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Volumn 194, Issue 3, 2012, Pages 677-685

The sulfur oxygenase reductase from the mesophilic bacterium Halothiobacillus neapolitanus is a highly active thermozyme

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; HYDROGEN SULFIDE; SULFITE; SULFUR OXYGENASE REDUCTASE; THIOSULFATE; UNCLASSIFIED DRUG;

EID: 84855915891     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.06531-11     Document Type: Article
Times cited : (22)

References (52)
  • 1
    • 84857922795 scopus 로고    scopus 로고
    • Phylogenetic assessment of culture collection strains of Thiobacillus thioparus, and definitive 16S rRNA gene sequences for T. thioparus, T. denitrificans, and Halothiobacillus neapolitanus
    • doi:10.1007/s00203-011-0747-0. 21 August [Epub ahead of print.]
    • Boden R, et al. 21 August 2011. Phylogenetic assessment of culture collection strains of Thiobacillus thioparus, and definitive 16S rRNA gene sequences for T. thioparus, T. denitrificans, and Halothiobacillus neapolitanus. Arch. Microbiol. doi:10.1007/s00203-011-0747-0. [Epub ahead of print.]
    • (2011) Arch. Microbiol.
    • Boden, R.1
  • 2
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 3
    • 84959252611 scopus 로고    scopus 로고
    • Microbial leaching of metals
    • Rehm HJ (ed), Special processes. Wiley-VCH, Weinheim, Germany
    • Brandl H. 2001. Microbial leaching of metals, p 191-224. In Rehm HJ (ed), Biotechnology, vol 10. Special processes. Wiley-VCH, Weinheim, Germany.
    • (2001) Biotechnology , vol.10 , pp. 191-224
    • Brandl, H.1
  • 4
    • 13544252537 scopus 로고    scopus 로고
    • Key role of cysteine residues in catalysis and subcellular localization of sulfur oxygenase-reductase of Acidianus tengchongensis
    • Chen ZW, Jiang CY, She Q, Liu SJ, Zhou PJ. 2005. Key role of cysteine residues in catalysis and subcellular localization of sulfur oxygenase-reductase of Acidianus tengchongensis. Appl. Environ. Microbiol. 71: 621-628.
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 621-628
    • Chen, Z.W.1    Jiang, C.Y.2    She, Q.3    Liu, S.J.4    Zhou, P.J.5
  • 5
    • 33847168962 scopus 로고    scopus 로고
    • Novel bacterial sulfur oxygenase reductases from bioreactors treating gold-bearing concentrates
    • Chen ZW, et al. 2007. Novel bacterial sulfur oxygenase reductases from bioreactors treating gold-bearing concentrates. Appl. Microbiol. Biotechnol. 74:688-698.
    • (2007) Appl. Microbiol. Biotechnol. , vol.74 , pp. 688-698
    • Chen, Z.W.1
  • 8
    • 0022977080 scopus 로고
    • Evidence for the existence of a sulfur oxygenase in Sulfolobus brierleyi
    • Emmel T, Sand W, König WA, Bock E. 1986. Evidence for the existence of a sulfur oxygenase in Sulfolobus brierleyi. J. Gen. Microbiol. 132: 3415-3420.
    • (1986) J. Gen. Microbiol. , vol.132 , pp. 3415-3420
    • Emmel, T.1    Sand, W.2    König, W.A.3    Bock, E.4
  • 9
    • 78651145002 scopus 로고
    • Simple serum iron method using new sensitive chromogen tripyridyl-s-triazine
    • Fischer DS, Price DC. 1964. Simple serum iron method using new sensitive chromogen tripyridyl-s-triazine. Clin. Chem. 10:21-25.
    • (1964) Clin. Chem. , vol.10 , pp. 21-25
    • Fischer, D.S.1    Price, D.C.2
  • 11
    • 0034672173 scopus 로고    scopus 로고
    • Cloning and heterologous expression of a sulfur oxygenase/reductase gene from the thermoacidophilic archaeon Acidianus sp. S5 in Escherichia coli
    • He Z, Li Y, Zhou P, Liu S. 2000. Cloning and heterologous expression of a sulfur oxygenase/reductase gene from the thermoacidophilic archaeon Acidianus sp. S5 in Escherichia coli. FEMS Microbiol. Lett. 193:217-221.
