메뉴 건너뛰기




Volumn 9, Issue 5, 2014, Pages

The structural and functional basis of catalysis mediated by NAD(P)H:acceptor Oxidoreductase (FerB) of Paracoccus denitrificans

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; APOENZYME; DIMER; FERB PROTEIN; FLAVINE MONONUCLEOTIDE; FLAVOPROTEIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; TETRAMER; UNCLASSIFIED DRUG; WATER; AMINO ACID; BACTERIAL PROTEIN; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; OXIDOREDUCTASE; PROTEIN BINDING; RIBOFLAVIN DERIVATIVE;

EID: 84901207700     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0096262     Document Type: Article
Times cited : (22)

References (46)
  • 2
    • 33751348735 scopus 로고    scopus 로고
    • Bacterial pathways for degradation of nitroaromatics
    • DOI 10.1039/b502796a
    • Symons ZC, Bruce NC (2006) Bacterial pathways for degradation of nitroaromatics. Nat Prod Rep 23: 845-850. (Pubitemid 44808989)
    • (2006) Natural Product Reports , vol.23 , Issue.6 , pp. 845-850
    • Symons, Z.C.1    Bruce, N.C.2
  • 5
    • 0842330593 scopus 로고    scopus 로고
    • Isolation and biochemical characterization of two soluble iron(III) reductases from Paracoccus denitrificans
    • DOI 10.1046/j.1432-1033.2003.03957.x
    • Mazoch J, Tesarik R, Sedlacek V, Kucera I, Turanek J (2004) Isolation and biochemical characterization of two soluble iron(III) reductases from Paracoccus denitrificans. Eur J Biochem 271: 553-562. (Pubitemid 38183629)
    • (2004) European Journal of Biochemistry , vol.271 , Issue.3 , pp. 553-562
    • Mazoch, J.1    Tesarik, R.2    Sedlacek, V.3    Kucera, I.4    Turanek, J.5
  • 6
    • 79952048197 scopus 로고    scopus 로고
    • Chromate reductase activity of the Paracoccus denitrificans ferric reductase B (FerB) protein and its physiological relevance
    • Sedlacek V, Kucera I (2010) Chromate reductase activity of the Paracoccus denitrificans ferric reductase B (FerB) protein and its physiological relevance. Arch Microbiol 192: 919-926.
    • (2010) Arch Microbiol , vol.192 , pp. 919-926
    • Sedlacek, V.1    Kucera, I.2
  • 7
    • 59849085116 scopus 로고    scopus 로고
    • Characterization of the quinone reductase activity of the ferric reductase B protein from Paracoccus denitrificans
    • Sedlacek V, van Spanning RJ, Kucera I (2009) Characterization of the quinone reductase activity of the ferric reductase B protein from Paracoccus denitrificans. Arch Biochem Biophys 483: 29-36.
    • (2009) Arch Biochem Biophys , vol.483 , pp. 29-36
    • Sedlacek, V.1    Van Spanning, R.J.2    Kucera, I.3
  • 9
    • 68749106118 scopus 로고    scopus 로고
    • New roles of flavoproteins in molecular cell biology: An unexpected role for quinone reductases as regulators of proteasomal degradation
    • Sollner S, Macheroux P (2009) New roles of flavoproteins in molecular cell biology: an unexpected role for quinone reductases as regulators of proteasomal degradation. FEBS J 276: 4313-4324.
    • (2009) FEBS J , vol.276 , pp. 4313-4324
    • Sollner, S.1    Macheroux, P.2
  • 12
    • 77950848166 scopus 로고    scopus 로고
    • Crystallization and initial X-ray diffraction studies of the flavoenzyme NAD(P)H:(acceptor) oxidoreductase (FerB) from the soil bacterium Paracoccus denitrificans
    • Klumpler T, Sedlacek V, Marek J, Wimmerova M, Kucera I (2010) Crystallization and initial X-ray diffraction studies of the flavoenzyme NAD(P)H:(acceptor) oxidoreductase (FerB) from the soil bacterium Paracoccus denitrificans. Acta Crystallogr Sect F Struct Biol Cryst Commun 66: 431-434.
