메뉴 건너뛰기




Volumn 68, Issue 3, 2014, Pages 311-316

A rhizobium selenitireducens protein showing selenite reductase activity

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEINS; CHEMICAL PRECIPITATION; CHROMATOGRAPHY, LIQUID; ELECTROPHORESIS; FMN REDUCTASE; NAD; OXIDATION-REDUCTION; SELENIOUS ACID; SEQUENCE HOMOLOGY, AMINO ACID; SINORHIZOBIUM; TANDEM MASS SPECTROMETRY;

EID: 84893967376     PISSN: 03438651     EISSN: 14320991     Source Type: Journal    
DOI: 10.1007/s00284-013-0474-7     Document Type: Article
Times cited : (47)

References (31)
  • 1
    • 0642308250 scopus 로고    scopus 로고
    • The respiratory arsenate reductase from Bacillus selenitireducens strain MLS10
    • 1:CAS:528:DC%2BD3sXnt1GmsLY%3D 13129615 10.1016/S0378-1097(03)00609-8
    • Afkar E, Lisak J, Saltikov C, Basu P, Oremland RS, Stolz JF (2003) The respiratory arsenate reductase from Bacillus selenitireducens strain MLS10. FEMS Microbiol Lett 226:107-112
    • (2003) FEMS Microbiol Lett , vol.226 , pp. 107-112
    • Afkar, E.1    Lisak, J.2    Saltikov, C.3    Basu, P.4    Oremland, R.S.5    Stolz, J.F.6
  • 2
    • 33847648982 scopus 로고    scopus 로고
    • Selenite-reducing capacity of the copper-containing nitrite reductase of Rhizobium sullae
    • 1:CAS:528:DC%2BD2sXjvVyntb0%3D 17227457 10.1111/j.1574-6968.2006.00617.x
    • Basaglia M, Toffanin A, Baldan E, Bottegal M, Shapleigh JP, Casella S (2007) Selenite-reducing capacity of the copper-containing nitrite reductase of Rhizobium sullae. FEMS Microbiol Lett 269:124-130
    • (2007) FEMS Microbiol Lett , vol.269 , pp. 124-130
    • Basaglia, M.1    Toffanin, A.2    Baldan, E.3    Bottegal, M.4    Shapleigh, J.P.5    Casella, S.6
  • 3
    • 0036956672 scopus 로고    scopus 로고
    • Involvement of a putative molybdenum enzyme in the reduction of selenate by Escherichia coli
    • 12480890
    • Bébien M, Kirsch J, Méjean V, Verméglio A (2002) Involvement of a putative molybdenum enzyme in the reduction of selenate by Escherichia coli. Microbiology 148:3865-3872
    • (2002) Microbiology , vol.148 , pp. 3865-3872
    • Bébien, M.1    Kirsch, J.2    Méjean, V.3    Verméglio, A.4
  • 4
    • 0024041236 scopus 로고
    • Purification and biochemical of tellurite-reducing activities from Thermus thermophilus HB8
    • 1:CAS:528:DyaL1cXlt1Cku70%3D 211280 3384810
    • Chiong M, Gonzales E, Barra R, Vasquez C (1988) Purification and biochemical of tellurite-reducing activities from Thermus thermophilus HB8. J Bacteriol 170:3269-3273
    • (1988) J Bacteriol , vol.170 , pp. 3269-3273
    • Chiong, M.1    Gonzales, E.2    Barra, R.3    Vasquez, C.4
  • 5
    • 0027295963 scopus 로고
    • The periplasmic nitrite reductase of Thauera selenatis may catalyze the reduction of selenite to elemental selenium
    • 1:CAS:528:DyaK3sXms1Kiurs%3D
    • DeMoll-Decker H, Macy JM (1993) The periplasmic nitrite reductase of Thauera selenatis may catalyze the reduction of selenite to elemental selenium. Arch Microbiol 160:241-247
    • (1993) Arch Microbiol , vol.160 , pp. 241-247
    • Demoll-Decker, H.1    Macy, J.M.2
