37, 577-597.
    • (1998) Angew. Chem., Int. Ed , vol.37 , pp. 577-597
    • Fetzner, S.1    Tshisuaka, B.2    Lingens, F.3    Kappl, R.4    Hüttermann, J.5
  • 10
    • 33745879474 scopus 로고    scopus 로고
    • Xenobiotic reductase A in the degradation of quinoline by Pseudomonas putida 86: Physiological function, structure and mechanism of 8-hydroxycoumarin reduction
    • Griese, J. J., Jakob, R. P., Schwarzinger, S., and Dobbek, H. (2006) Xenobiotic reductase A in the degradation of quinoline by Pseudomonas putida 86: Physiological function, structure and mechanism of 8-hydroxycoumarin reduction. J. Mol. Biol. 361, 140-152.
    • (2006) J. Mol. Biol , vol.361 , pp. 140-152
    • Griese, J.J.1    Jakob, R.P.2    Schwarzinger, S.3    Dobbek, H.4
  • 11
    • 23044455760 scopus 로고    scopus 로고
    • The 1.3 Å crystal structure of the flavoprotein YqjM reveals a novel class of Old Yellow Enzymes
    • Kitzing, K., Fitzpatrick, T. B., Wilken, C., Sawa, J., Bourenkov, G. P., Macheroux, P., and Clausen, T. (2005) The 1.3 Å crystal structure of the flavoprotein YqjM reveals a novel class of Old Yellow Enzymes. J. Biol. Chem. 280, 27904-27913.
    • (2005) J. Biol. Chem , vol.280 , pp. 27904-27913
    • Kitzing, K.1    Fitzpatrick, T.B.2    Wilken, C.3    Sawa, J.4    Bourenkov, G.P.5    Macheroux, P.6    Clausen, T.7
  • 12
    • 0028963408 scopus 로고
    • A new old yellow enzyme of Saccharomyces cerevisiae
    • Niino, Y. S., Chakraborty, S., Brown, B. J., and Massey, V. (1995) A new old yellow enzyme of Saccharomyces cerevisiae. J. Biol. Chem. 270, 1983-1991.
    • (1995) J. Biol. Chem , vol.270 , pp. 1983-1991
    • Niino, Y.S.1    Chakraborty, S.2    Brown, B.J.3    Massey, V.4
  • 13
    • 32944459987 scopus 로고    scopus 로고
    • Comparative characterization and expression analysis of the four Old Yellow Enzyme homologues from Shewanella oneidensis indicate differences in physiological function
    • Brige, A., Van den Hemel, D., Carpentier, W., De Smet, L., and Van Beeumen, J. J. (2006) Comparative characterization and expression analysis of the four Old Yellow Enzyme homologues from Shewanella oneidensis indicate differences in physiological function. Biochem. J. 394, 335-344.
    • (2006) Biochem. J , vol.394 , pp. 335-344
    • Brige, A.1    Van den Hemel, D.2    Carpentier, W.3    De Smet, L.4    Van Beeumen, J.J.5
  • 14
    • 55049133449 scopus 로고    scopus 로고
    • Subfunctionality of Hydride Transferases of the Old Yellow Enzyme Family of Flavoproteins of Pseudomonas putida
    • van Dillewijn, P., Wittich, R. M., Caballero, A., and Ramos, J. L. (2008) Subfunctionality of Hydride Transferases of the Old Yellow Enzyme Family of Flavoproteins of Pseudomonas putida. Appl. Environ. Microbiol. 74, 6703-6708.
    • (2008) Appl. Environ. Microbiol , vol.74 , pp. 6703-6708
    • van Dillewijn, P.1    Wittich, R.M.2    Caballero, A.3    Ramos, J.L.4
  • 15
    • 0035987236 scopus 로고    scopus 로고
    • New uses for an Old Enzyme': The Old Yellow Enzyme family of flavoenzymes
    • Williams, R. E., and Bruce, N. C. (2002) 'New uses for an Old Enzyme': The Old Yellow Enzyme family of flavoenzymes. Microbiology 148, 1607-1614.
    • (2002) Microbiology , vol.148 , pp. 1607-1614
    • Williams, R.E.1    Bruce, N.C.2
  • 16
    • 0017148370 scopus 로고
    • Interaction of phenols with old yellow enzyme. Physical evidence for charge-transfer complexes
    • Abramovitz, A. S., and Massey, V. (1976) Interaction of phenols with old yellow enzyme. Physical evidence for charge-transfer complexes. J. Biol. Chem. 251, 5327-5336.
