메뉴 건너뛰기




Volumn 102, Issue 2, 2018, Pages 985-994

Simultaneous detection of NADPH consumption and H 2 O 2 production using the Ampliflu™ Red assay for screening of P450 activities and uncoupling

Author keywords

Cytochrome P450; Hydrogen peroxide; N acetyl 3,7 dihydroxyphenoxazin; P450 BM3; Uncoupling

Indexed keywords

BACTERIOLOGY; ENZYMES; HYDROGEN PEROXIDE; IRON COMPOUNDS; OXIDATION; PEROXIDES; PORPHYRINS; SUBSTRATES;

EID: 85034217962     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-017-8636-3     Document Type: Article
Times cited : (39)

References (52)
  • 1
    • 0024281310 scopus 로고
    • Deuterium isotope effects in norcamphor metabolism by cytochrome P-450cam: kinetic evidence for the two-electron reduction of a high-valent iron-oxo intermediate
    • COI: 1:CAS:528:DyaL1cXhtVykt7o%3D, PID: 3284586
    • Atkins WM, Sligar SG (1988) Deuterium isotope effects in norcamphor metabolism by cytochrome P-450cam: kinetic evidence for the two-electron reduction of a high-valent iron-oxo intermediate. Biochemistry 27(5):1610–1616. https://doi.org/10.1021/bi00405a033
    • (1988) Biochemistry , vol.27 , Issue.5 , pp. 1610-1616
    • Atkins, W.M.1    Sligar, S.G.2
  • 2
    • 33744520321 scopus 로고    scopus 로고
    • Cytochromes P450 as versatile biocatalysts
    • COI: 1:CAS:528:DC%2BD28Xltl2isLw%3D, PID: 16516322
    • Bernhardt R (2006) Cytochromes P450 as versatile biocatalysts. J Biotechnol 124(1):128–145. https://doi.org/10.1016/j.jbiotec.2006.01.026
    • (2006) J Biotechnol , vol.124 , Issue.1 , pp. 128-145
    • Bernhardt, R.1
  • 3
    • 0026074611 scopus 로고
    • Cytochrome P-450 spin state and leakiness of the monooxygenase pathway
    • COI: 1:CAS:528:DyaK3MXitVahu7Y%3D, PID: 1848383
    • Blanck J, Ristau O, Zhukov AA, Archakov AI, Rein H, Ruckpaul K (1991) Cytochrome P-450 spin state and leakiness of the monooxygenase pathway. Xenobiotica 21(1):121–135. https://doi.org/10.3109/00498259109039456
    • (1991) Xenobiotica , vol.21 , Issue.1 , pp. 121-135
    • Blanck, J.1    Ristau, O.2    Zhukov, A.A.3    Archakov, A.I.4    Rein, H.5    Ruckpaul, K.6
  • 4
    • 84860741240 scopus 로고    scopus 로고
    • Engineering the third wave of biocatalysis
    • COI: 1:CAS:528:DC%2BC38XmvVeqsLk%3D, PID: 22575958
    • Bornscheuer UT, Huisman GW, Kazlauskas RJ, Lutz S, Moore JC, Robins K (2012) Engineering the third wave of biocatalysis. Nature 485(7397):185–194. https://doi.org/10.1038/nature11117
    • (2012) Nature , vol.485 , Issue.7397 , pp. 185-194
    • Bornscheuer, U.T.1    Huisman, G.W.2    Kazlauskas, R.J.3    Lutz, S.4    Moore, J.C.5    Robins, K.6
  • 5
    • 0034152767 scopus 로고    scopus 로고
    • Oxidative stress in bacteria and protein damage by reactive oxygen species
    • COI: 1:CAS:528:DC%2BD3cXksVCnur0%3D, PID: 10963327
    • Cabiscol E, Tamarit J, Ros J (2000) Oxidative stress in bacteria and protein damage by reactive oxygen species. Int Microbiol 3(1):3–8. https://doi.org/10.2436/im.v3i1.9235
    • (2000) Int Microbiol , vol.3 , Issue.1 , pp. 3-8
    • Cabiscol, E.1    Tamarit, J.2    Ros, J.3
  • 6
    • 0034819837 scopus 로고    scopus 로고
    • Protein engineering of Bacillus megaterium CYP102: the oxidation of polycyclic aromatic hydrocarbons
