메뉴 건너뛰기




Volumn 382, Issue 2, 2009, Pages 298-302

Respiratory arsenate reductase as a bidirectional enzyme

Author keywords

Alkalilimnicola ehrlichii; Arsenate reductase; Arsenite oxidase; Principle of microscopic reversibility

Indexed keywords

ARSENATE REDUCTASE; ARSENIC TRIOXIDE; BACTERIAL ENZYME; MOLYBDENUM;

EID: 63349107046     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2009.03.045     Document Type: Article
Times cited : (95)

References (32)
  • 1
    • 0037656045 scopus 로고    scopus 로고
    • The ecology of arsenic
    • Oremland R.S., and Stolz J.F. The ecology of arsenic. Science 300 (2003) 939-944
    • (2003) Science , vol.300 , pp. 939-944
    • Oremland, R.S.1    Stolz, J.F.2
  • 4
    • 2442699369 scopus 로고    scopus 로고
    • Dissimilatory arsenate reduction with sulfide as the electron donor: experiments with Mono Lake water and isolation of strain MLMS-1, a chemoautotrophic arsenate-respirer
    • Hoeft S.E., Kulp T.R., Stolz J.F., Hollibaugh J.T., and Oremland R.S. Dissimilatory arsenate reduction with sulfide as the electron donor: experiments with Mono Lake water and isolation of strain MLMS-1, a chemoautotrophic arsenate-respirer. Appl. Environ. Microbiol. 70 (2004) 2741-2747
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 2741-2747
    • Hoeft, S.E.1    Kulp, T.R.2    Stolz, J.F.3    Hollibaugh, J.T.4    Oremland, R.S.5
  • 5
    • 0036794790 scopus 로고    scopus 로고
    • Anaerobic oxidation of arsenite in Mono Lake water and by a facultative, arsenite-oxidizing chemoautotroph, strain MLHE-1
    • Oremland R.S., Hoeft S.E., Santini J.M., Bano N., Hollibaugh R.A., and Hollibaugh J.T. Anaerobic oxidation of arsenite in Mono Lake water and by a facultative, arsenite-oxidizing chemoautotroph, strain MLHE-1. Appl. Environ. Microbiol. 68 (2002) 4795-4802
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 4795-4802
    • Oremland, R.S.1    Hoeft, S.E.2    Santini, J.M.3    Bano, N.4    Hollibaugh, R.A.5    Hollibaugh, J.T.6
  • 7
    • 0006301126 scopus 로고    scopus 로고
    • Bacillus arsenicoselenatis sp. nov., and Bacillus selenitireducens sp. nov.: two haloalkaliphiles from Mono Lake, California, which respire oxyanions of selenium and arsenic
    • Switzer Blum J., Bindi A.B., Buzzelli J., Stolz J.F., and Oremland R.S. Bacillus arsenicoselenatis sp. nov., and Bacillus selenitireducens sp. nov.: two haloalkaliphiles from Mono Lake, California, which respire oxyanions of selenium and arsenic. Arch. Microbiol. 171 (1998) 19-30
    • (1998) Arch. Microbiol. , vol.171 , pp. 19-30
    • Switzer Blum, J.1    Bindi, A.B.2    Buzzelli, J.3    Stolz, J.F.4    Oremland, R.S.5
  • 8
    • 13544263302 scopus 로고    scopus 로고
    • Genes and enzymes involved in bacterial oxidation and reduction of inorganic arsenic
    • Silver S., and Phung L.T. Genes and enzymes involved in bacterial oxidation and reduction of inorganic arsenic. Appl. Environ. Microbiol. 71 (2005) 599-608
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 599-608
    • Silver, S.1    Phung, L.T.2
  • 10
    • 0027104536 scopus 로고
    • The purification and characterization of arsenite oxidase from Alcaligenes faecalis, a molybdenum-containing hydroxylase
