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Volumn 164, Issue 6, 2009, Pages 613-623

Identification and characterization of four strains of Acidithiobacillus ferrooxidans isolated from different sites in China

Author keywords

Acidithiobacillus ferrooxidans; Gene cloning; Genetic polymorphism; Physiological properties; Substrate oxidizing activity

Indexed keywords

BIOCHEMISTRY; CHLORINE COMPOUNDS; CLONING; DNA; GENES; HEAVY METALS; IRON; METAL IONS; MOLECULAR BIOLOGY; NUCLEIC ACIDS; PH EFFECTS; POLYMORPHISM; PYRITES; SUBSTRATES; SULFUR;

EID: 70449133385     PISSN: 09445013     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.micres.2007.09.002     Document Type: Article
Times cited : (28)

References (31)
  • 1
    • 0032755413 scopus 로고    scopus 로고
    • Characterization of an operon encoding two c-type cytochromes, an aa3-type cytochrome oxidase, and rusticyanin in Thiobacillus ferroxidans ATCC 33020
    • Appia-Ayme C., Guiliani N., Ratouchniak J., and Bonnefoy V. Characterization of an operon encoding two c-type cytochromes, an aa3-type cytochrome oxidase, and rusticyanin in Thiobacillus ferroxidans ATCC 33020. Appl Environ Microbiol 65 (1999) 4781-4787
    • (1999) Appl Environ Microbiol , vol.65 , pp. 4781-4787
    • Appia-Ayme, C.1    Guiliani, N.2    Ratouchniak, J.3    Bonnefoy, V.4
  • 2
    • 27644482059 scopus 로고    scopus 로고
    • Phenotypic characteristics of Thiobacillus ferrooxidans strains
    • Ageeva S.N., Kondrat'eva T.F., and Karavaiko G.I. Phenotypic characteristics of Thiobacillus ferrooxidans strains. Microbiology 70 (2001) 186-194
    • (2001) Microbiology , vol.70 , pp. 186-194
    • Ageeva, S.N.1    Kondrat'eva, T.F.2    Karavaiko, G.I.3
  • 4
    • 19044374613 scopus 로고    scopus 로고
    • The HiPIP from the acidophilic Acidithiobacillus ferrooxidans is correctly processed and translocated in Escherichia coli, in spite of the periplasm pH difference between these two micro-organisms
    • Bruscella P., Cassagnaud L., Ratouchniak J., Brasseur G., Lojou E., Amils R., et al. The HiPIP from the acidophilic Acidithiobacillus ferrooxidans is correctly processed and translocated in Escherichia coli, in spite of the periplasm pH difference between these two micro-organisms. Microbiology 151 (2005) 1421-1431
    • (2005) Microbiology , vol.151 , pp. 1421-1431
    • Bruscella, P.1    Cassagnaud, L.2    Ratouchniak, J.3    Brasseur, G.4    Lojou, E.5    Amils, R.6
  • 5
    • 0017871744 scopus 로고
    • The purification and some properties of rusticyanin, a blue copper protein involved in iron(II) oxidation from Thiobacillus ferrooxidans
    • Cox J.C., and Boxer D.H. The purification and some properties of rusticyanin, a blue copper protein involved in iron(II) oxidation from Thiobacillus ferrooxidans. Biochem J 174 (1978) 497-502
    • (1978) Biochem J , vol.174 , pp. 497-502
    • Cox, J.C.1    Boxer, D.H.2
  • 6
    • 0001165287 scopus 로고
    • The role of rusticyanin, a blue copper protein, in the electron transport chain of Thiobacillus ferrooxidans grown on iron or thiosulfate
    • Cox J.C., and Boxer D.H. The role of rusticyanin, a blue copper protein, in the electron transport chain of Thiobacillus ferrooxidans grown on iron or thiosulfate. Biotechnol Appl Biochem 8 (1986) 269-275
    • (1986) Biotechnol Appl Biochem , vol.8 , pp. 269-275
    • Cox, J.C.1    Boxer, D.H.2
  • 7
    • 0000351245 scopus 로고
    • The extraction of metals from ores using bacterial
    • Ewart D.K., and Hugues N.H. The extraction of metals from ores using bacterial. Adv Inorg Chem 36 (1991) 103-135