    • COI: 1:CAS:528:DC%2BD3MXktVSkur0%3D, PID: 11358532
    • Carmichael AB, Wong LL (2001) Protein engineering of Bacillus megaterium CYP102: the oxidation of polycyclic aromatic hydrocarbons. Eur J Biochem 268(10):3117–3125. https://doi.org/10.1046/j.1432-1327.2001.02212.x
    • (2001) Eur J Biochem , vol.268 , Issue.10 , pp. 3117-3125
    • Carmichael, A.B.1    Wong, L.L.2
  • 7
    • 65249112738 scopus 로고    scopus 로고
    • Bioreduction of idarubicin and formation of ROS responsible for DNA cleavage by NADPH-cytochrome P450 reductase and its potential role in the antitumor effect
    • Çelik H, Arinç E (2008) Bioreduction of idarubicin and formation of ROS responsible for DNA cleavage by NADPH-cytochrome P450 reductase and its potential role in the antitumor effect. J Pharm Sci 11(4):68–82
    • (2008) J Pharm Sci , vol.11 , Issue.4 , pp. 68-82
    • Çelik, H.1    Arinç, E.2
  • 8
    • 0016425962 scopus 로고
    • The steady-state kinetics of peroxidase with 2,2′-azino-di-(3-ethylbenzthiazoline- 6-sulphonic acid) as chromogen
    • COI: 1:STN:280:DyaE28%2FmtFGjtg%3D%3D, PID: 1191252
    • Childs BRE, Bardsley WG (1975) The steady-state kinetics of peroxidase with 2,2′-azino-di-(3-ethylbenzthiazoline- 6-sulphonic acid) as chromogen. Biochem J 145(1):93–103. https://doi.org/10.1042/bj1450093
    • (1975) Biochem J , vol.145 , Issue.1 , pp. 93-103
    • Childs, B.R.E.1    Bardsley, W.G.2
  • 9
    • 13844322067 scopus 로고    scopus 로고
    • CYTOCHROME P450: nature’s most versatile biological catalyst
    • COI: 1:CAS:528:DC%2BD2MXisVWjtrs%3D, PID: 15832443
    • Coon MJ (2005) CYTOCHROME P450: nature’s most versatile biological catalyst. Annu Rev Pharmacol Toxicol 45(1):1–25. https://doi.org/10.1146/annurev.pharmtox.45.120403.100030
    • (2005) Annu Rev Pharmacol Toxicol , vol.45 , Issue.1 , pp. 1-25
    • Coon, M.J.1
  • 10
    • 38849130706 scopus 로고    scopus 로고
    • The role of the conserved threonine in P450 BM3 oxygen activation: substrate-determined hydroxylation activity of the Thr268Ala mutant
    • COI: 1:CAS:528:DC%2BD1cXlt1Whs7g%3D, PID: 18161730
    • Cryle MJ, De Voss JJ (2008) The role of the conserved threonine in P450 BM3 oxygen activation: substrate-determined hydroxylation activity of the Thr268Ala mutant. Chembiochem 9(2):261–266. https://doi.org/10.1002/cbic.200700537
    • (2008) Chembiochem , vol.9 , Issue.2 , pp. 261-266
    • Cryle, M.J.1    De Voss, J.J.2
  • 11
    • 0030749297 scopus 로고    scopus 로고
    • Substrate docking algorithms and prediction of the substrate specificity of cytochrome P450(cam) and its L244A mutant
    • De Voss JJ, Sibbesen O, Zhang Z, Ortiz De Montellano PR (1997) Substrate docking algorithms and prediction of the substrate specificity of cytochrome P450(cam) and its L244A mutant. J Am Chem Soc 119(24):5489–5498. https://doi.org/10.1021/ja970349v
    • (1997) J Am Chem Soc , vol.119 , Issue.24 , pp. 5489-5498
    • De Voss, J.J.1    Sibbesen, O.2    Zhang, Z.3    Ortiz De Montellano, P.R.4
  • 12
    • 79951553420 scopus 로고    scopus 로고
    • Understanding uncoupling in the multiredox centre P450 3A4–BMR model system