    • (2010) Acta Crystallogr Sect F Struct Biol Cryst Commun , vol.66 , pp. 431-434
    • Klumpler, T.1    Sedlacek, V.2    Marek, J.3    Wimmerova, M.4    Kucera, I.5
  • 13
    • 70349459615 scopus 로고    scopus 로고
    • Heterologous expression and molecular characterization of the NAD(P)H:Acceptor oxidoreductase (FerB) of Paracoccus denitrificans
    • Tesarik R, Sedlacek V, Plockova J, Wimmerova M, Turanek J, et al. (2009) Heterologous expression and molecular characterization of the NAD(P)H:acceptor oxidoreductase (FerB) of Paracoccus denitrificans. Protein Expr Purif 68: 233-238.
    • (2009) Protein Expr Purif , vol.68 , pp. 233-238
    • Tesarik, R.1    Sedlacek, V.2    Plockova, J.3    Wimmerova, M.4    Turanek, J.5
  • 14
    • 23844492576 scopus 로고    scopus 로고
    • Auto-Rickshaw: An automated crystal structure determination platform as an efficient tool for the validation of an X-ray diffraction experiment
    • DOI 10.1107/S0907444905001307
    • Panjikar S, Parthasarathy V, Lamzin VS, Weiss MS, Tucker PA (2005) Autorickshaw: an automated crystal structure determination platform as an efficient tool for the validation of an X-ray diffraction experiment. Acta Crystallogr D Biol Crystallogr 61: 449-457. (Pubitemid 43934605)
    • (2005) Acta Crystallographica Section D: Biological Crystallography , vol.61 , Issue.4 , pp. 449-457
    • Panjikar, S.1    Parthasarathy, V.2    Lamzin, V.S.3    Weiss, M.S.4    Tucker, P.A.5
  • 18
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: Conservation mapping in 3D
    • Holm L, Rosenstrom P (2010) Dali server: conservation mapping in 3D. Nucleic Acids Res 38: W545-549.
    • (2010) Nucleic Acids Res , vol.38
    • Holm, L.1    Rosenstrom, P.2
  • 19
    • 0029185933 scopus 로고
    • CRYSOL - A program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates
    • DOI 10.1107/S0021889895007047
    • Svergun D, Barberato C, Koch MHJ (1995) CRYSOL - A program to evaluate x-ray solution scattering of biological macromolecules from atomic coordinates. J Appl Crystallogr 28: 768-773. (Pubitemid 3014671)
    • (1995) Journal of Applied Crystallography , vol.28 , Issue.6 , pp. 768-773
    • Svergun, D.1    Barberato, C.2    Koch, M.H.3
  • 21
    • 84859782518 scopus 로고    scopus 로고
    • New developments in the ATSAS program package for small-angle scattering data analysis
    • Petoukhov MV, Franke D, Shkumatov AV, Tria G, Kikhney AG, et al. (2012) New developments in the ATSAS program package for small-angle scattering data analysis. J Appl Crystallogr 45: 342-350.
    • (2012) J Appl Crystallogr , vol.45 , pp. 342-350
    • Petoukhov, M.V.1    Franke, D.2    Shkumatov, A.V.3    Tria, G.4    Kikhney, A.G.5
  • 23
    • 0002435359 scopus 로고
    • A simple method for the determination of redox potentials
    • Curti B, Ronchi S, Zanetti G, editors. Berlin: de Gruyter W.
    • Massey V (1990) A simple method for the determination of redox potentials. In: Curti B, Ronchi S, Zanetti G, editors. Flavins and Flavoproteins. Berlin: de Gruyter W. pp. 59-66.
    • (1990) Flavins and Flavoproteins , pp. 59-66
    • Massey, V.1
  • 24
    • 34548232365 scopus 로고    scopus 로고
    • Inference of Macromolecular Assemblies from Crystalline State
    • DOI 10.1016/j.jmb.2007.05.022, PII S0022283607006420
    • Krissinel E, Henrick K (2007) Inference of macromolecular assemblies from crystalline state. J Mol Biol 372: 774-797. (Pubitemid 47321791)
    • (2007) Journal of Molecular Biology , vol.372 , Issue.3 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 26
    • 84864713319 scopus 로고    scopus 로고
    • Structure determination and functional analysis of a chromate reductase from Gluconacetobacter hansenii
    • Jin H, Zhang Y, Buchko GW, Varnum SM, Robinson H, et al. (2012) Structure determination and functional analysis of a chromate reductase from Gluconacetobacter hansenii. PloS one 7: e42432.
