메뉴 건너뛰기




Volumn 312, Issue , 2012, Pages 87-96

Characterization of cofactors, substrates and inhibitor binding to flavoenzyme quinone reductase 2 by automated supramolecular nano-electrospray ionization mass spectrometry

Author keywords

Flavoprotein; Melatonin; Quinone reductase; Resveratrol; Supramolecular mass spectrometry

Indexed keywords


EID: 84857058412     PISSN: 13873806     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ijms.2011.07.011     Document Type: Article
Times cited : (11)

References (35)
  • 1
    • 28344433705 scopus 로고    scopus 로고
    • NRH:quinone reductase 2: An enzyme of surprises and mysteries
    • DOI 10.1016/j.bcp.2005.09.019, PII S0006295205005915
    • F. Vella, G. Ferry, P. Delagrange, and J.A. Boutin NRH:quinone reductase 2: an enzyme of surprises and mysteries Biochem. Pharmacol. 71 2005 1 12 (Pubitemid 41715231)
    • (2005) Biochemical Pharmacology , vol.71 , Issue.1-2 , pp. 1-12
    • Vella, F.1    Ferry, G.2    Delagrange, P.3    Boutin, J.A.4
  • 2
    • 0034527964 scopus 로고    scopus 로고
    • NRH:quinone oxidoreductase2 (NQO2)
    • DOI 10.1016/S0009-2797(00)00200-3, PII S0009279700002003
    • D.J. Long, and A.K. Jaiswal NRH:quinone oxidoreductase2 (NQO2) Chem. Biol. Interact. 129 2000 99 112 (Pubitemid 32061056)
    • (2000) Chemico-Biological Interactions , vol.129 , Issue.1-2 , pp. 99-112
    • Long II, D.J.1    Jaiswal, A.K.2
  • 3
    • 0025018844 scopus 로고
    • 2 gene locus on chromosome 6
    • A.K. Jaiswal, P. Burnett, M. Adesnik, and O.W. McBride Nucleotide deduced amino acid sequence of a human cDNA (NQO2) corresponding to a second member of the NAD(P)H:quinone oxidoreductase gene family. Extensive polymorphism at the NQO2 gene locus on chromosome 6 Biochemistry 29 1990 1899 1906 (Pubitemid 20074738)
    • (1990) Biochemistry , vol.29 , Issue.7 , pp. 1899-1906
    • Jaiswal, A.K.1    Burnett, P.2    Adesnik, M.3    McBride, O.W.4
  • 4
    • 0000665443 scopus 로고
    • Enzymatic oxidation of some non-phosphorylated derivatives of dihydronicotinamide
    • S. Liao, and H.G. Williams-Ashman Enzymatic oxidation of some non-phosphorylated derivatives of dihydronicotinamide Biochem. Biophys. Res. Commun. 4 1961 208 213
    • (1961) Biochem. Biophys. Res. Commun. , vol.4 , pp. 208-213
    • Liao, S.1    Williams-Ashman, H.G.2
  • 6
    • 0037195924 scopus 로고    scopus 로고
    • Disruption of dihydronicotinamide riboside:quinone oxidoreductase 2 (NQO2) leads to myeloid hyperplasia of bone marrow and decreased sensitivity to menadione toxicity
    • DOI 10.1074/jbc.M208675200
    • D.J. Long, K. Iskander, A. Gaikwad, M. Arin, D.R. Roop, R. Knox, R. Barrios, and A.K. Jaiswal Disruption of dihydronicotinamide riboside:quinone oxidoreductase 2 (NQO2) leads to myeloid hyperplasia of bone marrow and decreased sensitivity to menadione toxicity J. Biol. Chem. 277 2002 46131 46139 (Pubitemid 35417602)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.48 , pp. 46131-46139
    • Long II, D.J.1    Iskander, K.2    Gaikwad, A.3    Arin, M.4    Roop, D.R.5    Knox, R.6    Barrios, R.7    Jaiswal, A.K.8
  • 8
    • 9644278439 scopus 로고    scopus 로고
    • 3
    • DOI 10.1016/j.febslet.2004.10.083, PII S0014579304013493
    • F. Mailliet, G. Ferry, F. Vella, K. Thiam, P. Delagrange, and J.A. Boutin Organs from mice deleted for NRH:quinone oxidoreductase 2 are deprived of the melatonin binding site MT3 FEBS Lett. 578 2004 116 120 (Pubitemid 39576111)
    • (2004) FEBS Letters , vol.578 , Issue.1-2 , pp. 116-120
    • Mailliet, F.1    Ferry, G.2    Vella, F.3    Thiam, K.4    Delagrange, P.5    Boutin, J.A.6
  • 10
    • 0033520090 scopus 로고    scopus 로고
    • Crystal structure of human quinone reductase type 2, a metalloflavoprotein
    • C.E. Foster, M.A. Bianchet, P. Talalay, Q. Zhao, and L.M. Amzel Crystal structure of human quinone reductase type 2, a metalloflavoprotein, Biochemistry 38 1999 9881 9886
    • (1999) Biochemistry , vol.38 , pp. 9881-9886