    • COI: 1:CAS:528:DC%2BC3cXhtFOrtbvM, PID: 20857167
    • Degregorio D, Sadeghi SJ, Di Nardo G, Gilardi G, Solinas SP (2011) Understanding uncoupling in the multiredox centre P450 3A4–BMR model system. J Biol Inorg Chem 16(1):109–116. https://doi.org/10.1007/s00775-010-0708-0
    • (2011) J Biol Inorg Chem , vol.16 , Issue.1 , pp. 109-116
    • Degregorio, D.1    Sadeghi, S.J.2    Di Nardo, G.3    Gilardi, G.4    Solinas, S.P.5
  • 13
    • 85016159325 scopus 로고    scopus 로고
    • Human cytochrome P450 3A4 as a biocatalyst: effects of the engineered linker in modulation of coupling efficiency in 3A4-BMR chimeras
    • Degregorio D, D’Avino S, Castrignano S, di Nardo G, Sadeghi SJ, Catucci G, Gilardi G (2017) Human cytochrome P450 3A4 as a biocatalyst: effects of the engineered linker in modulation of coupling efficiency in 3A4-BMR chimeras. Front Pharmacol 8. https://doi.org/10.3389/fphar.2017.00121
    • (2017) Front Pharmacol , vol.8
    • Degregorio, D.1    D’Avino, S.2    Castrignano, S.3    di Nardo, G.4    Sadeghi, S.J.5    Catucci, G.6    Gilardi, G.7
  • 14
    • 21844434930 scopus 로고    scopus 로고
    • Structure and chemistry of cytochrome P450
    • COI: 1:CAS:528:DC%2BD2MXjtl2ns70%3D, PID: 15941214
    • Denisov IG, Makris TM, Sligar SG, Schlichting I (2005) Structure and chemistry of cytochrome P450. Chem Rev 105(6):2253–2277. https://doi.org/10.1021/cr0307143
    • (2005) Chem Rev , vol.105 , Issue.6 , pp. 2253-2277
    • Denisov, I.G.1    Makris, T.M.2    Sligar, S.G.3    Schlichting, I.4
  • 15
    • 34147112191 scopus 로고    scopus 로고
    • Cooperativity in cytochrome P450 3A4 linkages in substrate binding, spin state, uncoupling, and product formation
    • COI: 1:CAS:528:DC%2BD2sXitlSrs7g%3D, PID: 17213193
    • Denisov IG, Baas BJ, Grinkova YV, Sligar S (2007) Cooperativity in cytochrome P450 3A4 linkages in substrate binding, spin state, uncoupling, and product formation. J Biol Chem 282(10):7066–7076. https://doi.org/10.1074/jbc.M609589200
    • (2007) J Biol Chem , vol.282 , Issue.10 , pp. 7066-7076
    • Denisov, I.G.1    Baas, B.J.2    Grinkova, Y.V.3    Sligar, S.4
  • 16
    • 84859565523 scopus 로고    scopus 로고
    • Tuning P 450 enzymes as oxidation catalysts
    • COI: 1:CAS:528:DC%2BC38XislSrt7k%3D
    • Fasan R (2012) Tuning P 450 enzymes as oxidation catalysts. ACS Catal 2(4):647–666. https://doi.org/10.1021/cs300001x
    • (2012) ACS Catal , vol.2 , Issue.4 , pp. 647-666
    • Fasan, R.1
  • 17
    • 84874350400 scopus 로고    scopus 로고
    • Cytochrome P450 reductase from Candida apicola: versatile redox partner for bacterial P450s
    • COI: 1:CAS:528:DC%2BC3sXhvFGhtbk%3D, PID: 22526787
    • Girhard M, Tieves F, Weber E, Smit MS, Urlacher VB (2013) Cytochrome P450 reductase from Candida apicola: versatile redox partner for bacterial P450s. Appl Microbiol Biotechnol 97(4):1625–1635. https://doi.org/10.1007/s00253-012-4026-z
    • (2013) Appl Microbiol Biotechnol , vol.97 , Issue.4 , pp. 1625-1635
    • Girhard, M.1    Tieves, F.2    Weber, E.3    Smit, M.S.4    Urlacher, V.B.5
  • 18
    • 69949143453 scopus 로고    scopus 로고
    • Mechanistic aspects of horseradish peroxidase elucidated through single-molecule studies