    • (1991) Adv Inorg Chem , vol.36 , pp. 103-135
    • Ewart, D.K.1    Hugues, N.H.2
  • 8
    • 0000949929 scopus 로고
    • Fe(II)-oxidizing enzyme purified from Thiobacillus ferrooxidans
    • Fukumori Y., Yano T., Sato A., and Yamanaka T. Fe(II)-oxidizing enzyme purified from Thiobacillus ferrooxidans. FEMS Microbiol Lett 50 (1988) 169-172
    • (1988) FEMS Microbiol Lett , vol.50 , pp. 169-172
    • Fukumori, Y.1    Yano, T.2    Sato, A.3    Yamanaka, T.4
  • 9
    • 0032697794 scopus 로고    scopus 로고
    • Interaction-induced redox switch in the electron transfer complex rusticyanin-cytochrome c4
    • Giudici-Orticoni M.T., Guerlesquin F., Bruschi M., and Nitschke W. Interaction-induced redox switch in the electron transfer complex rusticyanin-cytochrome c4. J Biol Chem 274 (1999) 30365-30369
    • (1999) J Biol Chem , vol.274 , pp. 30365-30369
    • Giudici-Orticoni, M.T.1    Guerlesquin, F.2    Bruschi, M.3    Nitschke, W.4
  • 10
    • 0020053764 scopus 로고
    • Genomic and physiological diversity amongst strains of Thiobacillus ferrooxidans and genomic comparison with Thiobacillus thiooxidans
    • Harrison A.P. Genomic and physiological diversity amongst strains of Thiobacillus ferrooxidans and genomic comparison with Thiobacillus thiooxidans. Arch Microbiol 131 (1982) 68-76
    • (1982) Arch Microbiol , vol.131 , pp. 68-76
    • Harrison, A.P.1
  • 11
    • 33645320560 scopus 로고    scopus 로고
    • Studies of polymorphisms of Thiobacillus ferrooxidans using RAPD
    • (abstract in English)
    • He Z.G., Hu Y.H., Hu W.X., Zhong H., Xu J., and Zhu M. Studies of polymorphisms of Thiobacillus ferrooxidans using RAPD. Hereditas 26 (2004) 69-74 (abstract in English)
    • (2004) Hereditas , vol.26 , pp. 69-74
    • He, Z.G.1    Hu, Y.H.2    Hu, W.X.3    Zhong, H.4    Xu, J.5    Zhu, M.6
  • 12
    • 0030951541 scopus 로고    scopus 로고
    • Genomic organization of the acidophilic chemolithoautotrophic bacterium Thiobacillus ferrooxidans ATCC 21834
    • Irazabal N., Marin I., and Amils R. Genomic organization of the acidophilic chemolithoautotrophic bacterium Thiobacillus ferrooxidans ATCC 21834. J Bacteriol 179 (1997) 1946-1950
    • (1997) J Bacteriol , vol.179 , pp. 1946-1950
    • Irazabal, N.1    Marin, I.2    Amils, R.3
  • 13
    • 0024980091 scopus 로고
    • Cytochrome oxidase of an acidophilic iron-oxidizing bacterium, Thiobacillus ferrooxidans, functions at pH 3.5
    • Kai M., Yano T., Fukumori Y., and Yamanaka T. Cytochrome oxidase of an acidophilic iron-oxidizing bacterium, Thiobacillus ferrooxidans, functions at pH 3.5. Biochem Biophys Res Commun 160 (1989) 839-843
    • (1989) Biochem Biophys Res Commun , vol.160 , pp. 839-843
    • Kai, M.1    Yano, T.2    Fukumori, Y.3    Yamanaka, T.4
  • 15
    • 0026655489 scopus 로고
    • Molecular cloning of the gene encoding Thiobacillus ferrooxidans Fe(I1) oxidase, high homology of the gene product with HiPIP
    • Kusano T., Takeshima T., Sugawara K., Inoue C., Shiratori T., Yoano T., et al. Molecular cloning of the gene encoding Thiobacillus ferrooxidans Fe(I1) oxidase, high homology of the gene product with HiPIP. J Biol Chem 67 (1992) 11242-11247
    • (1992) J Biol Chem , vol.67 , pp. 11242-11247
    • Kusano, T.1    Takeshima, T.2    Sugawara, K.3    Inoue, C.4    Shiratori, T.5    Yoano, T.6
  • 16
    • 0011118573 scopus 로고
    • Gold recovery from arsenopyrite/pyrite ore by bacterial leaching and cyanidation
    • Rossi G., and Torma A.E. (Eds), Associazione Mineraria Sarda, Iglesias, Italy