    • (2012) PloS One , vol.7
    • Jin, H.1    Zhang, Y.2    Buchko, G.W.3    Varnum, S.M.4    Robinson, H.5
  • 27
    • 33646341791 scopus 로고    scopus 로고
    • Structure determination of an FMN reductase from Pseudomonas aeruginosa PA01 using sulfur anomalous signal
    • Agarwal R, Bonanno JB, Burley SK, Swaminathan S (2006) Structure determination of an FMN reductase from Pseudomonas aeruginosa PA01 using sulfur anomalous signal. Acta Crystallogr D Biol Crystallogr 62: 383-391.
    • (2006) Acta Crystallogr D Biol Crystallogr , vol.62 , pp. 383-391
    • Agarwal, R.1    Bonanno, J.B.2    Burley, S.K.3    Swaminathan, S.4
  • 28
    • 77953522703 scopus 로고    scopus 로고
    • Tracking flavin conformations in protein crystal structures with Raman spectroscopy and QM/MM calculations
    • Rohr AK, Hersleth HP, Andersson KK (2010) Tracking flavin conformations in protein crystal structures with Raman spectroscopy and QM/MM calculations. Angew Chem Int Ed Engl 49: 2324-2327.
    • (2010) Angew Chem Int Ed Engl , vol.49 , pp. 2324-2327
    • Rohr, A.K.1    Hersleth, H.P.2    Andersson, K.K.3
  • 30
    • 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
  • 31
    • 0031406030 scopus 로고    scopus 로고
    • Redox potentials and quinone reductase activity of L-aspartate oxidase from Escherichia coli
    • DOI 10.1021/bi970751m
    • Tedeschi G, Zetta L, Negri A, Mortarino M, Ceciliani F, et al. (1997) Redox potentials and quinone reductase activity of L-aspartate oxidase from Escherichia coli. Biochemistry 36: 16221-16230. (Pubitemid 28065037)
    • (1997) Biochemistry , vol.36 , Issue.51 , pp. 16221-16230
    • Tedeschi, G.1    Zetta, L.2    Negri, A.3    Mortarino, M.4    Ceciliani, F.5    Ronchi, S.6
  • 32
    • 0032610884 scopus 로고    scopus 로고
    • Potentiometric measurement of oxidation-reduction potentials
    • Mayhew SG (1999) Potentiometric measurement of oxidation-reduction potentials. Methods Mol Biol 131: 49-59.
    • (1999) Methods Mol Biol , vol.131 , pp. 49-59
    • Mayhew, S.G.1
  • 34
    • 0032516896 scopus 로고    scopus 로고
    • Biochemical characterization of WrbA, founding member of a new family of multimeric flavodoxin-like proteins
    • DOI 10.1074/jbc.273.33.20960
    • Grandori R, Khalifah P, Boice JA, Fairman R, Giovanielli K, et al. (1998) Biochemical characterization of WrbA, founding member of a new family of multimeric flavodoxin-like proteins. J Biol Chem 273: 20960-20966. (Pubitemid 28385378)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.33 , pp. 20960-20966
    • Grandori, R.1    Khalifah, P.2    Boice, J.A.3    Fairman, R.4    Giovanielli, K.5    Carey, J.6
  • 35
    • 33745149270 scopus 로고    scopus 로고
    • Why WrbA is weaker than flavodoxin in binding FMN. A molecular modeling study
    • Ji HF, Shen L, Carey J, Grandori R, Zhang HY (2006) Why WrbA is weaker than flavodoxin in binding FMN. A molecular modeling study. Theochem-J Mol Struct 764: 155-160.
    • (2006) Theochem-J Mol Struct , vol.764 , pp. 155-160
    • Ji, H.F.1    Shen, L.2    Carey, J.3    Grandori, R.4    Zhang, H.Y.5
  • 36
    • 33646052947 scopus 로고    scopus 로고
    • Flavodoxins: Sequence, folding, binding, function and beyond
    • Sancho J (2006) Flavodoxins: sequence, folding, binding, function and beyond. Cell Mol Life Sci 63: 855-864.
    • (2006) Cell Mol Life Sci , vol.63 , pp. 855-864
    • Sancho, J.1
  • 37
    • 57649136394 scopus 로고    scopus 로고
    • Crystal structures of NADH:FMN oxidoreductase (EmoB) at different stages of catalysis
    • Nissen MS, Youn B, Knowles BD, Ballinger JW, Jun SY, et al. (2008) Crystal structures of NADH:FMN oxidoreductase (EmoB) at different stages of catalysis. J Biol Chem 283: 28710-28720.