    • COI: 1:CAS:528:DC%2BD1MXjvFKrt7o%3D, PID: 19338338
    • Gorris HH, Walt DR (2009) Mechanistic aspects of horseradish peroxidase elucidated through single-molecule studies. J Am Chem Soc 131(4):6277–6282. 10.18433/j3s88w
    • (2009) J Am Chem Soc , vol.131 , Issue.4 , pp. 6277-6282
    • Gorris, H.H.1    Walt, D.R.2
  • 19
    • 0021138883 scopus 로고
    • On the stoichiometry of the oxidase and monooxygenase reactions catalyzed by liver microsomal cytochrome P-450
    • COI: 1:CAS:528:DyaL2cXksFSks7w%3D, PID: 6725272
    • Gorsky LD, Koop DR, Coon MJ (1984) On the stoichiometry of the oxidase and monooxygenase reactions catalyzed by liver microsomal cytochrome P-450. J Biol Chem 259(11):6812–6817
    • (1984) J Biol Chem , vol.259 , Issue.11 , pp. 6812-6817
    • Gorsky, L.D.1    Koop, D.R.2    Coon, M.J.3
  • 20
    • 0031021585 scopus 로고    scopus 로고
    • An active site substitution, F87V, converts cytochrome P450 BM-3 into a regio- and stereoselective (14S, 15R)-arachidonic acid epoxygenase
    • COI: 1:CAS:528:DyaK2sXmtFKhug%3D%3D, PID: 8995412
    • Graham-Lorence S, Truan G, Peterson JA, Falck JR, Wei S, Helvig C, Capdevila JH (1997) An active site substitution, F87V, converts cytochrome P450 BM-3 into a regio- and stereoselective (14S, 15R)-arachidonic acid epoxygenase. J Biol Chem 272(2):1127–1135. https://doi.org/10.1074/jbc.272.2.1127
    • (1997) J Biol Chem , vol.272 , Issue.2 , pp. 1127-1135
    • Graham-Lorence, S.1    Truan, G.2    Peterson, J.A.3    Falck, J.R.4    Wei, S.5    Helvig, C.6    Capdevila, J.H.7
  • 21
    • 0028860850 scopus 로고
    • The stoichiometry of the cytochrome P-450-catalyzed metabolism of methoxyflurane and benzphetamine in the presence and absence of cytochrome b5
    • COI: 1:CAS:528:DyaK2MXovFWnurc%3D, PID: 7559586
    • Gruenke LD, Konopka K, Cadieu M, Waskell L (1995) The stoichiometry of the cytochrome P-450-catalyzed metabolism of methoxyflurane and benzphetamine in the presence and absence of cytochrome b5. J Biol Chem 270(42):24707–24718. https://doi.org/10.1074/jbc.270.42.24707
    • (1995) J Biol Chem , vol.270 , Issue.42 , pp. 24707-24718
    • Gruenke, L.D.1    Konopka, K.2    Cadieu, M.3    Waskell, L.4
  • 22
    • 0014053835 scopus 로고
    • A new substrate for fluorometric determination of oxidative enzymes
    • Guilbaul GG, Kramer DN, Hackley E (1967) A new substrate for fluorometric determination of oxidative enzymes. Anal Chem 39(2):271. https://doi.org/10.1021/ac60246a029
    • (1967) Anal Chem , vol.39 , Issue.2 , pp. 271
    • Guilbaul, G.G.1    Kramer, D.N.2    Hackley, E.3
  • 23
    • 85016285668 scopus 로고    scopus 로고
    • Tips on the analysis of phosphatidic acid by the fluorometric coupled enzyme assay
    • COI: 1:CAS:528:DC%2BC2sXlsV2isLs%3D, PID: 28359787
    • Hassaninasab A, Han GS, Carman GM (2017) Tips on the analysis of phosphatidic acid by the fluorometric coupled enzyme assay. Anal Biochem 526:69–70. https://doi.org/10.1016/j.ab.2017.03.020
    • (2017) Anal Biochem , vol.526 , pp. 69-70
    • Hassaninasab, A.1    Han, G.S.2    Carman, G.M.3
  • 24
    • 43049128108 scopus 로고    scopus 로고
    • Heme-iron oxygenases: powerful industrial biocatalysts?
