메뉴 건너뛰기




Volumn 192, Issue 11, 2010, Pages 919-926

Chromate reductase activity of the Paracoccus denitrificans ferric reductase B (FerB) protein and its physiological relevance

Author keywords

Flavin radical; Flavoenzyme; Metal bioreduction; Oxidative stress

Indexed keywords

BACTERIAL PROTEIN; BETA GALACTOSIDASE; CHROMIC ACID; CITRININ; FERRIC REDUCTASE B PROTEIN; FERRICYANIDE; FLAVOPROTEIN; NITRATE REDUCTASE (NADH); QUERCETIN; UNCLASSIFIED DRUG; CHROMATE REDUCTASE; DRUG DERIVATIVE; FERRIC CITRATE IRON REDUCTASE; FLAVIN SEMIQUINONE; FLAVINE ADENINE NUCLEOTIDE; FLAVINE MONONUCLEOTIDE REDUCTASE; NICOTINAMIDE ADENINE DINUCLEOTIDE; OXIDOREDUCTASE;

EID: 79952048197     PISSN: 03028933     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00203-010-0622-4     Document Type: Article
Times cited : (23)

References (46)
  • 1
    • 3543112699 scopus 로고    scopus 로고
    • Mechanism of chromate reduction by the Escherichia coli protein, NfsA, and the role of different chromate reductases in minimizing oxidative stress during chromate reduction
    • DOI 10.1111/j.1462-2920.2004.00639.x
    • Ackerley DF, Gonzalez CF, Keyhan M, Blake R II, Matin A (2004) Mechanism of chromate reduction by the Escherichia coli protein, NfsA, and the role of different chromate reductases in minimizing oxidative stress during chromate reduction. Environ Microbiol 6:851-860 (Pubitemid 39017268)
    • (2004) Environmental Microbiology , vol.6 , Issue.8 , pp. 851-860
    • Ackerley, D.F.1    Gonzalez, C.F.2    Keyhan, M.3    Blake II, R.4    Matin, A.5
  • 3
    • 33750976704 scopus 로고    scopus 로고
    • Analysis of novel soluble chromate and uranyl reductases and generation of an improved enzyme by directed evolution
    • DOI 10.1128/AEM.01334-06
    • Barak Y, Ackerley DF, Dodge CJ, Banwari L, Alex C, Francis AJ, Matin A (2006) Analysis of novel soluble chromate and uranyl reductases and generation of an improved enzyme by directed evolution. Appl Environ Microbiol 72:7074-7082 (Pubitemid 44748420)
    • (2006) Applied and Environmental Microbiology , vol.72 , Issue.11 , pp. 7074-7082
    • Barak, Y.1    Ackerley, D.F.2    Dodge, C.J.3    Banwari, L.4    Alex, C.5    Francis, A.J.6    Matin, A.7
  • 5
    • 0016753870 scopus 로고
    • A reversibility of active sulphate transport in membrane vesicles of Paracoccus denitrificans
    • Burnell JN, John P, Whatley FR (1975) A reversibility of active sulphate transport in membrane vesicles of Paracoccus denitrificans. Biochem J 150:527-536
    • (1975) Biochem J , vol.150 , pp. 527-536
    • Burnell, J.N.1    John, P.2    Whatley, F.R.3
  • 6
    • 33845972300 scopus 로고    scopus 로고
    • Mechanism of hexavalent chromium detoxification by microorganisms and bioremediation application potential: A review
    • DOI 10.1016/j.ibiod.2006.05.002, PII S096483050600076X
    • Cheung KH, Gu JD (2007) Mechanism of hexavalent chromium detoxification by microorganisms and bioremediation application potential: a review. Int Biodeter Biodegr 59:8-15 (Pubitemid 46043548)
    • (2007) International Biodeterioration and Biodegradation , vol.59 , Issue.1 , pp. 8-15
    • Cheung, K.H.1    Gu, J.-D.2
  • 7
    • 0017615625 scopus 로고
    • Reduction of iron and synthesis of protoheme by Spirillum itersonii and other organisms
    • Dailey HA Jr, Lascelles J (1977) Reduction of iron and synthesis of protoheme by Spirillum itersonii and other organisms. J Bacteriol 129:815-820 (Pubitemid 8043897)
    • (1977) Journal of Bacteriology , vol.129 , Issue.2 , pp. 815-820
    • Dailey Jr., H.A.1    Lascelles, J.2
  • 9