    • (2008) J Biol Chem , vol.283 , pp. 28710-28720
    • Nissen, M.S.1    Youn, B.2    Knowles, B.D.3    Ballinger, J.W.4    Jun, S.Y.5
  • 38
    • 0029845902 scopus 로고    scopus 로고
    • The nicotinamide dinucleotide binding motif: A comparison of nucleotide binding proteins
    • Bellamacina CR (1996) The nicotinamide dinucleotide binding motif: A comparison of nucleotide binding proteins. Faseb J 10: 1257-1269.
    • (1996) Faseb J , vol.10 , pp. 1257-1269
    • Bellamacina, C.R.1
  • 39
    • 0034161331 scopus 로고    scopus 로고
    • Flavoenzymes: Diverse catalysts with recurrent features
    • DOI 10.1016/S0968-0004(99)01533-9, PII S0968000499015339
    • Fraaije MW, Mattevi A (2000) Flavoenzymes: diverse catalysts with recurrent features. Trends Biochem Sci 25: 126-132. (Pubitemid 30122424)
    • (2000) Trends in Biochemical Sciences , vol.25 , Issue.3 , pp. 126-132
    • Fraaije, M.W.1    Mattevi, A.2
  • 40
    • 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 U S A 92: 8846-8850.
    • (1995) Proc Natl Acad Sci U S a , vol.92 , pp. 8846-8850
    • Li, R.1    Bianchet, M.A.2    Talalay, P.3    Amzel, L.M.4
  • 41
    • 0035800760 scopus 로고    scopus 로고
    • NADPH-cytochrome P450 oxidoreductase. Structural basis for hydride and electron transfer
    • Hubbard PA, Shen AL, Paschke R, Kasper CB, Kim JJ (2001) NADPH-cytochrome P450 oxidoreductase. Structural basis for hydride and electron transfer. J Biol Chem 276: 29163-29170.
    • (2001) J Biol Chem , vol.276 , pp. 29163-29170
    • Hubbard, P.A.1    Shen, A.L.2    Paschke, R.3    Kasper, C.B.4    Kim, J.J.5
  • 42
    • 0141621166 scopus 로고    scopus 로고
    • The crystal structure and reaction mechanism of Escherichia coli 2,4-dienoyl-CoA reductase
    • DOI 10.1074/jbc.M304642200
    • Hubbard PA, Liang X, Schulz H, Kim JJ (2003) The crystal structure and reaction mechanism of Escherichia coli 2,4-dienoyl-CoA reductase. J Biol Chem 278: 37553-37560. (Pubitemid 37175277)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.39 , pp. 37553-37560
    • Hubbard, P.A.1    Liang, X.2    Schulz, H.3    Kim, J.-J.P.4
  • 44
    • 0034405702 scopus 로고    scopus 로고
    • Crystal structure of the peptidyl-cysteine decarboxylase EpiD complexed with a pentapeptide substrate
    • Blaesse M, Kupke T, Huber R, Steinbacher S (2000) Crystal structure of the peptidyl-cysteine decarboxylase EpiD complexed with a pentapeptide substrate. Embo J 19: 6299-6310.
    • (2000) Embo J , vol.19 , pp. 6299-6310
    • Blaesse, M.1    Kupke, T.2    Huber, R.3    Steinbacher, S.4
  • 45
    • 33745044453 scopus 로고    scopus 로고
    • Characterization of a thermostable NADPH:FMN oxidoreductase from the mesophilic bacterium Bacillus subtilis
    • DOI 10.1021/bi052478r
    • Deller S, Sollner S, Trenker-El-Toukhy R, Jelesarov I, Gubitz GM, et al. (2006) Characterization of a thermostable NADPH:FMN oxidoreductase from the mesophilic bacterium Bacillus subtilis. Biochemistry 45: 7083-7091. (Pubitemid 43877396)
    • (2006) Biochemistry , vol.45 , Issue.23 , pp. 7083-7091
    • Deller, S.1    Sollner, S.2    Trenker-El-Toukhy, R.3    Jelesarov, I.4    Gubitz, G.M.5    Macheroux, P.6
  • 46
    • 0030776076 scopus 로고    scopus 로고
    • 1H NMR shift measurements
    • DOI 10.1016/S0301-4622(97)00012-4, PII S0301462297000124
    • Bastian M, Sigel H (1997) The self-association of flavin mononucleotide (FMN(2-)) as determined by (1)H NMR shift measurements. Biophys Chem 67: 27-34. (Pubitemid 27512968)
    • (1997) Biophysical Chemistry , vol.67 , Issue.1-3 , pp. 27-34
    • Bastian, M.1    Sigel, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.