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Volumn 275, Issue 24, 2008, Pages 6192-6203

Reduction of aliphatic nitroesters and N-nitramines by Enterobacter cloacae PB2 pentaerythritol tetranitrate reductase: Quantitative structure-activity relationships

Author keywords

Glycerol trinitrate; Hexahydro 1,3,5 trinitro 1,3,5 triazine; Mechanism of reduction; Old Yellow Enzyme; Pentaerythritol tetranitrate reductase

Indexed keywords

ALIPHATIC COMPOUND; BACTERIAL ENZYME; CYCLONITE; DIGLYCEROL TETRANITRATE; ERYTHRITYL TETRANITRATE; ESTER; ESTER DERIVATIVE; FLAVOPROTEIN; GLYCEROL DERIVATIVE; GLYCERYL TRINITRATE; INOSITOL DERIVATIVE; INOSITOL HEXANITRATE; MANNITYL HEXANITRATE; NITRIC ACID DERIVATIVE; NITROGEN DERIVATIVE; OCTAHYDRO1,3,5,7 TETRANITRO 1,3,5,7 TETRAZOCINE; OCTANOL; ORGANIC COMPOUND; ORGANIC NITRATE; PENTAERYTHRITYL TETRANITRATE; PENTAERYTHRITYL TETRANITRATE REDUCTASE; SUPEROXIDE; UNCLASSIFIED DRUG; XYLITOL PENTANITRATE;

EID: 56849098621     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2008.06744.x     Document Type: Article
Times cited : (20)

