메뉴 건너뛰기




Volumn 96, Issue 5, 2015, Pages 1042-1052

ArsH is an organoarsenical oxidase that confers resistance to trivalent forms of the herbicide monosodium methylarsenate and the poultry growth promoter roxarsone

Author keywords

[No Author keywords available]

Indexed keywords

ARSENOSOBENZENE; ARSH PROTEIN; HERBICIDE; HYDROGEN PEROXIDE; MONOSODIUM METHYLARSENATE; ORGANOARSENIC DERIVATIVE; OXIDOREDUCTASE; ROXARSONE; UNCLASSIFIED DRUG; METHANEARSONIC ACID;

EID: 84929702472     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/mmi.12988     Document Type: Article
Times cited : (141)

References (30)
  • 1
    • 0034016916 scopus 로고    scopus 로고
    • The chromosomal arsenic resistance genes of Thiobacillus ferrooxidans have an unusual arrangement and confer increased arsenic and antimony resistance to Escherichia coli
    • Butcher, B.G., Deane, S.M., and Rawlings, D.E. (2000) The chromosomal arsenic resistance genes of Thiobacillus ferrooxidans have an unusual arrangement and confer increased arsenic and antimony resistance to Escherichia coli. Appl Environ Microbiol 66: 1826-1833.
    • (2000) Appl Environ Microbiol , vol.66 , pp. 1826-1833
    • Butcher, B.G.1    Deane, S.M.2    Rawlings, D.E.3
  • 2
    • 0347567163 scopus 로고    scopus 로고
    • Heavy metal tolerance and metal homeostasis in Pseudomonas putida as revealed by complete genome analysis
    • Canovas, D., Cases, I., and de Lorenzo, V. (2003) Heavy metal tolerance and metal homeostasis in Pseudomonas putida as revealed by complete genome analysis. Environ Microbiol 5: 1242-1256.
    • (2003) Environ Microbiol , vol.5 , pp. 1242-1256
    • Canovas, D.1    Cases, I.2    de Lorenzo, V.3
  • 3
    • 0028837094 scopus 로고
    • The ars operon of Escherichia coli confers arsenical and antimonial resistance
    • Carlin, A., Shi, W., Dey, S., and Rosen, B.P. (1995) The ars operon of Escherichia coli confers arsenical and antimonial resistance. J Bacteriol 177: 981-986.
    • (1995) J Bacteriol , vol.177 , pp. 981-986
    • Carlin, A.1    Shi, W.2    Dey, S.3    Rosen, B.P.4
  • 4
    • 84892741531 scopus 로고    scopus 로고
    • Biosensor for organoarsenical herbicides and growth promoters
    • Chen, J., Sun, S., Li, C.Z., Zhu, Y.G., and Rosen, B.P. (2014) Biosensor for organoarsenical herbicides and growth promoters. Environ Sci Technol 48: 1141-1147.
    • (2014) Environ Sci Technol , vol.48 , pp. 1141-1147
    • Chen, J.1    Sun, S.2    Li, C.Z.3    Zhu, Y.G.4    Rosen, B.P.5
  • 5
    • 79955867370 scopus 로고    scopus 로고
    • Polymorphisms in arsenic(+III oxidation state) methyltransferase (AS3MT) predict gene expression of AS3MT as well as arsenic metabolism
    • Engstrom, K., Vahter, M., Mlakar, S.J., Concha, G., Nermell, B., Raqib, R., etal. (2011) Polymorphisms in arsenic(+III oxidation state) methyltransferase (AS3MT) predict gene expression of AS3MT as well as arsenic metabolism. Environ Health Perspect 119: 182-188.
    • (2011) Environ Health Perspect , vol.119 , pp. 182-188
    • Engstrom, K.1    Vahter, M.2    Mlakar, S.J.3    Concha, G.4    Nermell, B.5    Raqib, R.6
  • 6
    • 0035958746 scopus 로고    scopus 로고
    • The composite genome of the legume symbiont Sinorhizobium meliloti
    • Galibert, F., Finan, T.M., Long, S.R., Puhler, A., Abola, P., Ampe, F., etal. (2001) The composite genome of the legume symbiont Sinorhizobium meliloti. Science 293: 668-672.
    • (2001) Science , vol.293 , pp. 668-672
    • Galibert, F.1    Finan, T.M.2    Long, S.R.3    Puhler, A.4    Abola, P.5    Ampe, F.6
  • 7
    • 84856920272 scopus 로고    scopus 로고
    • ArsH from the cyanobacterium Synechocystis sp. PCC 6803 is an efficient NADPH-dependent quinone reductase
