메뉴 건너뛰기




Volumn 54, Issue 2, 2007, Pages 379-385

Two-electron reduction of quinones by Enterobacter cloacae PB2 pentaerythritol tetranitrate reductase: Quantitative structure-activity relationships

Author keywords

Electron transfer; Pentaerythritol tetranitrate reductase; Quinones; Reduction mechanism

Indexed keywords

ENTEROBACTER CLOACAE; MAMMALIA;

EID: 34447300453     PISSN: 0001527X     EISSN: 1734154X     Source Type: Journal    
DOI: 10.18388/abp.2007_3260     Document Type: Article
Times cited : (8)

References (26)
  • 2
    • 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
    • Anusevičius, Z.1    Šarlauskas, J.2    Čėnas, N.3
  • 3
    • 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
  • 4
    • 0242582914 scopus 로고    scopus 로고
    • H-tunneling in the multiple H-transfers of the catalytic cycle of morphinone reductase and in the reductive half-reaction of the homologous pentaerythritol tetranitrate reductase
    • Basran J, Harris RJ, Sutcliffe MJ, Scrutton NS (2003) H-tunneling in the multiple H-transfers of the catalytic cycle of morphinone reductase and in the reductive half-reaction of the homologous pentaerythritol tetranitrate reductase. J Biol Chem 278: 43973-43982.
    • (2003) J Biol Chem , vol.278 , pp. 43973-43982
    • Basran, J.1    Harris, R.J.2    Sutcliffe, M.J.3    Scrutton, N.S.4
  • 5
    • 0029878360 scopus 로고    scopus 로고
    • Degradation of pentaerythritol tetranitrate by Enterobacter cloacae PB2
    • Binks PR, French CE, Nicklin S, Bruce NC (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
  • 6
    • 0001377673 scopus 로고
    • Mechanism of the oxidation of NADH by quinones. Energetics of one-electron and hydride routes
    • Carlson BW, Miller LL (1985) Mechanism of the oxidation of NADH by quinones. Energetics of one-electron and hydride routes. J Am Chem Soc 107: 479-485.
    • (1985) J Am Chem Soc , vol.107 , pp. 479-485
    • Carlson, B.W.1    Miller, L.L.2
  • 7
    • 34447342788 scopus 로고    scopus 로고
    • Čėnas NK, Vienožinskis JV, Kulys JJ (1987) Kinetic regularities of Cl. kluyveri diaphorase. Biokhimiya 52: 91-96 (in Russian).
    • Čėnas NK, Vienožinskis JV, Kulys JJ (1987) Kinetic regularities of Cl. kluyveri diaphorase. Biokhimiya 52: 91-96 (in Russian).
  • 10
    • 0017181413 scopus 로고
    • Potential central nervous system antitumor agents. Aziridinylbenzoquinones. 2
    • Chou F, Khan AH, Driscoll JS (1976) Potential central nervous system antitumor agents. Aziridinylbenzoquinones. 2. J Med Chem 19: 1302-1308.
    • (1976) J Med Chem , vol.19 , pp. 1302-1308
    • Chou, F.1    Khan, A.H.2    Driscoll, J.S.3
  • 11
    • 0029946464 scopus 로고    scopus 로고
    • Sequence and properties of pentaerythritol tetranitrate reductase from Enterobacter cloacae PB2
    • French CE, Nicklin S, Bruce N (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.3
  • 12
    • 0031948118 scopus 로고    scopus 로고
    • Aerobic degradation of 2,4,6-trinitrotoluene by Enterobacter cloacae PB2 and by pentaerythritol tetranitrate reductase
    • French CE, Nicklin S, Bruce N (1998) Aerobic degradation of 2,4,6-trinitrotoluene by Enterobacter cloacae PB2 and by pentaerythritol tetranitrate reductase. Appl Environ Microbiol 64: 2864-2868.
    • (1998) Appl Environ Microbiol , vol.64 , pp. 2864-2868
    • French, C.E.1    Nicklin, S.2    Bruce, N.3
  • 13
    • 37049073463 scopus 로고
    • Acid-catalysed reduction of p-benzoquinone derivatives by an NADH analoque, 9,10-dihydro-10- methylacridine. The energetic comparison of one-electron vs. two-electron pathways
    • Fukuzumi S, Ishikawa M, Tanaka T (1989) Acid-catalysed reduction of p-benzoquinone derivatives by an NADH analoque, 9,10-dihydro-10- methylacridine. The energetic comparison of one-electron vs. two-electron pathways. J Chem Soc Perkin Trans 2: 1811-1816.
    • (1989) J Chem Soc Perkin Trans , vol.2 , pp. 1811-1816
    • Fukuzumi, S.1    Ishikawa, M.2    Tanaka, T.3
  • 14
    • 0037192818 scopus 로고    scopus 로고
    • Structures of nitroreductase in three states. Effects of inhibitor binding and reduction
    • Haynes CA, Koder RL, Miller A-F, Rodgers DW (2002) Structures of nitroreductase in three states. Effects of inhibitor binding and reduction. J Biol Chem 277: 11513-11520.
    • (2002) J Biol Chem , vol.277 , pp. 11513-11520