  • 6
    • 0038820069 scopus 로고    scopus 로고
    • Characterization of YqjM, an old yellow enzyme homolog from Bacillus subtilis involved in the oxidative stress response
    • 1:CAS:528:DC%2BD3sXktVaqtL0%3D 12660247 10.1074/jbc.M211778200
    • Fitzpatrick TB, Amrhein N, Macheroux P (2003) Characterization of YqjM, an old yellow enzyme homolog from Bacillus subtilis involved in the oxidative stress response. J Biol Chem 278:19891-19897
    • (2003) J Biol Chem , vol.278 , pp. 19891-19897
    • Fitzpatrick, T.B.1    Amrhein, N.2    Macheroux, P.3
  • 7
    • 0028774535 scopus 로고
    • Old yellow enzyme at 2 Å resolution: Overall structure, ligand binding, and comparison with related flavoproteins
    • 1:CAS:528:DyaK2MXivFSku7g%3D 7881908 10.1016/S0969-2126(94)00111-1
    • Fox KM, Karplus A (1994) Old yellow enzyme at 2 Å resolution: overall structure, ligand binding, and comparison with related flavoproteins. Structure 2:1089-1105
    • (1994) Structure , vol.2 , pp. 1089-1105
    • Fox, K.M.1    Karplus, A.2
  • 8
    • 33745879474 scopus 로고    scopus 로고
    • Xenobiotic reductase A in the degradation of quinoline by Pseudomonas putida 86: Physiological function, structure and mechanism of 8-hydroxycoumarin reduction
    • 1:CAS:528:DC%2BD28XntFSgtb4%3D 16822524 10.1016/j.jmb.2006.06.007
    • Griese JJ, Jakob RP, Schwarzinger S, Dobbek H (2006) Xenobiotic reductase A in the degradation of quinoline by Pseudomonas putida 86: physiological function, structure and mechanism of 8-hydroxycoumarin reduction. J Mol Biol 361:140-152
    • (2006) J Mol Biol , vol.361 , pp. 140-152
    • Griese, J.J.1    Jakob, R.P.2    Schwarzinger, S.3    Dobbek, H.4
  • 9
    • 34248351434 scopus 로고    scopus 로고
    • An Azospira oryzae (syn Dechlorosoma suillum) strain that reduces selenate and selenite to elemental red selenium
    • 1:CAS:528:DC%2BD2sXltVGqsL4%3D 17486405 10.1007/s00284-006-0474-y
    • Hunter WJ (2007) An Azospira oryzae (syn Dechlorosoma suillum) strain that reduces selenate and selenite to elemental red selenium. Curr Microbiol 54:376-381
    • (2007) Curr Microbiol , vol.54 , pp. 376-381
    • Hunter, W.J.1
  • 10
    • 33645240942 scopus 로고    scopus 로고
    • Identification and characterization of an Aeromonas salmonicida (syn Haemophilus piscium) strain that reduces selenite to elemental red selenium
    • 1:CAS:528:DC%2BD28XivVegtbc%3D 16550462 10.1007/s00284-005-0303-8
    • Hunter WJ, Kuykendall LD (2006) Identification and characterization of an Aeromonas salmonicida (syn Haemophilus piscium) strain that reduces selenite to elemental red selenium. Curr Microbiol 52:305-309
    • (2006) Curr Microbiol , vol.52 , pp. 305-309
    • Hunter, W.J.1    Kuykendall, L.D.2
  • 11
    • 34648835346 scopus 로고    scopus 로고
    • Reduction of selenite to elemental red selenium by Rhizobium sp. Strain B1
    • 1:CAS:528:DC%2BD2sXhtVOisbnK 17882505 10.1007/s00284-007-0202-2
    • Hunter WJ, Kuykendall LD (2007) Reduction of selenite to elemental red selenium by Rhizobium sp. Strain B1. Curr Microbiol 55:344-349