References (37)
  • 4
    • 0032922021 scopus 로고    scopus 로고
    • Reaction of organic nitrate esters and S-nitrosothiols with reduced flavins: A possible mechanism of bioactivation
    • Wong PS-Y Fukuto JM (1999) Reaction of organic nitrate esters and S-nitrosothiols with reduced flavins: a possible mechanism of bioactivation. Drug Metab Dispos 27, 502 509.
    • (1999) Drug Metab Dispos , vol.27 , pp. 502-509
    • Ps-Y, W.1    Fukuto, J.M.2
  • 5
    • 0035902511 scopus 로고    scopus 로고
    • Old yellow enzyme: Reduction of nitrate esters, glycerin trinitrate, and propylene 1,2-dinitrate
    • Meah Y, Brown BJ, Chakraborty S Massey V (2001) Old yellow enzyme: reduction of nitrate esters, glycerin trinitrate, and propylene 1,2-dinitrate. Proc Natl Acad Sci USA 98, 8560 8565.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 8560-8565
    • Meah, Y.1    Brown, B.J.2    Chakraborty, S.3    Massey, V.4
  • 6
    • 0029946464 scopus 로고    scopus 로고
    • Sequence and properties of pentaerythritol tetranitrate reductase from Enterobacter cloacae PB2
    • French CE, Nicklin S Bruce NC (1996) Sequence and properties of pentaerythritol tetranitrate reductase from Enterobacter cloacae PB2. J Bacteriol 178, 6623 6627.
    • (1996) J Bacteriol , vol.178 , pp. 6623-6627
    • French, C.E.1    Nicklin, S.2    Bruce, N.C.3
  • 7
  • 8
    • 0030867134 scopus 로고    scopus 로고
    • Purification, properties, and sequence of glycerol trinitrate reductase from Agrobacterium radiobacter
    • Snape JR, Walkley NA, Morby AP, Nicklin S White GF (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
  • 9
    • 1542286918 scopus 로고    scopus 로고
    • Characterization of glycerol trinitrate reductase (NerA) and the catalytic role of active-site residues
    • Marshall SJ, Krause D, Blencowe DK White GF (2004) Characterization of glycerol trinitrate reductase (NerA) and the catalytic role of active-site residues. J Bacteriol 186, 1802 1810.
    • (2004) J Bacteriol , vol.186 , pp. 1802-1810
    • Marshall, S.J.1    Krause, D.2    Blencowe, D.K.3    White, G.F.4
  • 10
    • 0030731165 scopus 로고    scopus 로고
    • Regioselectivity of nitroglycerin denitration by flavoprotein nitroester reductases purified from two Pseudomonas species
    • Blehert DS, Knoke KL, Fox BG Chambliss GH (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
  • 11
    • 0032738032 scopus 로고    scopus 로고
    • Cloning and sequence of two Pseudomonas flavoprotein xenobiotic reductases
    • Blehert DS, Fox BG Chambliss GH (1999) Cloning and sequence 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
  • 12
    • 0037077313 scopus 로고    scopus 로고
    • Kinetic and structural basis of reactivity of pentaerythritol tetranitrate reductase with NADPH, 2-cyclohexanone, nitroesters, and nitroaromatic explosives
    • Khan H, Harris RJ, Barna T, Craig DH, Bruce NC, Munro AW, Moody PCE Scrutton NS (2002) Kinetic and structural basis of reactivity of pentaerythritol tetranitrate reductase with NADPH, 2-cyclohexanone, 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.E.7    Scrutton, N.S.8
  • 13
    • 0037098890 scopus 로고    scopus 로고
    • Biotransformation of hexahydro-1,3,5-trinitro-1.3,5-triazine catalyzed by a NAD(P)H:nitrate oxidoreductase from Aspergillus niger
    • Bhushan B, Halasz A, Spain J, Thiboutot S, Ampleman G Hawari J (2002) Biotransformation of hexahydro-1,3,5-trinitro-1.3,5-triazine catalyzed by a NAD(P)H:nitrate oxidoreductase from Aspergillus niger. Environ Sci Technol 36, 3104 3108.
    • (2002) Environ Sci Technol , vol.36 , pp. 3104-3108
    • Bhushan, B.1    Halasz, A.2    Spain, J.3    Thiboutot, S.4    Ampleman, G.5    Hawari, J.6
  • 14
    • 25144525665 scopus 로고    scopus 로고
    • Up-and-down procedure (UDP) determination of acute oral toxicity of nitroso degradation products of hexahydro-1,3,5-trinitro-1,3,5-triazine (RDX)
    • Meyer SA, Marchand AJ, Hight JL, Roberts GH, Escalon LB, Inouye LS MacMillan DK (2005) Up-and-down procedure (UDP) determination of acute oral toxicity of nitroso degradation products of hexahydro-1,3,5-trinitro-1,3,5- triazine (RDX). J Appl Toxicol 25, 427 434.
    • (2005) J Appl Toxicol , vol.25 , pp. 427-434
    • Meyer, S.A.1    Marchand, A.J.2    Hight, J.L.3    Roberts, G.H.4    Escalon, L.B.5    Inouye, L.S.6    MacMillan, D.K.7