    • COI: 1:CAS:528:DC%2BD1cXlslKlsbw%3D, PID: 18258209
    • Julsing MK, Cornelissen S, Bühler B, Schmid A (2008) Heme-iron oxygenases: powerful industrial biocatalysts? Curr Opin Chem Biol 12(2):177–186. https://doi.org/10.1016/j.cbpa.2008.01.029
    • (2008) Curr Opin Chem Biol , vol.12 , Issue.2 , pp. 177-186
    • Julsing, M.K.1    Cornelissen, S.2    Bühler, B.3    Schmid, A.4
  • 25
    • 0028788589 scopus 로고
    • Uncoupling oxygen transfer and electron transfer in the oxygenation of camphor analogues by cytochrome P450-CAM
    • COI: 1:CAS:528:DyaK2MXps1ahsrk%3D, PID: 7499289
    • Kadkhodayan S, Coulter ED, Maryniak DM, Bryson TA, Dawson JH (1995) Uncoupling oxygen transfer and electron transfer in the oxygenation of camphor analogues by cytochrome P450-CAM. J Biol Chem 270(47):28042–28048. https://doi.org/10.1074/jbc.270.47.28042
    • (1995) J Biol Chem , vol.270 , Issue.47 , pp. 28042-28048
    • Kadkhodayan, S.1    Coulter, E.D.2    Maryniak, D.M.3    Bryson, T.A.4    Dawson, J.H.5
  • 26
    • 34250776517 scopus 로고    scopus 로고
    • CYP2C9 protein interactions with cytochrome b5: effects on the coupling of catalysis
    • COI: 1:CAS:528:DC%2BD2sXns1yhs7s%3D, PID: 17446262
    • Locuson CW, Wienkers LC, Jones JP, Tracy TS (2007) CYP2C9 protein interactions with cytochrome b5: effects on the coupling of catalysis. Drug Metab Dispos 35(7):1174–1181. https://doi.org/10.1124/dmd.107.014910
    • (2007) Drug Metab Dispos , vol.35 , Issue.7 , pp. 1174-1181
    • Locuson, C.W.1    Wienkers, L.C.2    Jones, J.P.3    Tracy, T.S.4
  • 27
    • 0027375275 scopus 로고
    • Molecular recognition in cytochrome P-450: mechanism for the control of uncoupling reactions
    • COI: 1:CAS:528:DyaK3sXmt1Sgtro%3D, PID: 8218220
    • Loida PJ, Sligar SG (1993) Molecular recognition in cytochrome P-450: mechanism for the control of uncoupling reactions. Biochemistry 32(43):11530–11538. https://doi.org/10.1021/bi00094a009
    • (1993) Biochemistry , vol.32 , Issue.43 , pp. 11530-11538
    • Loida, P.J.1    Sligar, S.G.2
  • 28
    • 77952542916 scopus 로고    scopus 로고
    • Application of the Amplex red/horseradish peroxidase assay to measure hydrogen peroxide generation by recombinant microsomal enzymes
    • COI: 1:CAS:528:DC%2BC3cXlsFGru74%3D, PID: 20188819
    • Mishin V, Gray JP, Heck DE, Laskin DL, Laskin JD (2010) Application of the Amplex red/horseradish peroxidase assay to measure hydrogen peroxide generation by recombinant microsomal enzymes. Free Radic Biol Med 48(11):1485–1491. https://doi.org/10.1016/j.freeradbiomed.2010.02.030
    • (2010) Free Radic Biol Med , vol.48 , Issue.11 , pp. 1485-1491
    • Mishin, V.1    Gray, J.P.2    Heck, D.E.3    Laskin, D.L.4    Laskin, J.D.5
  • 29
    • 0031588923 scopus 로고    scopus 로고
    • 2 release from activated human leukocytes using a dihydroxyphenoxazine derivative
    • COI: 1:CAS:528:DyaK2sXhslOrs78%3D, PID: 9107302
    • 2 release from activated human leukocytes using a dihydroxyphenoxazine derivative. J Immunol Methods 202(2):133–141. https://doi.org/10.1016/S0022-1759(96)00244-X
    • (1997) J Immunol Methods , vol.202 , Issue.2 , pp. 133-141
    • Mohanty, J.G.1    Jaffe, J.S.2    Schulman, E.S.3    Raible, D.G.4
  • 33
    • 78651165715 scopus 로고
    • The carbon monoxide-biding pigment of liver microsomes