    • (2007) Curr Microbiol , vol.55 , pp. 344-349
    • Hunter, W.J.1    Kuykendall, L.D.2
  • 12
    • 44149120468 scopus 로고    scopus 로고
    • Bio-reduction of selenite to elemental red selenium by Tetrathiobacter kashmirensis
    • 1:CAS:528:DC%2BD1cXmtValsbg%3D 18389307 10.1007/s00284-008-9160-6
    • Hunter WJ, Manter DK (2008) Bio-reduction of selenite to elemental red selenium by Tetrathiobacter kashmirensis. Curr Microbiol 57:83-88
    • (2008) Curr Microbiol , vol.57 , pp. 83-88
    • Hunter, W.J.1    Manter, D.K.2
  • 13
    • 64549129561 scopus 로고    scopus 로고
    • Reduction of selenite to elemental red selenium by Pseudomonas sp. Strain CA5
    • 1:CAS:528:DC%2BD1MXktFCjtbg%3D 19189180 10.1007/s00284-009-9358-2
    • Hunter WJ, Manter DK (2009) Reduction of selenite to elemental red selenium by Pseudomonas sp. strain CA5. Curr Microbiol 58:493-498
    • (2009) Curr Microbiol , vol.58 , pp. 493-498
    • Hunter, W.J.1    Manter, D.K.2
  • 14
    • 35148855212 scopus 로고    scopus 로고
    • Rhizobium selenireducens sp. Nov.: A selenite-reducing a-Proteobacteria isolated from a bioreactor
    • 1:CAS:528:DC%2BD2sXht1yns7bO 17805926 10.1007/s00284-007-9020-9
    • Hunter WJ, Kuykendall LD, Manter DK (2007) Rhizobium selenireducens sp. nov.: a selenite-reducing a-Proteobacteria isolated from a bioreactor. Curr Microbiol 55:455-460
    • (2007) Curr Microbiol , vol.55 , pp. 455-460
    • Hunter, W.J.1    Kuykendall, L.D.2    Manter, D.K.3
  • 15
    • 29344445221 scopus 로고    scopus 로고
    • Identification of otubain 1 as a novel substrate for the Yersinia protein kinase using chemical genetics and mass spectrometry
    • 1:CAS:528:DC%2BD28XkslKq 16364312 10.1016/j.febslet.2005.11.071
    • Juris SJ, Shah K, Shokat K, Dixon JE, Vacratsis PO (2006) Identification of otubain 1 as a novel substrate for the Yersinia protein kinase using chemical genetics and mass spectrometry. FEBS Lett 580:179-183
    • (2006) FEBS Lett , vol.580 , pp. 179-183
    • Juris, S.J.1    Shah, K.2    Shokat, K.3    Dixon, J.E.4    Vacratsis, P.O.5
  • 16
    • 33645099466 scopus 로고    scopus 로고
    • Enzymic systems proposed to be involved in the dissimilatory reduction of selenite in the purple non-sulfur bacteria Rhodospirillum rubrum and Rhodobacter capsulatus
    • 1:CAS:528:DC%2BD28XjtVOltbk%3D 16514153 10.1099/mic.0.28240-0
    • Kessi J (2006) Enzymic systems proposed to be involved in the dissimilatory reduction of selenite in the purple non-sulfur bacteria Rhodospirillum rubrum and Rhodobacter capsulatus. Microbiology 152:731-743
    • (2006) Microbiology , vol.152 , pp. 731-743
    • Kessi, J.1
  • 17
    • 23044455760 scopus 로고    scopus 로고
    • The 1.3 Å crystal structure of the flavoprotein YqjM reveals a novel class of old yellow enzymes
    • 1:CAS:528:DC%2BD2MXmsVyqurk%3D 15890652 10.1074/jbc.M502587200
    • Kitzing K, Fitzpatrick TB, Wilken C, Sawa J, Bourenkov GP, Macheroux P, Clausen T (2005) The 1.3 Å crystal structure of the flavoprotein YqjM reveals a novel class of old yellow enzymes. J Biol Chem 280:27904-27913