    • Foster, C.E.1    Bianchet, M.A.2    Talalay, P.3    Zhao, Q.4    Amzel, L.M.5
  • 11
    • 4444265496 scopus 로고    scopus 로고
    • Kinetic Mechanism of Quinone Oxidoreductase 2 and Its Inhibition by the Antimalarial Quinolines
    • DOI 10.1021/bi035923w
    • J.J Kwiek, T.A. Haystead, and J. Rudolph Kinetic mechanism of quinone oxidoreductase 2 and its inhibition by the antimalarial quinolines Biochemistry 43 2004 4538 4547 (Pubitemid 38500583)
    • (2004) Biochemistry , vol.43 , Issue.15 , pp. 4538-4547
    • Kwiek, J.J.1    Haystead, T.A.J.2    Rudolph, J.3
  • 12
    • 40949107656 scopus 로고    scopus 로고
    • Structure, function, and mechanism of cytosolic quinone reductases
    • M.A. Bianchet, S.B. Erdemli, and L.M. Amzel Structure, function, and mechanism of cytosolic quinone reductases Vitam. Horm. 78 2008 63 84
    • (2008) Vitam. Horm. , vol.78 , pp. 63-84
    • Bianchet, M.A.1    Erdemli, S.B.2    Amzel, L.M.3
  • 13
    • 4444267291 scopus 로고    scopus 로고
    • Crystal structure of quinone reductase 2 in complex with resveratrol
    • DOI 10.1021/bi049162o
    • L. Buryanovskyy, Y. Fu, M. Boyd, Y. Ma, T.C. Hsieh, J.M. Wu, and Z. Zhang Crystal structure of quinone reductase 2 in complex with resveratrol Biochemistry 43 2004 11417 11426 (Pubitemid 39186963)
    • (2004) Biochemistry , vol.43 , Issue.36 , pp. 11417-11426
    • Buryanovskyy, L.1    Fu, Y.2    Boyd, M.3    Ma, Y.4    Hsieh, T.-C.5    Wu, J.M.6    Zhang, Z.7
  • 14
    • 24344493957 scopus 로고    scopus 로고
    • Crystal structure of quinone reductase 2 in complex with cancer prodrug CB1954
    • DOI 10.1016/j.bbrc.2005.08.081, PII S0006291X05017882
    • Y. Fu, L. Buryanovskyy, and Z. Zhang Crystal structure of quinone reductase 2 in complex with cancer prodrug CB1954 Biochem. Biophys. Res. Commun. 336 2005 332 338 (Pubitemid 41253438)
    • (2005) Biochemical and Biophysical Research Communications , vol.336 , Issue.1 , pp. 332-338
    • Fu, Y.1    Buryanovskyy, L.2    Zhang, Z.3
  • 15
    • 46249097454 scopus 로고    scopus 로고
    • Kinetic, thermodynamic and X-ray structural insights into the interaction of melatonin and analogues with quinone reductase 2
    • DOI 10.1042/BJ20071373
    • B. Calamini, B.D. Santarsiero, J.A. Boutin, and A.D. Mesecar Kinetic, thermodynamic and X-ray structural insights into the interaction of melatonin and analogues with quinone reductase 2 Biochem. J. 413 2008 81 91 (Pubitemid 351946864)
    • (2008) Biochemical Journal , vol.413 , Issue.1 , pp. 81-91
    • Calamini, B.1    Santarsiero, B.D.2    Boutin, J.A.3    Mesecar, A.D.4
  • 22
    • 0032612239 scopus 로고    scopus 로고
    • Identifying, and F.A.D. quantitating FMN in simple and in iron-sulfur-containing flavoproteins
    • A. Aliverti, B. Curti, M.A. Vanoni, Identifying, and F.A.D. quantitating FMN in simple and in iron-sulfur-containing flavoproteins Methods Mol. Biol. 131 1999 9 23
    • (1999) Methods Mol. Biol. , vol.131 , pp. 9-23
    • Aliverti, A.1    Curti, B.2    Vanoni, M.A.3
  • 23
    • 47249088189 scopus 로고    scopus 로고
    • Melatonin receptors, heterodimerization, signal transduction and binding sites: What's new?
    • DOI 10.1038/bjp.2008.184, PII BJP2008184
    • R. Jockers, P. Maurice, J.A. Boutin, and P. Delagrange Melatonin receptors, heterodimerization, signal transduction and binding sites: what's new? Br. J. Pharmacol. 154 2008 1182 1195 (Pubitemid 351992057)
    • (2008) British Journal of Pharmacology , vol.154 , Issue.6 , pp. 1182-1195
    • Jockers, R.1    Maurice, P.2    Boutin, J.A.3    Delagrange, P.4
  • 24
    • 22844439551 scopus 로고    scopus 로고
    • Molecular tools to study melatonin pathways and actions
    • DOI 10.1016/j.tips.2005.06.006, PII S0165614705001525
    • J.A. Boutin, V. Audinot, G. Ferry, and P. Delagrange Molecular tools to study melatonin pathways and actions Trends Pharmacol. Sci. 26 2005 412 419 (Pubitemid 41039217)
    • (2005) Trends in Pharmacological Sciences , vol.26 , Issue.8 , pp. 412-419