    • Hervas, M., Lopez-Maury, L., Leon, P., Sanchez-Riego, A.M., Florencio, F.J., and Navarro, J.A. (2012) ArsH from the cyanobacterium Synechocystis sp. PCC 6803 is an efficient NADPH-dependent quinone reductase. Biochemistry 51: 1178-1187.
    • (2012) Biochemistry , vol.51 , pp. 1178-1187
    • Hervas, M.1    Lopez-Maury, L.2    Leon, P.3    Sanchez-Riego, A.M.4    Florencio, F.J.5    Navarro, J.A.6
  • 10
    • 0042337279 scopus 로고    scopus 로고
    • Arsenic sensing and resistance system in the cyanobacterium Synechocystis sp. strain PCC 6803
    • Lopez-Maury, L., Florencio, F.J., and Reyes, J.C. (2003) Arsenic sensing and resistance system in the cyanobacterium Synechocystis sp. strain PCC 6803. J Bacteriol 185: 5363-5371.
    • (2003) J Bacteriol , vol.185 , pp. 5363-5371
    • Lopez-Maury, L.1    Florencio, F.J.2    Reyes, J.C.3
  • 11
    • 62249218236 scopus 로고    scopus 로고
    • Epoxidation of conjugated C=C-bonds and sulfur-oxidation of thioethers mediated by NADH:FMN-dependent oxidoreductases
    • Mueller, N.J., Stueckler, C., Hall, M., Macheroux, P., and Faber, K. (2009) Epoxidation of conjugated C=C-bonds and sulfur-oxidation of thioethers mediated by NADH:FMN-dependent oxidoreductases. Org Biomol Chem 7: 1115-1119.
    • (2009) Org Biomol Chem , vol.7 , pp. 1115-1119
    • Mueller, N.J.1    Stueckler, C.2    Hall, M.3    Macheroux, P.4    Faber, K.5
  • 12
    • 0031016475 scopus 로고    scopus 로고
    • Virulence and arsenic resistance in Yersiniae
    • Neyt, C., Iriarte, M., Thi, V.H., and Cornelis, G.R. (1997) Virulence and arsenic resistance in Yersiniae. J Bacteriol 179: 612-619.
    • (1997) J Bacteriol , vol.179 , pp. 612-619
    • Neyt, C.1    Iriarte, M.2    Thi, V.H.3    Cornelis, G.R.4
  • 13
    • 84921859136 scopus 로고    scopus 로고
    • Functional coexistence of twin arsenic resistance systems in Pseudomonas putida KT2440
    • Paez-Espino, A.D., Durante-Rodriguez, G., and de Lorenzo, V. (2015) Functional coexistence of twin arsenic resistance systems in Pseudomonas putida KT2440. Environ Microbiol 17: 229-238.
    • (2015) Environ Microbiol , vol.17 , pp. 229-238
    • Paez-Espino, A.D.1    Durante-Rodriguez, G.2    de Lorenzo, V.3
  • 14
    • 33144480276 scopus 로고    scopus 로고
    • Arsenic detoxification and evolution of trimethylarsine gas by a microbial arsenite S-adenosylmethionine methyltransferase
    • Qin, J., Rosen, B.P., Zhang, Y., Wang, G., Franke, S., and Rensing, C. (2006) Arsenic detoxification and evolution of trimethylarsine gas by a microbial arsenite S-adenosylmethionine methyltransferase. Proc Natl Acad Sci USA 103: 2075-2080.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 2075-2080
    • Qin, J.1    Rosen, B.P.2    Zhang, Y.3    Wang, G.4    Franke, S.5    Rensing, C.6
  • 15
    • 65249109869 scopus 로고    scopus 로고
    • Biotransformation of arsenic by a Yellowstone thermoacidophilic eukaryotic alga
    • Qin, J., Lehr, C.R., Yuan, C., Le, X.C., McDermott, T.R., and Rosen, B.P. (2009) Biotransformation of arsenic by a Yellowstone thermoacidophilic eukaryotic alga. Proc Natl Acad Sci USA 106: 5213-5217.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 5213-5217
    • Qin, J.1    Lehr, C.R.2    Yuan, C.3    Le, X.C.4    McDermott, T.R.5    Rosen, B.P.6
  • 16
    • 0017367539 scopus 로고
    • 74As-labeled arsenate and arsenite for use in biological experiments
    • 74As-labeled arsenate and arsenite for use in biological experiments. Anal Biochem 78: 557-560.
    • (1977) Anal Biochem , vol.78 , pp. 557-560
    • Reay, P.F.1    Asher, C.J.2
  • 17
    • 0036557991 scopus 로고    scopus 로고
    • Arsenical resistance in the IncHI2 plasmids
    • Ryan, D., and Colleran, E. (2002) Arsenical resistance in the IncHI2 plasmids. Plasmid 47: 234-240.
    • (2002) Plasmid , vol.47 , pp. 234-240
    • Ryan, D.1    Colleran, E.2
  • 19
    • 84901207700 scopus 로고    scopus 로고