    • (1976) J. Biol. Chem , vol.251 , pp. 5327-5336
    • Abramovitz, A.S.1    Massey, V.2
  • 17
    • 0028774535 scopus 로고
    • Old yellow enzyme at 2 Å resolution: Overall structure, ligand binding, and comparison with related flavoproteins
    • Fox, K. M., and Karplus, P. A. (1994) Old yellow enzyme at 2 Å resolution: Overall structure, ligand binding, and comparison with related flavoproteins. Structure 2, 1089-1105.
    • (1994) Structure , vol.2 , pp. 1089-1105
    • Fox, K.M.1    Karplus, P.A.2
  • 18
    • 0029557273 scopus 로고
    • Flavoprotein structure and mechanism. 8. Structure-function relations for old yellow enzyme
    • Karplus, P. A., Fox, K. M., and Massey, V. (1995) Flavoprotein structure and mechanism. 8. Structure-function relations for old yellow enzyme. FASEB J. 9, 1518-1526.
    • (1995) FASEB J , vol.9 , pp. 1518-1526
    • Karplus, P.A.1    Fox, K.M.2    Massey, V.3
  • 19
    • 0032483986 scopus 로고    scopus 로고
    • The oxidative half-reaction of Old Yellow Enzyme. The role of tyrosine 196
    • Kohli, R. M., and Massey, V. (1998) The oxidative half-reaction of Old Yellow Enzyme. The role of tyrosine 196. J. Biol. Chem. 273, 32763-32770.
    • (1998) J. Biol. Chem , vol.273 , pp. 32763-32770
    • Kohli, R.M.1    Massey, V.2
  • 20
    • 0032484145 scopus 로고    scopus 로고
    • On the active site of Old Yellow Enzyme. Role of histidine 191 and asparagine 194
    • Brown, B. J., Deng, Z., Karplus, P. A., and Massey, V. (1998) On the active site of Old Yellow Enzyme. Role of histidine 191 and asparagine 194. J. Biol. Chem. 273, 32753-32762.
    • (1998) J. Biol. Chem , vol.273 , pp. 32753-32762
    • Brown, B.J.1    Deng, Z.2    Karplus, P.A.3    Massey, V.4
  • 21
    • 0033616677 scopus 로고    scopus 로고
    • The role of threonine 37 in flavin reactivity of the old yellow enzyme
    • Xu, D., Kohli, R. M., and Massey, V. (1999) The role of threonine 37 in flavin reactivity of the old yellow enzyme. Proc. Natl. Acad. Sci. U. S.A. 96, 3556-3561.
    • (1999) Proc. Natl. Acad. Sci. U. S.A , vol.96 , pp. 3556-3561
    • Xu, D.1    Kohli, R.M.2    Massey, V.3
  • 22
    • 0033515586 scopus 로고    scopus 로고
    • The flavin environment in old yellow enzyme. An evaluation of insights from spectroscopic and artificial flavin studies
    • Fox, K. M., and Karplus, P. A. (1999) The flavin environment in old yellow enzyme. An evaluation of insights from spectroscopic and artificial flavin studies. J. Biol. Chem. 274, 9357-9362.
    • (1999) J. Biol. Chem , vol.274 , pp. 9357-9362
    • Fox, K.M.1    Karplus, P.A.2
  • 24
    • 0032546529 scopus 로고    scopus 로고
    • Reductive and oxidative half-reactions of morphinone reductase from Pseudomonas putida M10: A kinetic and thermodynamic analysis
    • Craig, D. H., Moody, P. C., Bruce, N. C., and Scrutton, N. S. (1998) Reductive and oxidative half-reactions of morphinone reductase from Pseudomonas putida M10: A kinetic and thermodynamic analysis. Biochemistry 37, 7598-7607.
    • (1998) Biochemistry , vol.37 , pp. 7598-7607
    • Craig, D.H.1    Moody, P.C.2    Bruce, N.C.3    Scrutton, N.S.4
  • 25
    • 0037163054 scopus 로고    scopus 로고
    • Crystal structure of bacterial morphinone reductase and properties of the C191A mutant enzyme
    • Barna, T., Messiha, H. L., Petosa, C., Bruce, N. C., Scrutton, N. S., and Moody, P. C. (2002) Crystal structure of bacterial morphinone reductase and properties of the C191A mutant enzyme. J. Biol. Chem. 277, 30976-30983.