    • 44149106382 scopus 로고    scopus 로고
    • Evaluation of in vitro Cr(VI) reduction potential in cytosolic extracts of three indigenous Bacillus sp. isolated from Cr(VI) polluted industrial landfill
    • Desai C, Jain K, Madamwar D (2008b) Evaluation of in vitro Cr(VI) reduction potential in cytosolic extracts of three indigenous Bacillus sp. isolated from Cr(VI) polluted industrial landfill. Bioresour Technol 99:6059-6069
    • (2008) Bioresour Technol , vol.99 , pp. 6059-6069
    • Desai, C.1    Jain, K.2    Madamwar, D.3
  • 10
    • 0001888973 scopus 로고
    • Isolation and characterization of Paracoccus denitrificans mutants with increased conjugation frequencies and pleiotropic loss of a (nGATCn) DNA-modifying property
    • de Vries GE, Harms N, Hoogendijk J, Stouthamer AH (1989) Isolation and characterization of Paracoccus denitrificans mutants with increased conjugation frequencies and pleiotropic loss of a (nGATCn) DNA-modifying property. Arch Microbiol 152:52-57
    • (1989) Arch Microbiol , vol.152 , pp. 52-57
    • De Vries, G.E.1    Harms, N.2    Hoogendijk, J.3    Stouthamer, A.H.4
  • 11
    • 4243735675 scopus 로고    scopus 로고
    • Molecular mechanisms of Cr(VI)-induced carcinogenesis
    • DOI 10.1023/A:1015975218920
    • Ding M, Shi X (2002) Molecular mechanisms of Cr(VI)-induced carcinogenesis. Mol Cell Biochem 234(235):293-300 (Pubitemid 34777868)
    • (2002) Molecular and Cellular Biochemistry , vol.234-235 , pp. 293-300
    • Ding, M.1    Shi, X.2
  • 14
    • 28844480427 scopus 로고    scopus 로고
    • Whole-genome transcriptional analysis of heavy metal stresses in Caulobacter crescentus
    • DOI 10.1128/JB.187.24.8437-8449.2005
    • Hu P, Brodie EL, Suzuki Y, McAdams HH, Andersen GL (2005) Whole-genome transcriptional analysis of heavy metal stresses in Caulobacter crescentus. J Bacteriol 187:8437-8449 (Pubitemid 41780508)
    • (2005) Journal of Bacteriology , vol.187 , Issue.24 , pp. 8437-8449
    • Hu, P.1    Brodie, E.L.2    Suzuki, Y.3    McAdams, H.H.4    Andersen, G.L.5
  • 15
    • 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, Sedláček V, Marek J, Wimmerová M, Kučera 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    Sedláček, V.2    Marek, J.3    Wimmerová, M.4    Kučera, I.5
  • 16
    • 33947094105 scopus 로고
    • A stable chromium(V) compound. Synthesis, properties, and crystal structure of potassium bis(2-hydroxy-2-methylbutyrato)-oxochromate(V) monohydrate
    • Krumpolc M, DeBoer BG, Roček J (1978) A stable chromium(V) compound. Synthesis, properties, and crystal structure of potassium bis(2-hydroxy-2-methylbutyrato)-oxochromate(V) monohydrate. J Am Chem Soc 100:145-153
    • (1978) J Am Chem Soc , vol.100 , pp. 145-153
    • Krumpolc, M.1    DeBoer, B.G.2    Roček, J.3
  • 17
    • 0023655975 scopus 로고
    • Control of respiration rate in non-growing cells of Paracoccus denitrificans
    • Kučera I, Lampardová L, Dadák V (1987) Control of respiration rate in non-growing cells of Paracoccus denitrificans. Biochem J 246:779-782
    • (1987) Biochem J , vol.246 , pp. 779-782
    • Kučera, I.1    Lampardová, L.2    Dadák, V.3
  • 18
    • 0023933580 scopus 로고
    • Separate binding sites for antimycin and mucidin in the respiratory chain of the bacterium Paracoccus denitrificans and their occurrence in other denitrifying bacteria
    • Kučera I, Hedbávný R, Dadák V (1988) Separate binding sites for antimycin and mucidin in the respiratory chain of the bacterium Paracoccus denitrificans and their occurrence in other denitrifying bacteria. Biochem J 252:905-908