    • (2000) FEMS Microbiol. Lett. , vol.193 , pp. 217-221
    • He, Z.1    Li, Y.2    Zhou, P.3    Liu, S.4
  • 12
    • 47349124813 scopus 로고    scopus 로고
    • Comparative architecture of octahedral protein cages. I. Indexed enclosing forms
    • Janner A. 2008. Comparative architecture of octahedral protein cages. I. Indexed enclosing forms. Acta Crystallogr. Sect. A 64:494-502.
    • (2008) Acta Crystallogr. Sect. A , vol.64 , pp. 494-502
    • Janner, A.1
  • 13
    • 47349089091 scopus 로고    scopus 로고
    • Comparative architecture of octahedral protein cages. II. Interplay between structural elements
    • Janner A. 2008. Comparative architecture of octahedral protein cages. II. Interplay between structural elements. Acta Crystallogr. Sect. A 64: 503-512.
    • (2008) Acta Crystallogr. Sect. A , vol.64 , pp. 503-512
    • Janner, A.1
  • 14
    • 72449122296 scopus 로고    scopus 로고
    • Sulfur oxygenase reductase in different Acidithiobacillus caldus-like strains
    • Janosch C, et al. 2009. Sulfur oxygenase reductase in different Acidithiobacillus caldus-like strains. Adv. Materials Res. 71-73:239-243.
    • (2009) Adv. Materials Res. , vol.71-73 , pp. 239-243
    • Janosch, C.1
  • 15
    • 69849113899 scopus 로고    scopus 로고
    • Solubility of cyclooctasulfur in pure water and sea water at different temperatures
    • Kamyshny A. 2009. Solubility of cyclooctasulfur in pure water and sea water at different temperatures. Geochim. Cosmochim. Acta 73: 6022-6028.
    • (2009) Geochim. Cosmochim. Acta , vol.73 , pp. 6022-6028
    • Kamyshny, A.1
  • 16
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the Web: a case study using the Phyre server
    • Kelley LA, Sternberg MJ. 2009. Protein structure prediction on the Web: a case study using the Phyre server. Nat. Protoc. 4:363-371.
    • (2009) Nat. Protoc. , vol.4 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.J.2
  • 17
    • 33747887884 scopus 로고    scopus 로고
    • Halothiobacillus
    • Brenner DJ, Krieg NR, Staley JT, Garrity GM (ed), 2nd ed. Springer, New York, NY
    • Kelly DP, Wood AP. 2005. Halothiobacillus, p 58-59. In Brenner DJ, Krieg NR, Staley JT, Garrity GM (ed), Bergey's manual of systematic bacteriology, 2nd ed, vol 2. Springer, New York, NY.
    • (2005) Bergey's manual of systematic bacteriology , vol.2 , pp. 58-59
    • Kelly, D.P.1    Wood, A.P.2
  • 18
    • 0034065246 scopus 로고    scopus 로고
    • Reclassification of some species of Thiobacillus to the newly designated genera Acidithiobacillus gen. nov., Halothiobacillus gen. nov. and Thermithiobacillus gen. nov
    • Kelly DP, Wood AP. 2000. Reclassification of some species of Thiobacillus to the newly designated genera Acidithiobacillus gen. nov., Halothiobacillus gen. nov. and Thermithiobacillus gen. nov. Int. J. Syst. Evol. Microbiol. 50(Part 2):511-516.