    • (2002) J. Biol. Chem , vol.277 , pp. 30976-30983
    • Barna, T.1    Messiha, H.L.2    Petosa, C.3    Bruce, N.C.4    Scrutton, N.S.5    Moody, P.C.6
  • 26
    • 22844450431 scopus 로고    scopus 로고
    • Role of active site residues and solvent in proton transfer and the modulation of flavin reduction potential in bacterial morphinone reductase
    • Messiha, H. L., Bruce, N. C., Sattelle, B. M., Sutcliffe, M. J., Munro, A. W., and Scrutton, N. S. (2005) Role of active site residues and solvent in proton transfer and the modulation of flavin reduction potential in bacterial morphinone reductase. J. Biol. Chem. 280, 27103-27110.
    • (2005) J. Biol. Chem , vol.280 , pp. 27103-27110
    • Messiha, H.L.1    Bruce, N.C.2    Sattelle, B.M.3    Sutcliffe, M.J.4    Munro, A.W.5    Scrutton, N.S.6
  • 27
    • 36148973895 scopus 로고    scopus 로고
    • Mutagenesis of morphinone reductase induces multiple reactive configurations and identifies potential ambiguity in kinetic analysis of enzyme tunneling mechanisms
    • Pudney, C. R., Hay, S., Pang, J., Costello, C., Leys, D., Sutcliffe, M. J., and Scrutton, N. S. (2007) Mutagenesis of morphinone reductase induces multiple reactive configurations and identifies potential ambiguity in kinetic analysis of enzyme tunneling mechanisms. J. Am. Chem. Soc. 129, 13949-13956.
    • (2007) J. Am. Chem. Soc , vol.129 , pp. 13949-13956
    • Pudney, C.R.1    Hay, S.2    Pang, J.3    Costello, C.4    Leys, D.5    Sutcliffe, M.J.6    Scrutton, N.S.7
  • 28
    • 0035816226 scopus 로고    scopus 로고
    • Crystal structure of pentaerythritol tetranitrate reductase: "Flipped" binding geometries for steroid substrates in different redox states of the enzyme
    • Barna, T. M., Khan, H., Bruce, N. C., Barsukov, I., Scrutton, N. S., and Moody, P. C. (2001) Crystal structure of pentaerythritol tetranitrate reductase: "Flipped" binding geometries for steroid substrates in different redox states of the enzyme. J. Mol. Biol. 310, 433-447.
    • (2001) J. Mol. Biol , vol.310 , pp. 433-447
    • Barna, T.M.1    Khan, H.2    Bruce, N.C.3    Barsukov, I.4    Scrutton, N.S.5    Moody, P.C.6
  • 29
    • 0037077313 scopus 로고    scopus 로고
    • Kinetic and structural basis of reactivity of pentaerythritol tetranitrate reductase with NADPH, 2-cyclohexenone, nitroesters, and nitroaromatic explosives
    • Khan, H., Harris, R. J., Barna, T., Craig, D. H., Bruce, N. C., Munro, A. W., Moody, P. C., and Scrutton, N. S. (2002) Kinetic and structural basis of reactivity of pentaerythritol tetranitrate reductase with NADPH, 2-cyclohexenone, nitroesters, and nitroaromatic explosives. J. Biol. Chem. 277, 21906-21912.
    • (2002) J. Biol. Chem , vol.277 , pp. 21906-21912
    • Khan, H.1    Harris, R.J.2    Barna, T.3    Craig, D.H.4    Bruce, N.C.5    Munro, A.W.6    Moody, P.C.7    Scrutton, N.S.8
  • 30
    • 3142695539 scopus 로고    scopus 로고
    • Atomic resolution structures and solution behavior of enzyme-substrate complexes of Enterobacter cloacae PB2 pentaerythritol tetranitrate reductase. Multiple conformational states and implications for the mechanism of nitroaromatic explosive degradation
    • Khan, H., Barna, T., Harris, R. J., Bruce, N. C., Barsukov, I., Munro, A. W., Moody, P. C., and Scrutton, N. S. (2004) Atomic resolution structures and solution behavior of enzyme-substrate complexes of Enterobacter cloacae PB2 pentaerythritol tetranitrate reductase. Multiple conformational states and implications for the mechanism of nitroaromatic explosive degradation. J. Biol. Chem. 279, 30563-30572.