    • Livesey-Goldblatt E., Norman P., and Livesey-Goldblatt D.R. Gold recovery from arsenopyrite/pyrite ore by bacterial leaching and cyanidation. In: Rossi G., and Torma A.E. (Eds). Recent progress in biohydrometallurgy (1983), Associazione Mineraria Sarda, Iglesias, Italy 627-641
    • (1983) Recent progress in biohydrometallurgy , pp. 627-641
    • Livesey-Goldblatt, E.1    Norman, P.2    Livesey-Goldblatt, D.R.3
  • 17
    • 0028179505 scopus 로고
    • The chemolithotrophic bacterium Thiobacillus ferrooxidans
    • Leduc L.G., and Ferroni G.D. The chemolithotrophic bacterium Thiobacillus ferrooxidans. FEMS Microbiol Lett 14 (1994) 103-120
    • (1994) FEMS Microbiol Lett , vol.14 , pp. 103-120
    • Leduc, L.G.1    Ferroni, G.D.2
  • 18
    • 0000198211 scopus 로고
    • Precise measurement of the G+C content of deoxyribonucleic acid by high-performance liquid chromatography
    • Mesbah M., Premachandran U., and Whitman W.B. Precise measurement of the G+C content of deoxyribonucleic acid by high-performance liquid chromatography. Int J Syst Bacteriol 39 (1989) 159-167
    • (1989) Int J Syst Bacteriol , vol.39 , pp. 159-167
    • Mesbah, M.1    Premachandran, U.2    Whitman, W.B.3
  • 19
    • 0003564799 scopus 로고
    • Bioleaching of uranium
    • Ehrlich H.L., and Brierley C.L. (Eds), McGraw-Hill Book Co., New York
    • McCready R.G.L., and Gould W.D. Bioleaching of uranium. In: Ehrlich H.L., and Brierley C.L. (Eds). Microbial mineral recovery (1990), McGraw-Hill Book Co., New York 107-126
    • (1990) Microbial mineral recovery , pp. 107-126
    • McCready, R.G.L.1    Gould, W.D.2
  • 20
    • 0037409542 scopus 로고    scopus 로고
    • Complexation of uranium (VI) by three eco-types of Acidithiobacillus ferrooxidans studied using time-resolved laser-induced fluorescence spectroscopy and infrared spectroscopy
    • Merroun M.L., Geipel G., Nicolai R., Heise K.H., and Selenska-Pobell S. Complexation of uranium (VI) by three eco-types of Acidithiobacillus ferrooxidans studied using time-resolved laser-induced fluorescence spectroscopy and infrared spectroscopy. Biometals 16 (2003) 331-339
    • (2003) Biometals , vol.16 , pp. 331-339
    • Merroun, M.L.1    Geipel, G.2    Nicolai, R.3    Heise, K.H.4    Selenska-Pobell, S.5
  • 21
    • 0028202450 scopus 로고
    • Molecular genetics of Thiobacillus ferrooxidans
    • Rawlings D.E., and Kusano T. Molecular genetics of Thiobacillus ferrooxidans. Microbiol Rev 3 (1994) 39-55
    • (1994) Microbiol Rev , vol.3 , pp. 39-55
    • Rawlings, D.E.1    Kusano, T.2
  • 22
    • 26844536951 scopus 로고    scopus 로고
    • Characteristics and adaptability of iron- and sulfur-oxidizing microorganisms used for the recovery of metals from minerals and their concentrates
    • Rawlings D.E. Characteristics and adaptability of iron- and sulfur-oxidizing microorganisms used for the recovery of metals from minerals and their concentrates. Microb Cell Factories 4 (2005) 13-18
    • (2005) Microb Cell Factories , vol.4 , pp. 13-18
    • Rawlings, D.E.1
  • 23
    • 1642480180 scopus 로고    scopus 로고
    • Bioleaching review part A: progress in bioleaching: fundamentals and mechanism of bacterial metal sulfide oxidation
    • Rohwerder T., Gehrke T., Kinzler K., and Sand W. Bioleaching review part A: progress in bioleaching: fundamentals and mechanism of bacterial metal sulfide oxidation. Appl Microbiol Biotechnol 63 (2003) 239-248
    • (2003) Appl Microbiol Biotechnol , vol.63 , pp. 239-248