    • (2000) Int. J. Syst. Evol. Microbiol. , vol.50 , Issue.PART 2 , pp. 511-516
    • Kelly, D.P.1    Wood, A.P.2
  • 19
    • 70349655938 scopus 로고    scopus 로고
    • Oxidation of sulfur and inorganic sulfur compounds in Acidianus ambivalens
    • Dahl C, Friedrich CG (ed), Springer, Berlin, Germany
    • Kletzin A. 2008. Oxidation of sulfur and inorganic sulfur compounds in Acidianus ambivalens, p 184-201. In Dahl C, Friedrich CG (ed), Microbial sulfur metabolism. Springer, Berlin, Germany.
    • (2008) Microbial sulfur metabolism , pp. 184-201
    • Kletzin, A.1
  • 20
    • 0024637896 scopus 로고
    • Coupled enzymatic production of sulfite, thiosulfate, and hydrogen sulfide from sulfur: purification and properties of a sulfur oxygenase reductase from the facultatively anaerobic archaebacterium Desulfurolobus ambivalens
    • Kletzin A. 1989. Coupled enzymatic production of sulfite, thiosulfate, and hydrogen sulfide from sulfur: purification and properties of a sulfur oxygenase reductase from the facultatively anaerobic archaebacterium Desulfurolobus ambivalens. J. Bacteriol. 171:1638-1643.
    • (1989) J. Bacteriol. , vol.171 , pp. 1638-1643
    • Kletzin, A.1
  • 21
    • 0026706351 scopus 로고
    • Molecular characterization of the sor gene, which encodes the sulfur oxygenase reductase of the thermoacidophilic archaeon Desulfurolobus ambivalens
    • Kletzin A. 1992. Molecular characterization of the sor gene, which encodes the sulfur oxygenase reductase of the thermoacidophilic archaeon Desulfurolobus ambivalens. J. Bacteriol. 174:5854-5859.
    • (1992) J. Bacteriol. , vol.174 , pp. 5854-5859
    • Kletzin, A.1
  • 22
    • 77957963055 scopus 로고    scopus 로고
    • Achieving reliability and high accuracy in automated protein docking: ClusPro, PIPER, SDU, and stability analysis in CAPRI rounds 13-19
    • Kozakov D, et al. 2010. Achieving reliability and high accuracy in automated protein docking: ClusPro, PIPER, SDU, and stability analysis in CAPRI rounds 13-19. Proteins 78:3124-3130.
    • (2010) Proteins , vol.78 , pp. 3124-3130
    • Kozakov, D.1
  • 23
    • 34250872670 scopus 로고
    • The stability of the fullerenes C-24, C-28, C-32, C-36, C-50, C-60 and C-70
    • Kroto HW. 1987. The stability of the fullerenes C-24, C-28, C-32, C-36, C-50, C-60 and C-70. Nature 329:529-531.
    • (1987) Nature , vol.329 , pp. 529-531
    • Kroto, H.W.1
  • 24
    • 29244447181 scopus 로고    scopus 로고
    • Kalign-an accurate and fast multiple sequence alignment algorithm
    • Lassmann T, Sonnhammer EL. 2005. Kalign-an accurate and fast multiple sequence alignment algorithm. BMC Bioinformatics 6:298.
    • (2005) BMC Bioinformatics , vol.6 , pp. 298
    • Lassmann, T.1    Sonnhammer, E.L.2
  • 25
    • 41149124804 scopus 로고    scopus 로고
    • Crystal structure studies on sulfur oxygenase reductase from Acidianus tengchongensis
    • Li M, et al. 2008. Crystal structure studies on sulfur oxygenase reductase from Acidianus tengchongensis. Biochem. Biophys. Res. Commun. 369: 919-923.
    • (2008) Biochem. Biophys. Res. Commun. , vol.369 , pp. 919-923
    • Li, M.1
  • 26
    • 79961131441 scopus 로고    scopus 로고
    • Sulfur metabolism in the extreme acidophile Acidithiobacillus caldus
    • Mangold S, Valdés J, Holmes D, Dopson M. 2011. Sulfur metabolism in the extreme acidophile Acidithiobacillus caldus. Front. Microbiol. 2:17.