    • (2005) J Biol Chem , vol.280 , pp. 27904-27913
    • Kitzing, K.1    Fitzpatrick, T.B.2    Wilken, C.3    Sawa, J.4    Bourenkov, G.P.5    Macheroux, P.6    Clausen, T.7
  • 18
    • 0017120383 scopus 로고
    • Association-dissociation behavior and subunits structure of heat-released nitrate reductase from Escherichia coli
    • 1:CAS:528:DyaE28XktVWkt7k%3D 770463
    • Lund K, DeMoss JA (1976) Association-dissociation behavior and subunits structure of heat-released nitrate reductase from Escherichia coli. J Biol Chem 251:2207-2213
    • (1976) J Biol Chem , vol.251 , pp. 2207-2213
    • Lund, K.1    Demoss, J.A.2
  • 21
    • 41949115394 scopus 로고    scopus 로고
    • A novel chromate reductase from Thermus scotoductus SA-01 related to old yellow enzyme
    • 1:CAS:528:DC%2BD1cXkslygsbY%3D 18263719 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 Bact 190:3076-3082
    • (2008) J Bact , vol.190 , pp. 3076-3082
    • Opperman, D.J.1    Piater, L.A.2    Van Heerden, E.3
  • 22
    • 33646539096 scopus 로고    scopus 로고
    • Genetic and biochemical evidence for the involvement of a molybdenum-dependent enzyme in one of the selenite reduction pathways of Rhodobacter sphaeroides f. Sp. Denitrificans IL106
    • 1:CAS:528:DC%2BD28XkvFSqur0%3D 1472318 16672451 10.1128/AEM.72.5.3147- 3153.2006
    • Pierru B, Grosse S, Pignol D, Sabaty M (2006) Genetic and biochemical evidence for the involvement of a molybdenum-dependent enzyme in one of the selenite reduction pathways of Rhodobacter sphaeroides f. sp. denitrificans IL106. Appl Environ Microbiol 72:3147-3153
    • (2006) Appl Environ Microbiol , vol.72 , pp. 3147-3153
    • Pierru, B.1    Grosse, S.2    Pignol, D.3    Sabaty, M.4
  • 23
    • 0031228020 scopus 로고    scopus 로고
    • Active oxygen generation as a possible mechanism of selenium toxicity
    • 1:STN:280:DyaK2svmtV2lsg%3D%3D 9315327
    • Seko Y, Imura N (1997) Active oxygen generation as a possible mechanism of selenium toxicity. Biomed Environ Sci 10:333-339
    • (1997) Biomed Environ Sci , vol.10 , pp. 333-339
    • Seko, Y.1    Imura, N.2
  • 24
    • 77957228998 scopus 로고    scopus 로고
    • Determinants of substrate binding and protonation in the flavoenzyme xenobiotic reductase A
    • 1:CAS:528:DC%2BC3cXht1CgtrjK 20826164 10.1016/j.jmb.2010.08.047
    • Spiegelhauer O (2010) Determinants of substrate binding and protonation in the flavoenzyme xenobiotic reductase A. J Mol Biol 403:286-298
    • (2010) J Mol Biol , vol.403 , pp. 286-298
    • Spiegelhauer, O.1
  • 25
    • 77950866209 scopus 로고    scopus 로고
    • Cysteine as a modulator residue in the active site of xenobiotic reductase A: A structural, thermodynamic and kinetic study
    • 1:CAS:528:DC%2BC3cXktlCrt7k%3D 20206186 10.1016/j.jmb.2010.02.044
    • Spiegelhauer O, Mende S, Dickert F, Knauer SH, Ullmann GM, Dobbek H (2010) Cysteine as a modulator residue in the active site of xenobiotic reductase A: a structural, thermodynamic and kinetic study. J Mol Biol 398:66-82
    • (2010) J Mol Biol , vol.398 , pp. 66-82