    • Rohwerder, T.1    Gehrke, T.2    Kinzler, K.3    Sand, W.4
  • 25
    • 0141937980 scopus 로고    scopus 로고
    • Surface characterization of Acidithiobacillus ferrooxidans cells grown under different conditions
    • Sharma P.K., Das A., Rao K.H., and Forssberg K.S.E. Surface characterization of Acidithiobacillus ferrooxidans cells grown under different conditions. Hydrometallurgy 71 (2003) 285-292
    • (2003) Hydrometallurgy , vol.71 , pp. 285-292
    • Sharma, P.K.1    Das, A.2    Rao, K.H.3    Forssberg, K.S.E.4
  • 26
    • 0021715576 scopus 로고
    • Determination of DNA base composition by reversed-phase high-performance liquid chromatography
    • Tamaoka J., and Komagata K. Determination of DNA base composition by reversed-phase high-performance liquid chromatography. FEMS Microbiol 25 (1984) 125-128
    • (1984) FEMS Microbiol , vol.25 , pp. 125-128
    • Tamaoka, J.1    Komagata, K.2
  • 27
    • 84982585936 scopus 로고
    • Molecular aspects of the electron transfer system which participates in the oxidation of ferrous ion by Thiobacillus ferrooxidans
    • Yamanaka T., and Fukumori Y. Molecular aspects of the electron transfer system which participates in the oxidation of ferrous ion by Thiobacillus ferrooxidans. FEMS Microbiol Lett 17 (1995) 401-413
    • (1995) FEMS Microbiol Lett , vol.17 , pp. 401-413
    • Yamanaka, T.1    Fukumori, Y.2
  • 28
    • 0036397766 scopus 로고    scopus 로고
    • Numerical modeling of ferrous-ion oxidation rate in Acidithiobacillus ferrooxidans ATCC 23270: optimization of culture conditions through statistically designed experiments
    • Yasser R.A., Wael R.A., Rogelio Z., and James R.P. Numerical modeling of ferrous-ion oxidation rate in Acidithiobacillus ferrooxidans ATCC 23270: optimization of culture conditions through statistically designed experiments. Acta Microbiol Pol 51 (2002) 225-235
    • (2002) Acta Microbiol Pol , vol.51 , pp. 225-235
    • Yasser, R.A.1    Wael, R.A.2    Rogelio, Z.3    James, R.P.4
  • 29
    • 0036134778 scopus 로고    scopus 로고
    • The high molecular weight cytochrome c Cyc2 of Acidithiobacillus ferrooxidans is an outer membrane protein
    • Yarzabal A., Brasseur G., Ratouchniak J., Lund K., Lemesle-Meunier D., DeMoss J.A., et al. The high molecular weight cytochrome c Cyc2 of Acidithiobacillus ferrooxidans is an outer membrane protein. J Bacteriol 184 (2002) 313-317
    • (2002) J Bacteriol , vol.184 , pp. 313-317
    • Yarzabal, A.1    Brasseur, G.2    Ratouchniak, J.3    Lund, K.4    Lemesle-Meunier, D.5    DeMoss, J.A.6
  • 30
    • 4344634473 scopus 로고    scopus 로고
    • Regulation of the expression of the Acidithiobacillus ferrooxidans rus operon encoding two cytochromes c, a cytochrome oxidase and rusticyanin
    • Yarzabal A., Appia-Ayme C., Ratouchniak J., and Bonnefoy V. Regulation of the expression of the Acidithiobacillus ferrooxidans rus operon encoding two cytochromes c, a cytochrome oxidase and rusticyanin. Microbiology 150 (2004) 2113-2123
    • (2004) Microbiology , vol.150 , pp. 2113-2123
    • Yarzabal, A.1    Appia-Ayme, C.2    Ratouchniak, J.3    Bonnefoy, V.4
  • 31
    • 70449086371 scopus 로고    scopus 로고
    • Study on growth conditions of desulfurization microorganism
    • (abstract in English)
    • Zhang Y., Li X.D., and Wang Y.G. Study on growth conditions of desulfurization microorganism. J Shenyang Univ 17 (2005) 44-46 (abstract in English)
    • (2005) J Shenyang Univ , vol.17 , pp. 44-46
    • Zhang, Y.1    Li, X.D.2    Wang, Y.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.