    • (2011) Front. Microbiol. , vol.2 , pp. 17
    • Mangold, S.1    Valdés, J.2    Holmes, D.3    Dopson, M.4
  • 27
    • 0001369336 scopus 로고
    • A buffer solution for colorimetric comparison
    • McIlvaine TC. 1921. A buffer solution for colorimetric comparison. J. Biol. Chem. 49:183-186.
    • (1921) J. Biol. Chem. , vol.49 , pp. 183-186
    • McIlvaine, T.C.1
  • 28
    • 0000720562 scopus 로고
    • Chemiosmotic H+ cycling across the plasma membrane of the thermoacidophilic archaebacterium Sulfolobus acidocaldarius
    • Moll R, Schäfer G. 1988. Chemiosmotic H+ cycling across the plasma membrane of the thermoacidophilic archaebacterium Sulfolobus acidocaldarius. FEBS Lett. 232:359-363.
    • (1988) FEBS Lett. , vol.232 , pp. 359-363
    • Moll, R.1    Schäfer, G.2
  • 29
    • 0000307959 scopus 로고
    • Species of sulphur bacteria associated with the corrosion of concrete
    • Parker CD. 1947. Species of sulphur bacteria associated with the corrosion of concrete. Nature 159:439.
    • (1947) Nature , vol.159 , pp. 439
    • Parker, C.D.1
  • 30
    • 40349091401 scopus 로고    scopus 로고
    • First characterisation of the active oligomer form of sulfur oxygenase reductase from the bacterium Aquifex aeolicus
    • Pelletier N, Leroy G, Guiral M, Giudici-Orticoni MT, Aubert C. 2008. First characterisation of the active oligomer form of sulfur oxygenase reductase from the bacterium Aquifex aeolicus. Extremophiles 12:205-215.
    • (2008) Extremophiles , vol.12 , pp. 205-215
    • Pelletier, N.1    Leroy, G.2    Guiral, M.3    Giudici-Orticoni, M.T.4    Aubert, C.5
  • 31
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera-a visualization system for exploratory research and analysis
    • Pettersen EF, et al. 2004. UCSF Chimera-a visualization system for exploratory research and analysis. J. Comput. Chem. 25:1605-1612.
    • (2004) J. Comput. Chem. , vol.25 , pp. 1605-1612
    • Pettersen, E.F.1
  • 32
    • 0037810930 scopus 로고    scopus 로고
    • The sulfane sulfur of persulfides is the actual substrate of the sulfur-oxidizing enzymes from Acidithiobacillus and Acidiphilium spp
    • Rohwerder T, Sand W. 2003. The sulfane sulfur of persulfides is the actual substrate of the sulfur-oxidizing enzymes from Acidithiobacillus and Acidiphilium spp. Microbiology 149:1699-1710.
    • (2003) Microbiology , vol.149 , pp. 1699-1710
    • Rohwerder, T.1    Sand, W.2
  • 33
    • 84890721622 scopus 로고
    • The chemistry of some sulphur compounds
    • Roy AB, Trudinger PA (ed), Cambridge University Press, Cambridge, United Kingdom
    • Roy AB, Trudinger PA. 1970. The chemistry of some sulphur compounds, p 7-29. In Roy AB, Trudinger PA (ed), The biochemistry of inorganic compounds of sulphur. Cambridge University Press, Cambridge, United Kingdom.
    • (1970) The biochemistry of inorganic compounds of sulphur , pp. 7-29
    • Roy, A.B.1    Trudinger, P.A.2
  • 34
    • 0017001906 scopus 로고
    • Mesophilic rod-like nonsporeforming bacterium reducing sulfates
    • In Russian
    • Rozanova EP, Nazina TN. 1976. Mesophilic rod-like nonsporeforming bacterium reducing sulfates. Mikrobiologiia 45:825-830. (In Russian.)