    • (1988) Biochem J , vol.252 , pp. 905-908
    • Kučera, I.1    Hedbávný, R.2    Dadák, V.3
  • 19
    • 0029859863 scopus 로고    scopus 로고
    • DT-diaphorase maintains the reduced state of ubiquinones in lipid vesicles thereby promoting their antioxidant function
    • DOI 10.1016/S0891-5849(96)00294-8
    • Landi L, Fiorentini D, Galli MC, Segura-Aguilar J, Beyer RE (1997) DT-Diaphorase maintains the reduced state of ubiquinones in lipid vesicles thereby promoting their antioxidant function. Free Radic Biol Med 22:329-335 (Pubitemid 26399339)
    • (1996) Free Radical Biology and Medicine , vol.22 , Issue.1-2 , pp. 329-335
    • Landi, L.1    Fiorentini, D.2    Galli, M.C.3    Segura-Aguilar, J.4    Beyer, R.E.5
  • 20
    • 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, Tesařík R, Sedláček V, Kučera I, Turánek 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
  • 23
    • 70349183960 scopus 로고    scopus 로고
    • Capillary zone electrophoresis with field enhanced sample stacking as a tool for targeted metabolome analysis of adenine nucleotides and coenzymes in Paracoccus denitrificans
    • Musilová J, Sedláček V, Kučera I, Glatz Z (2009) Capillary zone electrophoresis with field enhanced sample stacking as a tool for targeted metabolome analysis of adenine nucleotides and coenzymes in Paracoccus denitrificans. J Sep Sci 32:2416-2420
    • (2009) J Sep Sci , vol.32 , pp. 2416-2420
    • Musilová, J.1    Sedláček, V.2    Kučera, I.3    Glatz, Z.4
  • 24
    • 35448934965 scopus 로고    scopus 로고
    • Aerobic Cr(VI) reduction by Thermus scotoductus strain SA-01
    • DOI 10.1111/j.1365-2672.2007.03429.x
    • Opperman DJ, van Heerden E (2007) Aerobic Cr(VI) reduction by Thermus scotoductus strain SA-01. J Appl Microbiol 103:1907-1913 (Pubitemid 47620580)
    • (2007) Journal of Applied Microbiology , vol.103 , Issue.5 , pp. 1907-1913
    • Opperman, D.J.1    Van Heerden, E.2
  • 25
    • 41949115394 scopus 로고    scopus 로고
    • A novel chromate reductase from Thermus scotoductus SA-01 related to old yellow enzyme
    • DOI 10.1128/JB.01766-07
    • Opperman DJ, Piater LA, van Heerden E (2008) A novel chromate reductase from Thermus scotoductus SA-01 related to old yellow enzyme. J Bacteriol 190:3076-3082 (Pubitemid 351508208)
    • (2008) Journal of Bacteriology , vol.190 , Issue.8 , pp. 3076-3082
    • Opperman, D.J.1    Piater, L.A.2    Van Heerden, E.3
  • 26
    • 27744551363 scopus 로고    scopus 로고
    • Reduction of Hexavalent Chromium by Cell-Free Extract of Bacillus sphaericus and 303 Isolated from Serpentine Soil
    • DOI 10.1007/s00284-005-0048-4
    • Pal A, Dutta S, Paul AK (2005) Reduction of hexavalent chromium by cell-free extract of Bacillus sphaericus AND 303 isolated from serpentine soil. Curr Microbiol 51:327-330 (Pubitemid 41586784)
    • (2005) Current Microbiology , vol.51 , Issue.5 , pp. 327-330
    • Pal, A.1    Dutta, S.2    Paul, A.K.3
  • 27
    • 0034021727 scopus 로고    scopus 로고
    • Purification to homogeneity and characterization of a novel Pseudomonas putida chromate reductase
    • DOI 10.1128/AEM.66.5.1788-1795.2000
    • Park CH, Keyhan M, Wielinga B, Fendorf S, Matin A (2000) Purification to homogeneity and characterization of a novel Pseudomonas putida chromate reductase. Appl Environ Microbiol 66:1788-1795 (Pubitemid 30253691)
    • (2000) Applied and Environmental Microbiology , vol.66 , Issue.5 , pp. 1788-1795
    • Park, C.H.1    Keyhan, M.2    Wielinga, B.3    Fendorf, S.4    Matin, A.5
  • 28
    • 33748638376 scopus 로고    scopus 로고