    • COI: 1:CAS:528:DyaF2cXktF2gur4%3D, PID: 14209971
    • Omura T, Sato R (1964) The carbon monoxide-biding pigment of liver microsomes. J Biol Chem 239:2370–2378
    • (1964) J Biol Chem , vol.239 , pp. 2370-2378
    • Omura, T.1    Sato, R.2
  • 34
    • 0032544220 scopus 로고    scopus 로고
    • Electron shuttle between membrane-bound cytochrome P450 3A4 and b5 rules uncoupling mechanisms
    • COI: 1:CAS:528:DyaK1cXkvVGrur4%3D, PID: 9708976
    • Perret A, Pompon D (1998) Electron shuttle between membrane-bound cytochrome P450 3A4 and b5 rules uncoupling mechanisms. Biochemistry 37(33):11412–11424. https://doi.org/10.1021/bi980908q
    • (1998) Biochemistry , vol.37 , Issue.33 , pp. 11412-11424
    • Perret, A.1    Pompon, D.2
  • 35
    • 0242330792 scopus 로고    scopus 로고
    • Regio- and enantioselective alkane hydroxylation with modified cytochrome P450
    • COI: 1:CAS:528:DC%2BD3sXnvFOitrc%3D, PID: 14583039
    • Peters MW, Meinhold P, Glieder A, Arnold FH (2003) Regio- and enantioselective alkane hydroxylation with modified cytochrome P450. J Am Chem Soc 125(44):13442–13450. https://doi.org/10.1021/ja0303790
    • (2003) J Am Chem Soc , vol.125 , Issue.44 , pp. 13442-13450
    • Peters, M.W.1    Meinhold, P.2    Glieder, A.3    Arnold, F.H.4
  • 36
    • 84883272014 scopus 로고    scopus 로고
    • Biocatalysis in organic chemistry and biotechnology: past, present, and future
    • COI: 1:CAS:528:DC%2BC3sXht1CltLnO, PID: 23930719
    • Reetz MT (2013) Biocatalysis in organic chemistry and biotechnology: past, present, and future. J Am Chem Soc 135(34):12480–12496. https://doi.org/10.1021/ja405051f
    • (2013) J Am Chem Soc , vol.135 , Issue.34 , pp. 12480-12496
    • Reetz, M.T.1
  • 37
    • 85020373991 scopus 로고    scopus 로고
    • Mapping of enzyme kinetics on a microfluidic device
    • PID: 27082243
    • Rho HS, Hanke AT, Ottens M, Gardeniers H (2016) Mapping of enzyme kinetics on a microfluidic device. PLoS One 11(4):e0153437. https://doi.org/10.1371/journal.pone.0153437
    • (2016) PLoS One , vol.11 , Issue.4
    • Rho, H.S.1    Hanke, A.T.2    Ottens, M.3    Gardeniers, H.4
  • 38
    • 0344348884 scopus 로고    scopus 로고
    • A continuous spectrophotometric assay for P450 BM-3, a fatty acid hydroxylating enzyme, and its mutant F87A
    • COI: 1:CAS:528:DyaK1MXis1Kmu7o%3D, PID: 10222011
    • Schwaneberg U, Schmidt-Dannert C, Schmitt J, Schmid RD (1999) A continuous spectrophotometric assay for P450 BM-3, a fatty acid hydroxylating enzyme, and its mutant F87A. Anal Biochem 269(2):359–366. https://doi.org/10.1006/abio.1999.4047
    • (1999) Anal Biochem , vol.269 , Issue.2 , pp. 359-366
    • Schwaneberg, U.1    Schmidt-Dannert, C.2    Schmitt, J.3    Schmid, R.D.4
  • 39
    • 0038676413 scopus 로고    scopus 로고
    • Measurement of enzyme kinetics using a continuous-flow microfluidic system
    • Seong GH, Heo J, Crooks RM (2003) Measurement of enzyme kinetics using a continuous-flow microfluidic system. Anal Chem 75(13):5206–5212. https://doi.org/10.1021/ac034155b
    • (2003) Anal Chem , vol.75 , Issue.13 , pp. 5206-5212
    • Seong, G.H.1    Heo, J.2    Crooks, R.M.3
  • 40
    • 85018477464 scopus 로고    scopus 로고
    • Role of thiolate ligand in spin state and redox switching in the cytochrome P450 catalytic cycle