    • The structural and functional basis of catalysis mediated by NAD(P)H:acceptor oxidoreductase (FerB) of Paracoccus denitrificans
    • Sedlacek, V., Klumpler, T., Marek, J., and Kucera, I. (2014) The structural and functional basis of catalysis mediated by NAD(P)H:acceptor oxidoreductase (FerB) of Paracoccus denitrificans. PLoS ONE 9: e96262.
    • (2014) PLoS ONE , vol.9 , pp. e96262
    • Sedlacek, V.1    Klumpler, T.2    Marek, J.3    Kucera, I.4
  • 21
    • 84899448312 scopus 로고    scopus 로고
    • Arsenic methyltransferases
    • Kretsinger, R.H., Uversky, V.N., and Permyakov, E.A. (eds). New York: Springer New York
    • Thomas, D.J., and Rosen, B.P. (2013) Arsenic methyltransferases. In Encyclopedia of Metalloproteins. Kretsinger, R.H., Uversky, V.N., and Permyakov, E.A. (eds). New York: Springer New York, pp. 140-145.
    • (2013) Encyclopedia of Metalloproteins , pp. 140-145
    • Thomas, D.J.1    Rosen, B.P.2
  • 22
    • 84903878096 scopus 로고    scopus 로고
    • ArsH from Synechocystis sp. PCC 6803 reduces chromate and ferric iron
    • Xue, X.M., Yan, Y., Xu, H.J., Wang, N., Zhang, X., and Ye, J. (2014) ArsH from Synechocystis sp. PCC 6803 reduces chromate and ferric iron. FEMS Microbiol Lett 356: 105-112.
    • (2014) FEMS Microbiol Lett , vol.356 , pp. 105-112
    • Xue, X.M.1    Yan, Y.2    Xu, H.J.3    Wang, N.4    Zhang, X.5    Ye, J.6
  • 23
    • 26444519913 scopus 로고    scopus 로고
    • Novel pathway for arsenic detoxification in the legume symbiont Sinorhizobium meliloti
    • Yang, H.C., Cheng, J., Finan, T.M., Rosen, B.P., and Bhattacharjee, H. (2005) Novel pathway for arsenic detoxification in the legume symbiont Sinorhizobium meliloti. J Bacteriol 187: 6991-6997.
    • (2005) J Bacteriol , vol.187 , pp. 6991-6997
    • Yang, H.C.1    Cheng, J.2    Finan, T.M.3    Rosen, B.P.4    Bhattacharjee, H.5
  • 25
    • 34547652441 scopus 로고    scopus 로고
    • Crystal structure of the flavoprotein ArsH from Sinorhizobium meliloti
    • Ye, J., Yang, H.C., Rosen, B.P., and Bhattacharjee, H. (2007) Crystal structure of the flavoprotein ArsH from Sinorhizobium meliloti. FEBS Lett 581: 3996-4000.
    • (2007) FEBS Lett , vol.581 , pp. 3996-4000
    • Ye, J.1    Yang, H.C.2    Rosen, B.P.3    Bhattacharjee, H.4
  • 26
    • 84862776542 scopus 로고    scopus 로고
    • Arsenic biomethylation by photosynthetic organisms
    • Ye, J., Rensing, C., Rosen, B.P., and Zhu, Y.G. (2012) Arsenic biomethylation by photosynthetic organisms. Trends Plant Sci 17: 155-162.
    • (2012) Trends Plant Sci , vol.17 , pp. 155-162
    • Ye, J.1    Rensing, C.2    Rosen, B.P.3    Zhu, Y.G.4
  • 27
    • 84901675745 scopus 로고    scopus 로고
    • A CAs lyase for degradation of environmental organoarsenical herbicides and animal husbandry growth promoters
    • Yoshinaga, M., and Rosen, B.P. (2014) A CAs lyase for degradation of environmental organoarsenical herbicides and animal husbandry growth promoters. Proc Natl Acad Sci USA 111: 7701-7706.
    • (2014) Proc Natl Acad Sci USA , vol.111 , pp. 7701-7706
    • Yoshinaga, M.1    Rosen, B.P.2
  • 28
    • 79955043823 scopus 로고    scopus 로고
    • Demethylation of methylarsonic acid by a microbial community
    • Yoshinaga, M., Cai, Y., and Rosen, B.P. (2011) Demethylation of methylarsonic acid by a microbial community. Environ Microbiol 13: 1205-1215.
    • (2011) Environ Microbiol , vol.13 , pp. 1205-1215
    • Yoshinaga, M.1    Cai, Y.2    Rosen, B.P.3
  • 29
    • 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
    • Zhou, M., Diwu, Z., Panchuk-Voloshina, N., and Haugland, R.P. (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: 162-168.
    • (1997) Anal Biochem , vol.253 , pp. 162-168
    • Zhou, M.1    Diwu, Z.2    Panchuk-Voloshina, N.3    Haugland, R.P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.