    • (1976) Mikrobiologiia , vol.45 , pp. 825-830
    • Rozanova, E.P.1    Nazina, T.N.2
  • 35
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfatepolyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger H, von Jagow G. 1987. Tricine-sodium dodecyl sulfatepolyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166:368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schägger, H.1    von Jagow, G.2
  • 36
    • 0028806517 scopus 로고
    • Picrophilus gen. nov., fam. nov.: a novel aerobic, heterotrophic, thermoacidophilic genus and family comprising archaea capable of growth around pH 0
    • Schleper C, et al. 1995. Picrophilus gen. nov., fam. nov.: a novel aerobic, heterotrophic, thermoacidophilic genus and family comprising archaea capable of growth around pH 0. J. Bacteriol. 177:7050-7059.
    • (1995) J. Bacteriol. , vol.177 , pp. 7050-7059
    • Schleper, C.1
  • 37
    • 1842542089 scopus 로고
    • Zur Stabilität der dünnwandigen Hohlkugel unter gleichmäßigem Außendruck
    • Schwerin E. 1922. Zur Stabilität der dünnwandigen Hohlkugel unter gleichmäßigem Außendruck. Z. Angew. Math. Mechanik 2:81-91.
    • (1922) Z. Angew. Math. Mechanik , vol.2 , pp. 81-91
    • Schwerin, E.1
  • 38
    • 0028555357 scopus 로고
    • Use of the tetracycline promoter for the tightly regulated production of a murine antibody fragment in Escherichia coli
    • Skerra A. 1994. Use of the tetracycline promoter for the tightly regulated production of a murine antibody fragment in Escherichia coli. Gene 151: 131-135.
    • (1994) Gene , vol.151 , pp. 131-135
    • Skerra, A.1
  • 39
    • 0030069026 scopus 로고    scopus 로고
    • Thermal stability of horse spleen apoferritin and human recombinant H apoferritin
    • Stefanini S, et al. 1996. Thermal stability of horse spleen apoferritin and human recombinant H apoferritin. Arch. Biochem. Biophys. 325:58-64.
    • (1996) Arch. Biochem. Biophys. , vol.325 , pp. 58-64
    • Stefanini, S.1
  • 41
    • 0642307164 scopus 로고    scopus 로고
    • Purification and properties of the sulfur oxygenase/reductase from the acidothermophilic archaeon, Acidianus strain S5
    • Sun CW, Chen ZW, He ZG, Zhou PJ, Liu SJ. 2003. Purification and properties of the sulfur oxygenase/reductase from the acidothermophilic archaeon, Acidianus strain S5. Extremophiles 7:131-134.
    • (2003) Extremophiles , vol.7 , pp. 131-134
    • Sun, C.W.1    Chen, Z.W.2    He, Z.G.3    Zhou, P.J.4    Liu, S.J.5
  • 42
    • 0013844188 scopus 로고
    • Oxidation of elemental sulfur by an enzyme system of Thiobacillus thiooxidans
    • Suzuki I. 1965. Oxidation of elemental sulfur by an enzyme system of Thiobacillus thiooxidans. Biochim. Biophys. Acta 104:359-371.
    • (1965) Biochim. Biophys. Acta , vol.104 , pp. 359-371
    • Suzuki, I.1
  • 43
    • 16544388246 scopus 로고
    • Physiological studies on thiobacilli. Part II. The metabolism of colloidal sulfur by the cell-free enzyme system of Thiobacillus thiooxidans
    • Tano T, Imai K. 1968. Physiological studies on thiobacilli. Part II. The metabolism of colloidal sulfur by the cell-free enzyme system of Thiobacillus thiooxidans. Agric. Biol. Chem. 32:51-54.
    • (1968) Agric. Biol. Chem. , vol.32 , pp. 51-54
    • Tano, T.1    Imai, K.2
  • 44
    • 34250347772 scopus 로고    scopus 로고
    • Structural analysis of CsoS1A and the protein shell of the Halothiobacillus neapolitanus carboxysome
    • Tsai Y, et al. 2007. Structural analysis of CsoS1A and the protein shell of the Halothiobacillus neapolitanus carboxysome. PLoS Biol. 5:e144.