    • COI: 1:CAS:528:DC%2BC2sXkvFemsbo%3D, PID: 28350457
    • Suzuki H, Inabe K, Shirakawa Y, Umezawa N, Kato N, Higuchi T (2017) Role of thiolate ligand in spin state and redox switching in the cytochrome P450 catalytic cycle. Inorg Chem 56(8):4245–4248. https://doi.org/10.1021/acs.inorgchem.6b02499
    • (2017) Inorg Chem , vol.56 , Issue.8 , pp. 4245-4248
    • Suzuki, H.1    Inabe, K.2    Shirakawa, Y.3    Umezawa, N.4    Kato, N.5    Higuchi, T.6
  • 41
    • 0036136872 scopus 로고    scopus 로고
    • High throughput assay for cytochrome P450 BM3 for screening libraries of substrates and combinatorial mutants
    • COI: 1:CAS:528:DC%2BD3MXptVSmu74%3D, PID: 11742743
    • Tsotsou GE, Edward A, Cass G, Gilardi G (2002) High throughput assay for cytochrome P450 BM3 for screening libraries of substrates and combinatorial mutants. Biosens Bioelectron 17(1-2):119–131. https://doi.org/10.1016/s0956-5663(01)00285-8
    • (2002) Biosens Bioelectron , vol.17 , Issue.1-2 , pp. 119-131
    • Tsotsou, G.E.1    Edward, A.2    Cass, G.3    Gilardi, G.4
  • 42
    • 2442472003 scopus 로고    scopus 로고
    • Microbial P450 enzymes in biotechnology
    • COI: 1:CAS:528:DC%2BD2cXjt1ChsL4%3D, PID: 14716467
    • Urlacher VB, Lutz-Wahl S, Schmid RD (2004) Microbial P450 enzymes in biotechnology. Appl Microbiol Biotechnol 64(3):317–325. https://doi.org/10.1007/s00253-003-1514-1
    • (2004) Appl Microbiol Biotechnol , vol.64 , Issue.3 , pp. 317-325
    • Urlacher, V.B.1    Lutz-Wahl, S.2    Schmid, R.D.3
  • 43
    • 0242500462 scopus 로고    scopus 로고
    • Practical issues in the application of oxygenases
    • PID: 12679065
    • Van Beilen JB, Duetz WA, Schmid A, Witholt B (2003) Practical issues in the application of oxygenases. Trends Biotechnol 21(4):170–177. https://doi.org/10.1016/S0167-7799(03)00032-5
    • (2003) Trends Biotechnol , vol.21 , Issue.4 , pp. 170-177
    • Van Beilen, J.B.1    Duetz, W.A.2    Schmid, A.3    Witholt, B.4
  • 44
    • 34248347907 scopus 로고    scopus 로고
    • Stochastic simulations of the cytochrome P450 catalytic cycle
    • COI: 1:CAS:528:DC%2BD2sXjs1Oqurs%3D, PID: 17402779
    • Wang Y, Li Y, Wang B (2007) Stochastic simulations of the cytochrome P450 catalytic cycle. J Phys Chem B 111(16):4251–4260. https://doi.org/10.1021/jp071222n
    • (2007) J Phys Chem B , vol.111 , Issue.16 , pp. 4251-4260
    • Wang, Y.1    Li, Y.2    Wang, B.3
  • 45
    • 0034572736 scopus 로고    scopus 로고
    • Cytochromes P450: a success story
    • Werck-Reichhart D, Feyereisen R (2000) Cytochromes P450: a success story. Genome Biol 1(6):3003.1–3003.9. https://doi.org/10.1186/gb-2000-1-6-reviews3003
    • (2000) Genome Biol , vol.1 , Issue.6 , pp. 3003.1-3003.9
    • Werck-Reichhart, D.1    Feyereisen, R.2
  • 46
    • 84855952259 scopus 로고    scopus 로고
    • P450 BM3 (CYP102A1): connecting the dots
    • COI: 1:CAS:528:DC%2BC38Xns1Oquw%3D%3D, PID: 22008827
    • Whitehouse CJC, Bell SG, Wong L-L (2012) P450 BM3 (CYP102A1): connecting the dots. Chem Soc Rev 41(3):1218–1260. https://doi.org/10.1039/C1CS15192D
    • (2012) Chem Soc Rev , vol.41 , Issue.3 , pp. 1218-1260
    • Whitehouse, C.J.C.1    Bell, S.G.2    Wong, L.-L.3
  • 47
    • 4444268690 scopus 로고    scopus 로고
    • Mechanisms that regulate production of reactive oxygen species by cytochrome P 450