    • The equilibrium between the oxidation of hydrogen peroxide by oxygen and the dismutation of peroxyl or superoxide radicals in aqueous solutions in contact with oxygen
    • Petlicki J, van de Ven TGM (1998) The equilibrium between the oxidation of hydrogen peroxide by oxygen and the dismutation of peroxyl or superoxide radicals in aqueous solutions in contact with oxygen. J Chem Soc Faraday Trans 94:2763-2767 (Pubitemid 128759943)
    • (1998) Journal of the Chemical Society - Faraday Transactions , vol.94 , Issue.18 , pp. 2763-2767
    • Petlicki, J.1    Van De Ven, T.G.M.2
  • 30
    • 67649743513 scopus 로고    scopus 로고
    • Studies on biological reduction of chromate by Streptomyces griseus
    • Poopal AC, Laxman RS (2009) Studies on biological reduction of chromate by Streptomyces griseus. J Hazard Mater 169:539-545
    • (2009) J Hazard Mater , vol.169 , pp. 539-545
    • Poopal, A.C.1    Laxman, R.S.2
  • 32
    • 59849085116 scopus 로고    scopus 로고
    • Characterization of the quinone reductase activity of the ferric reductase B protein from Paracoccus denitrificans
    • Sedláček V, van Spanning RJ, Kučera I (2009a) 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
    • Sedláček, V.1    Van Spanning, R.J.2    Kučera, I.3
  • 33
    • 65649117786 scopus 로고    scopus 로고
    • Ferric reductase A is essential for effective iron acquisition in Paracoccus denitrificans
    • Sedláček V, van Spanning RJ, Kučera I (2009b) Ferric reductase A is essential for effective iron acquisition in Paracoccus denitrificans. Microbiology 155:1294-1301
    • (2009) Microbiology , vol.155 , pp. 1294-1301
    • Sedláček, V.1    Van Spanning, R.J.2    Kučera, I.3
  • 34
    • 0034326675 scopus 로고    scopus 로고
    • Speciation of aqueous chromium(VI) solutions with the aid of Q-mode factor analysis followed by oblique projection
    • Sena MA, Scarminio IS, Collins KE, Collins CH (2000) Speciation of aqueous chromium(VI) solutions with the aid of Q-mode factor analysis followed by oblique projection. Talanta 53:453-461
    • (2000) Talanta , vol.53 , pp. 453-461
    • Sena, M.A.1    Scarminio, I.S.2    Collins, K.E.3    Collins, C.H.4
  • 35
    • 0025602251 scopus 로고
    • NADPH-dependent flavoenzymes catalyze one electron reduction of metal ions and molecular oxygen and generate hydroxyl radicals
    • Shi XL, Dalal NS (1990) NADPH-dependent flavoenzymes catalyze one electron reduction of metal ions and molecular oxygen and generate hydroxyl radicals. FEBS Lett 276:189-191
    • (1990) FEBS Lett , vol.276 , pp. 189-191
    • Shi, X.L.1    Dalal, N.S.2
  • 36
    • 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
  • 37
    • 33846970531 scopus 로고    scopus 로고
    • Lot6p from Saccharomyces cerevisiae is a FMN-dependent reductase with a potential role in quinone detoxification
    • Sollner S, Nebauer R, Ehammer H, Prem A, Deller S, Palfey BA, Daum G, Macheroux P (2007) Lot6p from Saccharomyces cerevisiae is a FMN-dependent reductase with a potential role in quinone detoxification. FEBS J 274:1328-1339
    • (2007) FEBS J , vol.274 , pp. 1328-1339
    • Sollner, S.1    Nebauer, R.2    Ehammer, H.3    Prem, A.4    Deller, S.5    Palfey, B.A.6    Daum, G.7    Macheroux, P.8
  • 38
    • 0033452469 scopus 로고    scopus 로고
    • Cloning and heterologous expression of NAD(P)H:quinone reductase of Arabidopsis thaliana, a functional homologue of animal DT-diaphorase
    • DOI 10.1016/S0014-5793(99)01625-7, PII S0014579399016257
    • Sparla F, Tedeschi G, Pupillo P, Trost P (1999) Cloning and heterologous expression of NAD(P)H:quinone reductase of Arabidopsis thaliana, a functional homologue of animal DT-diaphorase. FEBS Lett 463:382-386 (Pubitemid 30001955)