    • (2007) PLoS Biol. , vol.5
    • Tsai, Y.1
  • 45
    • 3142776185 scopus 로고    scopus 로고
    • The sulphur oxygenase reductase from Acidianus ambivalens is a multimeric protein containing a low-potential mononuclear non-haem iron centre
    • Urich T, et al. 2004. The sulphur oxygenase reductase from Acidianus ambivalens is a multimeric protein containing a low-potential mononuclear non-haem iron centre. Biochem. J. 381:137-146.
    • (2004) Biochem. J. , vol.381 , pp. 137-146
    • Urich, T.1
  • 46
    • 33144477916 scopus 로고    scopus 로고
    • X-ray structure of a self-compartmentalizing sulfur cycle metalloenzyme
    • Urich T, Gomes CM, Kletzin A, Frazao C. 2006. X-ray structure of a self-compartmentalizing sulfur cycle metalloenzyme. Science 311: 996-1000.
    • (2006) Science , vol.311 , pp. 996-1000
    • Urich, T.1    Gomes, C.M.2    Kletzin, A.3    Frazao, C.4
  • 47
    • 21744450397 scopus 로고    scopus 로고
    • Identification of core active site residues of the sulfur oxygenase reductase from Acidianus ambivalens by site-directed mutagenesis
    • Urich T, et al. 2005. Identification of core active site residues of the sulfur oxygenase reductase from Acidianus ambivalens by site-directed mutagenesis. FEMS Microbiol. Lett. 248:171-176.
    • (2005) FEMS Microbiol. Lett. , vol.248 , pp. 171-176
    • Urich, T.1
  • 48
    • 84855953639 scopus 로고    scopus 로고
    • Substrate pathways and mechanisms of inhibition in the sulfur oxygenase reductase of Acidianus ambivalens
    • Veith A, et al. 2011. Substrate pathways and mechanisms of inhibition in the sulfur oxygenase reductase of Acidianus ambivalens. Front. Microbiol. 2:37.
    • (2011) Front. Microbiol. , vol.2 , pp. 37
    • Veith, A.1
  • 49
    • 25144470739 scopus 로고    scopus 로고
    • Halothiobacillus neapolitanus strain OSWA isolated from "The Old Sulphur Well" at Harrowgate (Yorkshire, England)
    • Wood AP, Woodall CA, Kelly DP. 2005. Halothiobacillus neapolitanus strain OSWA isolated from "The Old Sulphur Well" at Harrowgate (Yorkshire, England). Syst. Appl. Microbiol. 28:746-748.
    • (2005) Syst. Appl. Microbiol. , vol.28 , pp. 746-748
    • Wood, A.P.1    Woodall, C.A.2    Kelly, D.P.3
  • 50
    • 0032560505 scopus 로고    scopus 로고
    • Adjustment of conformational flexibility is a key event in the thermal adaptation of proteins
    • Zavodszky P, Kardos J, Svingor Petsko GA. 1998. Adjustment of conformational flexibility is a key event in the thermal adaptation of proteins. Proc. Natl. Acad. Sci. U. S. A. 95:7406-7411.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 7406-7411
    • Zavodszky, P.1    Kardos, J.2    Svingor Petsko, G.A.3
  • 51
    • 39449115394 scopus 로고    scopus 로고
    • I-TASSER server for protein 3D structure prediction
    • Zhang Y. 2008. I-TASSER server for protein 3D structure prediction. BMC Bioinformatics. 9:40.
    • (2008) BMC Bioinformatics. , vol.9 , pp. 40
    • Zhang, Y.1
  • 52
    • 0000947137 scopus 로고
    • Desulfurolobus ambivalens gen. nov., sp. nov., an autotrophic archaebacterium facultatively oxidizing and reducing sulfur
    • Zillig W, et al. 1986. Desulfurolobus ambivalens gen. nov., sp. nov., an autotrophic archaebacterium facultatively oxidizing and reducing sulfur. Syst. Appl. Microbiol. 8:197-203.
    • (1986) Syst. Appl. Microbiol. , vol.8 , pp. 197-203
    • Zillig, W.1


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