  • 15
    • 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 RJ, Bruce NC, Barsukov I, Munro AW, Moody PCE Scrutton NS (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.E.7    Scrutton, N.S.8
  • 16
    • 34447300453 scopus 로고    scopus 로고
    • Two-electron reduction of quinones by Enterobacter cloacae PB2 pentaerythritol tetranitrate reductase: Quantitative structure-activity relationships
    • Misevičienė L, Anusevičius Ž, Šarlauskas J, Harris RJ, Scrutton NS Čėnas N (2007) Two-electron reduction of quinones by Enterobacter cloacae PB2 pentaerythritol tetranitrate reductase: quantitative structure-activity relationships. Acta Biochim Polon 54, 379 385.
    • (2007) Acta Biochim Polon , vol.54 , pp. 379-385
    • Misevičiene, L.1    Ž, A.2    Šarlauskas, J.3    Harris, R.J.4    Scrutton, N.S.5    Čenas, N.6
  • 17
    • 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 TM, Khan H, Bruce NC, Barsukov I, Scrutton NS Moody PCE (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.E.6
  • 18
    • 0032937445 scopus 로고    scopus 로고
    • Biodegradation of explosives by transgenic plants expressing pentaerythritol tetranitrate reductase
    • French CE, Rosser SJ, Davies GJ, Nicklin S Bruce NC (1999) Biodegradation of explosives by transgenic plants expressing pentaerythritol tetranitrate reductase. Nat Biotechnol 17, 491 494.
    • (1999) Nat Biotechnol , vol.17 , pp. 491-494
    • French, C.E.1    Rosser, S.J.2    Davies, G.J.3    Nicklin, S.4    Bruce, N.C.5
  • 19
    • 0036386376 scopus 로고    scopus 로고
    • Diaphorase-catalyzed biotransformation of RDX via N-denitration mechanism
    • Bhushan B, Halasz A, Spain JC Hawari J (2002) Diaphorase-catalyzed biotransformation of RDX via N-denitration mechanism. Biochem Biophys Res Commun 296, 779 784.
    • (2002) Biochem Biophys Res Commun , vol.296 , pp. 779-784
    • Bhushan, B.1    Halasz, A.2    Spain, J.C.3    Hawari, J.4
  • 20
    • 0018727622 scopus 로고
    • Product inhibition and abortive complex formation
    • Rudolph FB (1979) Product inhibition and abortive complex formation. Methods Enzymol 63A, 411 436.
    • (1979) Methods Enzymol , vol.63 , pp. 411-436
    • Rudolph, F.B.1
  • 21
    • 49049150043 scopus 로고
    • The reduction of propylene glycol dinitrate and other related nitrate esters on silver electrodes
    • Miles MH Fine DA (1981) The reduction of propylene glycol dinitrate and other related nitrate esters on silver electrodes. J Electroanal Chem 127, 143 155.
    • (1981) J Electroanal Chem , vol.127 , pp. 143-155
    • Miles, M.H.1    Fine, D.A.2
  • 22
    • 0034775362 scopus 로고    scopus 로고
    • Quantitative structure-activity relationships in two-electron reduction of nitroaromatic compounds by Enterobacter cloacae NAD(P)H:nitroreductase
    • Nivinskas H, Koder RL, Anusevičius Ž, Šarlauskas J, Miller A-F Čėnas N (2001) Quantitative structure-activity relationships in two-electron reduction of nitroaromatic compounds by Enterobacter cloacae NAD(P)H:nitroreductase. Arch Biochem Biophys 385, 170 178.
    • (2001) Arch Biochem Biophys , vol.385 , pp. 170-178
    • Nivinskas, H.1    Koder, R.L.2    Ž, A.3    Šarlauskas, J.4    Miller, A.-F.5    Čenas, N.6
  • 25
    • 0029863639 scopus 로고    scopus 로고
    • Effects of amino acid residues at the cleavable site of substrates on the remarkable activation of thermolysin by salts
    • Inouye K, Lee S-B Tonomura B (1996) Effects of amino acid residues at the cleavable site of substrates on the remarkable activation of thermolysin by salts. Biochem J 315, 133 138.
    • (1996) Biochem J , vol.315 , pp. 133-138
    • Inouye, K.1    Lee, S.-B.2    Tonomura, B.3
  • 26
    • 33744964055 scopus 로고    scopus 로고
    • Characterization of the mechanism of cytochrome P450 reductase-cytochrome P450-mediated nitric oxide and nitrosothiol generation from organic nitrates
    • Li H, Liu X, Cui H, Chen Y-R, Cardounel AJ Zweier JL (2006) Characterization of the mechanism of cytochrome P450 reductase-cytochrome P450-mediated nitric oxide and nitrosothiol generation from organic nitrates. J Biol Chem 281, 12546 12554.
    • (2006) J Biol Chem , vol.281 , pp. 12546-12554
    • Li, H.1    Liu, X.2    Cui, H.3    Chen, Y.-R.4    Cardounel, A.J.5    Zweier, J.L.6
  • 27