    • (2004) J. Biol. Chem , vol.279 , pp. 30563-30572
    • Khan, H.1    Barna, T.2    Harris, R.J.3    Bruce, N.C.4    Barsukov, I.5    Munro, A.W.6    Moody, P.C.7    Scrutton, N.S.8
  • 31
    • 25444502896 scopus 로고    scopus 로고
    • Proton transfer in the oxidative half-reaction of pentaerythritol tetranitrate reductase. Structure of the reduced enzyme-progesterone complex and the roles of residues Tyr186, His181, His184
    • Khan, H., Barna, T., Bruce, N. C., Munro, A. W., Leys, D., and Scrutton, N. S. (2005) Proton transfer in the oxidative half-reaction of pentaerythritol tetranitrate reductase. Structure of the reduced enzyme-progesterone complex and the roles of residues Tyr186, His181, His184. FEBS J. 272, 4660-4671.
    • (2005) FEBS J , vol.272 , pp. 4660-4671
    • Khan, H.1    Barna, T.2    Bruce, N.C.3    Munro, A.W.4    Leys, D.5    Scrutton, N.S.6
  • 33
    • 0034980393 scopus 로고    scopus 로고
    • X-ray structure of 12-oxophytodienoate reductase 1 provides structural insight into substrate binding and specificity within the family of OYE
    • Breithaupt, C., Strassner, J., Breitinger, U., Huber, R., Macheroux, P., Schaller, A., and Clausen, T. (2001) X-ray structure of 12-oxophytodienoate reductase 1 provides structural insight into substrate binding and specificity within the family of OYE. Structure 9, 419-429.
    • (2001) Structure , vol.9 , pp. 419-429
    • Breithaupt, C.1    Strassner, J.2    Breitinger, U.3    Huber, R.4    Macheroux, P.5    Schaller, A.6    Clausen, T.7
  • 34
  • 36
    • 0032612239 scopus 로고    scopus 로고
    • Identifying and quantitating FAD and FMN in simple and in iron-sulfur-containing flavoproteins
    • Aliverti, A., Curti, B., and Vanoni, M. A. (1999) Identifying and quantitating FAD and FMN in simple and in iron-sulfur-containing flavoproteins. Methods Mol. Biol. 131, 9-23.
    • (1999) Methods Mol. Biol , vol.131 , pp. 9-23
    • Aliverti, A.1    Curti, B.2    Vanoni, M.A.3
  • 37
    • 0017855692 scopus 로고
    • Light-mediated reduction of flavoproteins with flavins as catalysts
    • Massey, V., Stankovich, M., and Hemmerich, P. (1978) Light-mediated reduction of flavoproteins with flavins as catalysts. Biochemistry 17, 1-8.
    • (1978) Biochemistry , vol.17 , pp. 1-8
    • Massey, V.1    Stankovich, M.2    Hemmerich, P.3
  • 38
    • 23044506644 scopus 로고    scopus 로고
    • The reductase of p-hydroxyphenylacetate 3-hydroxylase from Acinetobacter baumannii requires p-hydroxyphenylacetate for effective catalysis
    • Sucharitakul, J., Chaiyen, P., Entsch, B., and Ballou, D. P. (2005) The reductase of p-hydroxyphenylacetate 3-hydroxylase from Acinetobacter baumannii requires p-hydroxyphenylacetate for effective catalysis. Biochemistry 44, 10434-10442.
    • (2005) Biochemistry , vol.44 , pp. 10434-10442
    • Sucharitakul, J.1    Chaiyen, P.2    Entsch, B.3    Ballou, D.P.4
  • 39
    • 0004204454 scopus 로고
    • Oxidation-reduction potentials: Absorbance bands and molar absorbance of compounds used in biochemical studies
    • Sorber, H. A, Ed, pp, CRC Press, Cleveland, OH
    • Loach, P. A. (1973) Oxidation-reduction potentials: Absorbance bands and molar absorbance of compounds used in biochemical studies. In Handbook of Biochemistry Selected Data for Molecular Biology (Sorber, H. A., Ed.) pp J33-J40, CRC Press, Cleveland, OH.
    • (1973) Handbook of Biochemistry Selected Data for Molecular Biology
    • Loach, P.A.1
  • 40
    • 0003518480 scopus 로고
    • John Wiley and Sons, New York
    • Segel, I. H. (1993) Enzyme Kinetics , John Wiley and Sons, New York.