    • Haynes, C.A.1    Koder, R.L.2    Miller, A.-F.3    Rodgers, D.W.4
  • 15
    • 0025128366 scopus 로고
    • On the mechanism of one-electron and two-electron reduction of quinones by microsomal flavin enzymes - the kinetic analysis between cytochrome-B5 and menadione
    • Iyanagi T (1990) On the mechanism of one-electron and two-electron reduction of quinones by microsomal flavin enzymes - the kinetic analysis between cytochrome-B5 and menadione. Free Radic Res Commun 8: 259-268.
    • (1990) Free Radic Res Commun , vol.8 , pp. 259-268
    • Iyanagi, T.1
  • 16
    • 0037077313 scopus 로고    scopus 로고
    • Kinetic and structure basis of reactivity of pentaerythritol tetranitrate reductase with NADPH, 2-cyclohexenone, nitroesters and nitroaromatic explosives
    • Khan H, Harris RJ, Barna T, Craig DH, Bruce NC, Munro AW, Moody PCE, Scrutton NS (2002) Kinetic and structure 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.E.7    Scrutton, N.S.8
  • 17
    • 3142695539 scopus 로고    scopus 로고
    • Atomic resolution structures and solution behavior of enzyme-substrate complexes of Enterobacter cloacae PB2 pentaerythritol tetranitrate reductase
    • 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. 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
  • 18
    • 2242420015 scopus 로고    scopus 로고
    • Flavin thermodynamics explain the oxygen insensitivity of enteric nitroreductases
    • Koder RL, Haynes CA, Rodgers ME, Rodgers DW, Miller A-F (2002) Flavin thermodynamics explain the oxygen insensitivity of enteric nitroreductases. Biochemistry 41: 14197-14205.
    • (2002) Biochemistry , vol.41 , pp. 14197-14205
    • Koder, R.L.1    Haynes, C.A.2    Rodgers, M.E.3    Rodgers, D.W.4    Miller, A.-F.5
  • 20
    • 0029068515 scopus 로고
    • The threedimentional structure of NADP(H) : Quinone reductase, a flavoprotein involved in cancer chemoprotection and chemotherapy: mechanism of the two-electron reduction
    • Li R, Bianchet MA, Talalay P, Amzel M (1995) The threedimentional structure of NADP(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, M.4
  • 21
    • 0022004980 scopus 로고
    • Electron transfers in chemistry and biology
    • Marcus RA, Sutin N (1985) Electron transfers in chemistry and biology. Biochim Biophys Acta 811: 265-322.
    • (1985) Biochim Biophys Acta , vol.811 , pp. 265-322
    • Marcus, R.A.1    Sutin, N.2
  • 22
    • 0022649071 scopus 로고
    • Reactivity of old yellow enzyme with alpha-NADPH and other pyridine nucleotides
    • Massey V, Schopfer LM (1986) Reactivity of old yellow enzyme with alpha-NADPH and other pyridine nucleotides. J Biol Chem 261: 1215-1222.
    • (1986) J Biol Chem , vol.261 , pp. 1215-1222
    • Massey, V.1    Schopfer, L.M.2
  • 23
    • 0037099606 scopus 로고    scopus 로고
    • Two-electron reduction of quinones by Enterobacter cloacae NAD(P)H : Nitroreductase: quantitative structure-activity relationships
    • Nivinskas H, Staškevičienė S, Šarlauskas J, Koder RL, Miller A-F, Čėnas N (2002) Two-electron reduction of quinones by Enterobacter cloacae NAD(P)H : nitroreductase: quantitative structure-activity relationships. Arch Biochem Biophys 403: 249-258.
    • (2002) Arch Biochem Biophys , vol.403 , pp. 249-258
    • Nivinskas, H.1    Staškevičienė, S.2    Šarlauskas, J.3    Koder, R.L.4    Miller, A.-F.5    Čėnas, N.6
  • 24
    • 0026040838 scopus 로고
    • Molecular mechanisms of quinone cytotoxicity
    • O'Brien PJ (1991) Molecular mechanisms of quinone cytotoxicity. Chem Biol Interact 80: 1-41.
    • (1991) Chem Biol Interact , vol.80 , pp. 1-41
    • O'Brien, P.J.1
  • 25
    • 0028893931 scopus 로고
    • DT-diaphorase. Redox potential, steady-state, and rapid reaction studies
    • Tedeschi G, Chen S, Massey V (1995) DT-diaphorase. Redox potential, steady-state, and rapid reaction studies. J Biol Chem 270: 1198-1204.
    • (1995) J Biol Chem , vol.270 , pp. 1198-1204
    • Tedeschi, G.1    Chen, S.2    Massey, V.3
  • 26
    • 84872846883 scopus 로고
    • Reduction potentials of one-electron couples involving free radicals in aqueous solutions
    • Wardman P (1989) Reduction potentials of one-electron couples involving free radicals in aqueous solutions. J Phys Chem Ref Data 18: 1637-1755.
    • (1989) J Phys Chem Ref Data , vol.18 , pp. 1637-1755
    • Wardman, P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.