    • 20444451649 scopus 로고    scopus 로고
    • Xanthine oxidase catalyzes anaerobic transformation of organic nitroesters to nitric oxide and nitrosothiols. Characterization of this mechanism and the link between organic nitrate and guanylyl cyclase activation
    • Li H, Cui H, Liu X Zweier JL (2005) Xanthine oxidase catalyzes anaerobic transformation of organic nitroesters to nitric oxide and nitrosothiols. Characterization of this mechanism and the link between organic nitrate and guanylyl cyclase activation. J Biol Chem 280, 16594 16600.
    • (2005) J Biol Chem , vol.280 , pp. 16594-16600
    • Li, H.1    Cui, H.2    Liu, X.3    Zweier, J.L.4
  • 28
    • 36749100010 scopus 로고    scopus 로고
    • Exploring the biochemical properties and remediation applications of the unusual explosive-degrading P450 system XplA/B
    • Jackson RG, Rylott EL, Fournier D, Hawari J Bruce NC (2007) Exploring the biochemical properties and remediation applications of the unusual explosive-degrading P450 system XplA/B. Proc Natl Acad Sci USA 104, 16822 16827.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 16822-16827
    • Jackson, R.G.1    Rylott, E.L.2    Fournier, D.3    Hawari, J.4    Bruce, N.C.5
  • 29
    • 11244257041 scopus 로고    scopus 로고
    • Diaphorase can metabolize some vasorelaxants to NO and eliminate NO scavenging effect of 2-phenyl-4,4,5,5-tetramethylimidazoline-1-oxyl-3-oxide (PTO)
    • Bartik P, Chalupsky K, Vavruska L, Muller B, Stocklet JC Entlicher G (2004) Diaphorase can metabolize some vasorelaxants to NO and eliminate NO scavenging effect of 2-phenyl-4,4,5,5-tetramethylimidazoline-1-oxyl-3-oxide (PTO). Physiol Res 53, 615 620.
    • (2004) Physiol Res , vol.53 , pp. 615-620
    • Bartik, P.1    Chalupsky, K.2    Vavruska, L.3    Muller, B.4    Stocklet, J.C.5    Entlicher, G.6
  • 31
    • 0037079889 scopus 로고    scopus 로고
    • Factors influencing rates and clearance in P450-mediated reactions: QSARs for substrates of the xenobiotic-metabolizing hepatic microsomal P450s
    • Lewis DFV Dickins M (2002) Factors influencing rates and clearance in P450-mediated reactions: QSARs for substrates of the xenobiotic-metabolizing hepatic microsomal P450s. Toxicology 170, 45 53.
    • (2002) Toxicology , vol.170 , pp. 45-53
    • Lewis, D.F.V.1    Dickins, M.2
  • 32
    • 0026709245 scopus 로고
    • Quantitative structure-metabolism relationship analyses of MAO-mediated toxication of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine and analogs
    • Altomare C, Carrupt P-A, Gaillard P, Tayar NE, Testa B Carotti A (1992) Quantitative structure-metabolism relationship analyses of MAO-mediated toxication of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine and analogs. Chem Res Toxicol 5, 366 375.
    • (1992) Chem Res Toxicol , vol.5 , pp. 366-375
    • Altomare, C.1    Carrupt, P.-A.2    Gaillard, P.3    Tayar, N.E.4    Testa, B.5    Carotti, A.6
  • 34
    • 0037102466 scopus 로고    scopus 로고
    • Two-electron reduction of quinones by rat liver NAD(P)H:quinone oxidoreductase: Quantitative structure-activity relationships
    • Anusevičius Ž, Šarlauskas J Čėnas N (2002) Two-electron reduction of quinones by rat liver NAD(P)H:quinone oxidoreductase: quantitative structure-activity relationships. Arch Biochem Biophys 404, 254 262.
    • (2002) Arch Biochem Biophys , vol.404 , pp. 254-262
    • Ž, A.1    Šarlauskas, J.2    Čenas, N.3
  • 35
    • 0029068515 scopus 로고
    • The three-dimensional structure of NAD(P)H:quinone reductase, a flavoprotein involved in cancer chemoprotection and chemotherapy: Mechanism of the two-electron reduction
    • Li R, Bianchet MA, Talalay P Amzel LM (1995) The three-dimensional structure of NAD(P)H:quinone reductase, a flavoprotein involved in cancer chemoprotection and chemotherapy: mechanism of the two-electron reduction. Proc Natl Acad Sci USA 92, 8846 8850.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 8846-8850
    • Li, R.1    Bianchet, M.A.2    Talalay, P.3    Amzel, L.M.4
  • 36
    • 0028774535 scopus 로고
    • Old yellow enzyme at 2 Å resolution: Overall structure, ligand binding, and comparison with related flavoproteins
    • Fox KM Karplus PA (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


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