    • Anderson G.L., Williams J., and Hille R. The purification and characterization of arsenite oxidase from Alcaligenes faecalis, a molybdenum-containing hydroxylase. J. Biol. Chem. 267 (1992) 23674-23682
    • (1992) J. Biol. Chem. , vol.267 , pp. 23674-23682
    • Anderson, G.L.1    Williams, J.2    Hille, R.3
  • 12
    • 33947186216 scopus 로고    scopus 로고
    • Alkalilimnicola ehrlichii sp. nov., a novel arsenite-oxidizing haloalkaliphilic gamma proteobacterium capable of chemoautotrophic or heterotrophic growth with nitrate or oxygen as the electron acceptor
    • Hoeft S.E., Switzer Blum J., Stolz J.F., Tabita F.R., Witte B., King G.M., Santini J.M., and Oremland R.S. Alkalilimnicola ehrlichii sp. nov., a novel arsenite-oxidizing haloalkaliphilic gamma proteobacterium capable of chemoautotrophic or heterotrophic growth with nitrate or oxygen as the electron acceptor. Int. J. Syst. Evol. Microbiol. 57 (2007) 504-512
    • (2007) Int. J. Syst. Evol. Microbiol. , vol.57 , pp. 504-512
    • Hoeft, S.E.1    Switzer Blum, J.2    Stolz, J.F.3    Tabita, F.R.4    Witte, B.5    King, G.M.6    Santini, J.M.7    Oremland, R.S.8
  • 14
    • 0141591471 scopus 로고    scopus 로고
    • Genetic identification of a respiratory arsenate reductase
    • Saltikov C.W., and Newman D.K. Genetic identification of a respiratory arsenate reductase. Proc. Natl. Acad. Sci. USA 100 (2003) 10983-10988
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 10983-10988
    • Saltikov, C.W.1    Newman, D.K.2
  • 16
    • 0017616853 scopus 로고
    • Sites and specificity of the reaction of bipyridylium compounds with anaerobic respiratory enzymes of Escherichia coli
    • Jones R.W., and Garland P.B. Sites and specificity of the reaction of bipyridylium compounds with anaerobic respiratory enzymes of Escherichia coli. Biochem. J. 164 (1977) 199-211
    • (1977) Biochem. J. , vol.164 , pp. 199-211
    • Jones, R.W.1    Garland, P.B.2
  • 17
    • 34548178909 scopus 로고    scopus 로고
    • In-gel digestion for mass spectrometric characterization of proteins and proteomes
    • Shevchenko A., Tomas H., Havlis J., Olsen J.V., and Mann M. In-gel digestion for mass spectrometric characterization of proteins and proteomes. Nat. Protoc. 1 (2006) 2856-2860
    • (2006) Nat. Protoc. , vol.1 , pp. 2856-2860
    • Shevchenko, A.1    Tomas, H.2    Havlis, J.3    Olsen, J.V.4    Mann, M.5
  • 20
    • 37549027623 scopus 로고    scopus 로고
    • Characterization of the arsenate respiratory reductase from Shewanella sp. strain ANA-3
    • Malasarn D., Keeffe J.R., and Newman D.K. Characterization of the arsenate respiratory reductase from Shewanella sp. strain ANA-3. J. Bacteriol. 190 (2008) 135-142
    • (2008) J. Bacteriol. , vol.190 , pp. 135-142
    • Malasarn, D.1    Keeffe, J.R.2    Newman, D.K.3
  • 21
    • 0017232611 scopus 로고
    • Mobility of sodium-dodecyl sulphate-protein complexes
    • Dunker A.K., and Kenyon A.J. Mobility of sodium-dodecyl sulphate-protein complexes. Biochem. J. 153 (1976) 191-197
    • (1976) Biochem. J. , vol.153 , pp. 191-197
    • Dunker, A.K.1    Kenyon, A.J.2
  • 23
    • 0001273302 scopus 로고
    • The principle of microscope reversibility
    • Tolman R.C. The principle of microscope reversibility. Proc. Natl. Acad. Sci. USA 11 (1925) 436-439
    • (1925) Proc. Natl. Acad. Sci. USA , vol.11 , pp. 436-439