    • Boutin, J.A.1    Audinot, V.2    Ferry, G.3    Delagrange, P.4
  • 25
    • 0028318860 scopus 로고
    • Human NAD(P)H:quinone oxidoreductase 2. Gene structure, activity, and tissue-specific expression
    • A.K. Jaiswal Human NAD(P)H:quinone oxidoreductase 2. Gene structure, activity, and tissue-specific expression J. Biol. Chem. 269 1994 14502 14508
    • (1994) J. Biol. Chem. , vol.269 , pp. 14502-14508
    • Jaiswal, A.K.1
  • 29
    • 64049094455 scopus 로고    scopus 로고
    • Detection and pharmacological modulation of nicotinamide mononucleotide (NMN) in vitro and in vivo
    • L. Formentini, F. Moroni, and A. Chiarugi Detection and pharmacological modulation of nicotinamide mononucleotide (NMN) in vitro and in vivo Biochem. Pharmacol. 77 2009 1612 1620
    • (2009) Biochem. Pharmacol. , vol.77 , pp. 1612-1620
    • Formentini, L.1    Moroni, F.2    Chiarugi, A.3
  • 30
    • 0035894046 scopus 로고    scopus 로고
    • Influence of pressure in the first pumping stage on analyte desolvation and fragmentation in Nano-ESI MS
    • DOI 10.1021/ac010451h
    • A. Schmidt, U. Bahr, and M. Karas Influence of pressure in the first pumping stage on analyte desolvation and fragmentation in nano-ESI MS Anal. Chem. 73 2001 6040 6046 (Pubitemid 34042222)
    • (2001) Analytical Chemistry , vol.73 , Issue.24 , pp. 6040-6046
    • Schmidt, A.1    Bahr, U.2    Karas, M.3
  • 31
    • 0035029535 scopus 로고    scopus 로고
    • The effect of the source pressure on the abundance of ions of noncovalent protein assemblies in an electrospray ionization orthogonal time-of-flight instrument
    • DOI 10.1002/rcm.275
    • N. Tahallah, M. Pinkse, C.S. Maier, and A.J. Heck The effect of the source pressure on the abundance of ions of noncovalent protein assemblies in an electrospray ionization orthogonal time-of-flight instrument Rapid Commun. Mass Spectrom. 15 2001 596 601 (Pubitemid 32391094)
    • (2001) Rapid Communications in Mass Spectrometry , vol.15 , Issue.8 , pp. 596-601
    • Tahallah, N.1    Pinkse, M.2    Maier, C.S.3    Heck, A.J.R.4
  • 32
    • 0036756804 scopus 로고    scopus 로고
    • Electrospray ionization mass spectrometry analysis revealed a ∼310 kDa noncovalent hexamer of HPr kinase/phosphatase from Bacillus subtilis
    • S. Sanglier, H. Ramstrom, J. Haiech, E. Leize, and A. Van Dorsselaer Electrospray ionization mass spectrometry analysis revealed a ∼310 kDa noncovalent hexamer of HPr kinase/phosphatase from Bacillus subtilis Int. J. Mass Spectrom. 219 2002 681 696
    • (2002) Int. J. Mass Spectrom. , vol.219 , pp. 681-696
    • Sanglier, S.1    Ramstrom, H.2    Haiech, J.3    Leize, E.4    Van Dorsselaer, A.5
  • 33
    • 3543008337 scopus 로고    scopus 로고
    • Determination of dissociation constants for protein-ligand complexes by electrospray ionization mass spectrometry
    • DOI 10.1021/ac0497914
    • A. Tjernberg, S. Carno, F. Oliv, K. Benkestock, P.O. Edlund, W.J. Griffiths, and D. Hallen Determination of dissociation constants for protein-ligand complexes by electrospray ionization mass spectrometry Anal. Chem. 76 2004 4325 4331 (Pubitemid 39014001)
    • (2004) Analytical Chemistry , vol.76 , Issue.15 , pp. 4325-4331
    • Tjernberg, A.1    Carno, S.2    Oliv, F.3    Benkestock, K.4    Edlund, P.-O.5    Griffiths, W.J.6    Hallen, D.7
  • 35
    • 79955415835 scopus 로고    scopus 로고
    • Mass spectrometry reveals that the antibiotic simocyclinone D8 binds to DNA gyrase in a "bent-over" conformation: Evidence for positive cooperativity in binding
    • M.J. Edwards, M.A. Williams, A. Maxwell, and A.R. McKay Mass spectrometry reveals that the antibiotic simocyclinone D8 binds to DNA gyrase in a "bent-over" conformation: evidence for positive cooperativity in binding Biochemistry 50 2011 3432 3440
    • (2011) Biochemistry , vol.50 , pp. 3432-3440
    • Edwards, M.J.1    Williams, M.A.2    Maxwell, A.3    McKay, A.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.