    • COI: 1:CAS:528:DC%2BD2cXnsFGgurY%3D, PID: 15364547
    • Zangar RC, Davydov DR, Verma S (2004) Mechanisms that regulate production of reactive oxygen species by cytochrome P 450. Toxicol Appl Pharmacol 199(3):316–331. https://doi.org/10.1016/j.taap.2004.01.018
    • (2004) Toxicol Appl Pharmacol , vol.199 , Issue.3 , pp. 316-331
    • Zangar, R.C.1    Davydov, D.R.2    Verma, S.3
  • 48
    • 77949832008 scopus 로고    scopus 로고
    • Towards preparative scale steroid hydroxylation with cytochrome P450 monooxygenase CYP106A2
    • COI: 1:CAS:528:DC%2BC3cXjs1Olsbg%3D, PID: 20183841
    • Zehentgruber D, Hannemann F, Bleif S, Bernhardt R, Lütz S (2010) Towards preparative scale steroid hydroxylation with cytochrome P450 monooxygenase CYP106A2. Chembiochem 11(5):713–721. https://doi.org/10.1002/cbic.200900706
    • (2010) Chembiochem , vol.11 , Issue.5 , pp. 713-721
    • Zehentgruber, D.1    Hannemann, F.2    Bleif, S.3    Bernhardt, R.4    Lütz, S.5
  • 49
    • 85047686583 scopus 로고    scopus 로고
    • Cytochrome P450 reaction-phenotyping: an industrial perspective
    • COI: 1:CAS:528:DC%2BD2sXhtFyqsrnL, PID: 17916054
    • Zhang H, Davis CD, Sinz MW, Rodrigues AD (2007) Cytochrome P450 reaction-phenotyping: an industrial perspective. Expert Opin Drug Metab Toxicol 3(5):667–687. https://doi.org/10.1517/17425255.3.5.667
    • (2007) Expert Opin Drug Metab Toxicol , vol.3 , Issue.5 , pp. 667-687
    • Zhang, H.1    Davis, C.D.2    Sinz, M.W.3    Rodrigues, A.D.4
  • 50
    • 84864929834 scopus 로고    scopus 로고
    • Photooxidation of Amplex Red to resorufin: implications of exposing the Amplex Red assay to light
    • Zhao B, Summers FA, Mason RP (2013) Photooxidation of Amplex Red to resorufin: implications of exposing the Amplex Red assay to light. Free Radic Biol Med 53(5):1080–1087. https://doi.org/10.1016/j.freeradbiomed.2012.06.034
    • (2013) Free Radic Biol Med , vol.53 , Issue.5 , pp. 1080-1087
    • Zhao, B.1    Summers, F.A.2    Mason, R.P.3
  • 51
    • 0031573401 scopus 로고    scopus 로고
    • A stable nonfluorescent derivative of resorufin for the fluorometric determination of trace hydrogen peroxide: applications in detecting the activity of phagocyte NADPH oxidase and other oxidases
    • COI: 1:CAS:528:DyaK2sXnsFahsr4%3D, PID: 9367498
    • Zhou M, Diwu Z, Panchuk-Voloshina N, Haugland RP (1997) A stable nonfluorescent derivative of resorufin for the fluorometric determination of trace hydrogen peroxide: applications in detecting the activity of phagocyte NADPH oxidase and other oxidases. Anal Biochem 253(2):162–168. https://doi.org/10.1006/abio.1997.2391
    • (1997) Anal Biochem , vol.253 , Issue.2 , pp. 162-168
    • Zhou, M.1    Diwu, Z.2    Panchuk-Voloshina, N.3    Haugland, R.P.4
  • 52
    • 84930641416 scopus 로고    scopus 로고
    • Ultra-high-throughput screening of an in vitro-synthesized horseradish peroxidase displayed on microbeads using cell sorter
    • Zhu B, Mizoguchi T, Kojima T, Nakano H (2015) Ultra-high-throughput screening of an in vitro-synthesized horseradish peroxidase displayed on microbeads using cell sorter. PLoS One 10(5):1–17. https://doi.org/10.1371/journal.pone.0127479
    • (2015) PLoS One , vol.10 , Issue.5 , pp. 1-17
    • Zhu, B.1    Mizoguchi, T.2    Kojima, T.3    Nakano, H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.