    • (1993) Enzyme Kinetics
    • Segel, I.H.1
  • 41
    • 0016749447 scopus 로고
    • Determination of dissociation constants and specific rate constants of enzyme-substrate (or protein-ligand) interactions from rapid reaction kinetic data
    • Strickland, S., Palmer, G., and Massey, V. (1975) Determination of dissociation constants and specific rate constants of enzyme-substrate (or protein-ligand) interactions from rapid reaction kinetic data. J. Biol. Chem. 250, 4048-4052.
    • (1975) J. Biol. Chem , vol.250 , pp. 4048-4052
    • Strickland, S.1    Palmer, G.2    Massey, V.3
  • 43
    • 0242593434 scopus 로고    scopus 로고
    • Development and current status of the CHARMM force field for nucleic acids
    • MacKerell, A. D.Jr., Banavali, N., and Foloppe, N. (2000) Development and current status of the CHARMM force field for nucleic acids. Biopolymers 56, 257-265.
    • (2000) Biopolymers , vol.56 , pp. 257-265
    • MacKerell Jr., A.D.1    Banavali, N.2    Foloppe, N.3
  • 44
    • 67650500988 scopus 로고    scopus 로고
    • Brooks, B. R., Brooks, C. L.III, Mackerell, A. D.Jr., Nilsson, L., Petrella, R. J., Roux, B., Won, Y., Archontis, G., Bartels, C., Boresch, S., Caflisch, A., Caves, L., Cui, Q., Dinner, A. R., Feig, M., Fischer, S., Gao, J., Hodoscek, M., Im, W., Kuczera, K., Lazaridis, T., Ma, J., Ovchinnikov, V., Paci, E., Pastor, R. W., Post, C. B., Pu, J. Z., Schaefer, M., Tidor, B., Venable, R. M., Woodcock, H. L., Wu, X., Yang, W., York, D. M., and Karplus, M. (2009) CHARMM: The biomolecular simulation program. J. Comput. Chem. 30, 1545-1614.
    • Brooks, B. R., Brooks, C. L.III, Mackerell, A. D.Jr., Nilsson, L., Petrella, R. J., Roux, B., Won, Y., Archontis, G., Bartels, C., Boresch, S., Caflisch, A., Caves, L., Cui, Q., Dinner, A. R., Feig, M., Fischer, S., Gao, J., Hodoscek, M., Im, W., Kuczera, K., Lazaridis, T., Ma, J., Ovchinnikov, V., Paci, E., Pastor, R. W., Post, C. B., Pu, J. Z., Schaefer, M., Tidor, B., Venable, R. M., Woodcock, H. L., Wu, X., Yang, W., York, D. M., and Karplus, M. (2009) CHARMM: The biomolecular simulation program. J. Comput. Chem. 30, 1545-1614.
  • 45
    • 0025197061 scopus 로고
    • pKa's of ionizable groups in proteins: Atomic detail from a continuum electrostatic model
    • Bashford, D., and Karplus, M. (1990) pKa's of ionizable groups in proteins: Atomic detail from a continuum electrostatic model. Biochemistry 29, 10219-10225.
    • (1990) Biochemistry , vol.29 , pp. 10219-10225
    • Bashford, D.1    Karplus, M.2
  • 46
    • 15444372631 scopus 로고    scopus 로고
    • Reaction of morphinone reductase with 2-cyclohexen-1-one and 1-nitrocyclohexene: Proton donation, ligand binding, and the role of residues Histidine 186 and Asparagine 189
    • Messiha, H. L., Munro, A. W., Bruce, N. C., Barsukov, I., and Scrutton, N. S. (2005) Reaction of morphinone reductase with 2-cyclohexen-1-one and 1-nitrocyclohexene: Proton donation, ligand binding, and the role of residues Histidine 186 and Asparagine 189. J. Biol. Chem. 280, 10695-10709.
    • (2005) J. Biol. Chem , vol.280 , pp. 10695-10709
    • Messiha, H.L.1    Munro, A.W.2    Bruce, N.C.3    Barsukov, I.4    Scrutton, N.S.5
  • 47
    • 0022393945 scopus 로고
    • Potentiometric studies of native and flavin-substituted Old Yellow Enzyme
    • Stewart, R. C., and Massey, V. (1985) Potentiometric studies of native and flavin-substituted Old Yellow Enzyme. J. Biol. Chem. 260, 13639-13647.
    • (1985) J. Biol. Chem , vol.260 , pp. 13639-13647
    • Stewart, R.C.1    Massey, V.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.