    • Tolman, R.C.1
  • 24
    • 0029159268 scopus 로고
    • Direct oxygen atom transfer in the mechanism of action in Rhodobacter sphaeroides dimethyl sulfoxide reductase
    • Schultz B.E., Hille R., and Holme R.H. Direct oxygen atom transfer in the mechanism of action in Rhodobacter sphaeroides dimethyl sulfoxide reductase. J. Am. Chem. Soc. 117 (1995) 827-828
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 827-828
    • Schultz, B.E.1    Hille, R.2    Holme, R.H.3
  • 26
    • 1042265201 scopus 로고    scopus 로고
    • Electrochemical studies of arsenite oxidase: an unusual example of a highly cooperative two-electron molybdenum center
    • Hoke K.R., Cobb N., Armstrong F.A., and Hille R. Electrochemical studies of arsenite oxidase: an unusual example of a highly cooperative two-electron molybdenum center. Biochemistry 43 (2004) 1667-1674
    • (2004) Biochemistry , vol.43 , pp. 1667-1674
    • Hoke, K.R.1    Cobb, N.2    Armstrong, F.A.3    Hille, R.4
  • 27
    • 0035095129 scopus 로고    scopus 로고
    • Crystal structure of the 100 kDa arsenite oxidase from Alcaligenes faecalis in two crystal forms at 1.64 and 2.06 Å
    • Ellis P.J., Conrads T., Hille R., and Kuhn P. Crystal structure of the 100 kDa arsenite oxidase from Alcaligenes faecalis in two crystal forms at 1.64 and 2.06 Å. Structure 9 (2001) 125-132
    • (2001) Structure , vol.9 , pp. 125-132
    • Ellis, P.J.1    Conrads, T.2    Hille, R.3    Kuhn, P.4
  • 28
    • 43049125503 scopus 로고    scopus 로고
    • Design, syntheses, and characterization of dioxo-molybdenum(VI) complexes with thiolate ligands: effects of intralig and NH···S hydrogen bonding
    • Sengar R.S., Miller J.J., and Basu P. Design, syntheses, and characterization of dioxo-molybdenum(VI) complexes with thiolate ligands: effects of intralig and NH···S hydrogen bonding. Dalton Trans. 2 (2008) 2569-2577
    • (2008) Dalton Trans. , vol.2 , pp. 2569-2577
    • Sengar, R.S.1    Miller, J.J.2    Basu, P.3
  • 29
    • 0037060707 scopus 로고    scopus 로고
    • Synthesis, characterization, electrochemistry, electronic structure, and isomerization in mononuclear oxo-molybdenum(V) complexes: the serine gate hypothesis in the function of DMSO reductases
    • Kail B., Nemykin V.N., Davie S.R., Carrano C.J., Hammes B., and Basu P. Synthesis, characterization, electrochemistry, electronic structure, and isomerization in mononuclear oxo-molybdenum(V) complexes: the serine gate hypothesis in the function of DMSO reductases. Inorg. Chem. 41 (2002) 1281-1291
    • (2002) Inorg. Chem. , vol.41 , pp. 1281-1291
    • Kail, B.1    Nemykin, V.N.2    Davie, S.R.3    Carrano, C.J.4    Hammes, B.5    Basu, P.6
  • 31
    • 49249132556 scopus 로고    scopus 로고
    • Enzyme phylogenies as markers for the oxidation state of the environment: the case of respiratory arsenate reductase and related enzymes
    • Duval S., Ducluzeau A.-L., Nitschke W., and Schoepp-Cothenet B. Enzyme phylogenies as markers for the oxidation state of the environment: the case of respiratory arsenate reductase and related enzymes. BMC Evol. Biol. 8 (2008) 206
    • (2008) BMC Evol. Biol. , vol.8 , pp. 206
    • Duval, S.1    Ducluzeau, A.-L.2    Nitschke, W.3    Schoepp-Cothenet, B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.