    • (1999) FEBS Letters , vol.463 , Issue.3 , pp. 382-386
    • Sparla, F.1    Tedeschi, G.2    Pupillo, P.3    Trost, P.4
  • 40
    • 0034531942 scopus 로고    scopus 로고
    • Iron metabolism in anoxic environments at near neutral pH
    • DOI 10.1016/S0168-6496(00)00088-X, PII S016864960000088X
    • Straub KL, Benz M, Schink B (2001) Iron metabolism in anoxic environments at near neutral pH. FEMS Microbiol Ecol 34:181-186 (Pubitemid 32008683)
    • (2000) FEMS Microbiology Ecology , vol.34 , Issue.3 , pp. 181-186
    • Straub, K.L.1    Benz, M.2    Schink, B.3
  • 41
    • 0032002313 scopus 로고    scopus 로고
    • Mechanistic study of the autoxidation of reduced flavin and quinone compounds
    • PII S0022072897005202
    • Tatsumi H, Nakase H, Kano K, Ikeda T (1998) Mechanistic study of the autoxidation of reduced flavin and quinone compounds. J Electroanal Chem 443:236-242 (Pubitemid 128391927)
    • (1998) Journal of Electroanalytical Chemistry , vol.443 , Issue.2 , pp. 236-242
    • Tatsumi, H.1    Nakase, H.2    Kano, K.3    Ikeda, T.4
  • 42
    • 70349459615 scopus 로고    scopus 로고
    • Heterologous expression and molecular characterization of the NAD(P)H:acceptor oxidoreductase (FerB) of Paracoccus denitrificans
    • Tesařík R, Sedláček V, Plocková J, Wimmerová M, Turánek J, Kučera I (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
    • Tesařík, R.1    Sedláček, V.2    Plocková, J.3    Wimmerová, M.4    Turánek, J.5    Kučera, I.6
  • 43
    • 0037199162 scopus 로고    scopus 로고
    • Chromate/nitrite interactions in Shewanella oneidensis MR-1: Evidence for multiple hexavalent chromium [Cr(VI)] reduction mechanisms dependent on physiological growth conditions
    • DOI 10.1002/bit.10261
    • Viamajala S, Peyton BM, Apel WA, Petersen JN (2002) Chromate/nitrite interactions in Shewanella oneidensis MR-1: evidence for multiple hexavalent chromium [Cr(VI)] reduction mechanisms dependent on physiological growth conditions. Biotechnol Bioeng 78:770-778 (Pubitemid 34747102)
    • (2002) Biotechnology and Bioengineering , vol.78 , Issue.7 , pp. 770-778
    • Viamajala, S.1    Peyton, B.M.2    Apel, W.A.3    Petersen, J.N.4
  • 44
    • 34250307422 scopus 로고    scopus 로고
    • Bioremediation of soils polluted with hexavalent chromium using bacteria: A challenge
    • Singh SN, Tripathi RD (eds), Springer, Berlin
    • Viti C, Giovannetti L (2007) Bioremediation of soils polluted with hexavalent chromium using bacteria: a challenge. In: Singh SN, Tripathi RD (eds) Environmental bioremediation techniques. Springer, Berlin, pp 57-76
    • (2007) Environmental Bioremediation Techniques , pp. 57-76
    • Viti, C.1    Giovannetti, L.2
  • 45
    • 0037438569 scopus 로고    scopus 로고
    • Automated screening in environmental arrays allows analysis of quantitative phenotypic profiles in Saccharomyces cerevisiae
    • DOI 10.1002/yea.931
    • Warringer J, Blomberg A (2003) Automated screening in environmental arrays allows analysis of quantitative phenotypic profiles in Saccharomyces cerevisiae. Yeast 20:53-67 (Pubitemid 36054265)
    • (2003) Yeast , vol.20 , Issue.1 , pp. 53-67
    • Warringer, J.1    Blomberg, A.2
  • 46
    • 0039479067 scopus 로고
    • The mechanisms of chromic acid oxidations
    • Westheimer FH (1949) The mechanisms of chromic acid oxidations. Chem Rev 45:419-451
    • (1949) Chem Rev , vol.45 , pp. 419-451
    • Westheimer, F.H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.