    • Spiegelhauer, O.1    Mende, S.2    Dickert, F.3    Knauer, S.H.4    Ullmann, G.M.5    Dobbek, H.6
  • 26
    • 0000808024 scopus 로고
    • Reindarstellung der Wirkungsgruppe des gelben Ferments
    • 1:CAS:528:DyaA2MXhvF2jsQ%3D%3D
    • Theorell H (1935) Reindarstellung der Wirkungsgruppe des gelben Ferments. Biochemische Zeitschrift 275:344-346
    • (1935) Biochemische Zeitschrift , vol.275 , pp. 344-346
    • Theorell, H.1
  • 27
    • 0027058448 scopus 로고
    • Reduction of selenate and selenite to elemental selenium by Wolinella succinogenes
    • 10.1139/m92-219
    • Tomei FA, Barton LL, Lemanski CL, Zocco TG (1962) Reduction of selenate and selenite to elemental selenium by Wolinella succinogenes. Can J Microbiol 38:1328-1333
    • (1962) Can J Microbiol , vol.38 , pp. 1328-1333
    • Tomei, F.A.1    Barton, L.L.2    Lemanski, C.L.3    Zocco, T.G.4
  • 28
    • 0031735176 scopus 로고    scopus 로고
    • Selenium metabolism in Escherichia coli
    • 1:CAS:528:DyaK1cXnvV2lu7o%3D 9850565 10.1023/A:1009290213301
    • Turner RJ, Weiner JH, Taylor DE (1998) Selenium metabolism in Escherichia coli. Biometals 11:223-227
    • (1998) Biometals , vol.11 , pp. 223-227
    • Turner, R.J.1    Weiner, J.H.2    Taylor, D.E.3
  • 29
    • 0344585331 scopus 로고    scopus 로고
    • Selenate reduction by Enterobacter cloacae SLD1a-1 is catalysed by a molybdenum-dependent membrane-bound enzyme that is distinct from the membrane-bound nitrate reductase
    • 1:CAS:528:DC%2BD3sXpt1ektLc%3D 14638434 10.1016/S0378-1097(03)00782-1
    • Watts CA, Ridley H, Condie KL, Leaver JT, Richardson DJ, Butler CS (2003) Selenate reduction by Enterobacter cloacae SLD1a-1 is catalysed by a molybdenum-dependent membrane-bound enzyme that is distinct from the membrane-bound nitrate reductase. FEMS Microbiol Lett 228:273-279
    • (2003) FEMS Microbiol Lett , vol.228 , pp. 273-279
    • Watts, C.A.1    Ridley, H.2    Condie, K.L.3    Leaver, J.T.4    Richardson, D.J.5    Butler, C.S.6
  • 30
    • 2942563803 scopus 로고    scopus 로고
    • Biotransformation of explosives by the old yellow enzyme Family of flavoproteins
    • 10.1128/AEM.70.6.3566-3574.2004 1:CAS:528:DC%2BD2cXltFCitbs%3D 427764 15184158 10.1128/AEM.70.6.3566-3574.2004
    • Williams RE, Rathbone DA, Scrutton NS, Bruce NC (2004) Biotransformation of explosives by the old yellow enzyme Family of flavoproteins. Appl Environ Microbiol 70:3566-3574. doi: 10.1128/AEM.70.6.3566-3574.2004
    • (2004) Appl Environ Microbiol , vol.70 , pp. 3566-3574
    • Williams, R.E.1    Rathbone, D.A.2    Scrutton, N.S.3    Bruce, N.C.4
  • 31
    • 0002842958 scopus 로고
    • Hydrogenase (I) of Clostridium pasteurianum functions a novel selenite reductase
    • 1:CAS:528:DyaK28XkvV2ltbw%3D 16887509 10.1016/S1075-9964(95)80457-9
    • Yanke LJ, Bryant RD, Laishley EJ (1995) Hydrogenase (I) of Clostridium pasteurianum functions a novel selenite reductase. Anaerobe 1:61-67
    • (1995) Anaerobe , vol.1 , pp. 61-67
    • Yanke, L.J.1    Bryant, R.D.2    Laishley, E.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.