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Volumn 101, Issue 3, 2012, Pages 561-573

Kinetics of anaerobic elemental sulfur oxidation by ferric iron in Acidithiobacillus ferrooxidans and protein identification by comparative 2-DE-MS/MS

Author keywords

Acidithiobacillus; Anaerobic sulfur oxidation; Ferric iron reduction; MS analysis; Proteomics

Indexed keywords

CYTOCHROME C; DISULFIDE; FERRIC ION; PYRIDINE; RUSTICYANIN; SULFUR;

EID: 84857911928     PISSN: 00036072     EISSN: 15729699     Source Type: Journal    
DOI: 10.1007/s10482-011-9670-2     Document Type: Article
Times cited : (25)

References (59)
  • 1
    • 0025970548 scopus 로고
    • Effect of external pH perturbations on in vivo protein synthesis by the acidophilic bacterium Thiobacillus ferrooxidans
    • Amaro AM, Chamorro D, Seeger M, Arredondo R, Peirano I, Jerez CA (1991) Effect of external pH perturbations on in vivo protein synthesis by the acidophilic bacterium Thiobacillus ferrooxidans. J Bacteriol 173:910-915
    • (1991) J Bacteriol , vol.173 , pp. 910-915
    • Amaro, A.M.1    Chamorro, D.2    Seeger, M.3    Arredondo, R.4    Peirano, I.5    Jerez, C.A.6
  • 2
    • 0031726026 scopus 로고    scopus 로고
    • 552) and a high-molecular-mass cytochrome c from Thiobacillus ferrooxidans ATCC 33020
    • DOI 10.1016/S0378-1097(98)00385-1, PII S0378109798003851
    • Appia-Ayme C, Bengrine A, Cavazza C, Giudici-Orticoni MT, Bruschi M, Chippaux M, Bonnefoy V (1998) Characterization and expression of the co-transcribed cyc1 and cyc2 genes encoding the cytochrome c4 (c552) and a high-molecular- mass cytochrome c from Thiobacillus ferrooxidans ATCC 33020. FEMS Microbiol Lett 167:171-177 (Pubitemid 28479757)
    • (1998) FEMS Microbiology Letters , vol.167 , Issue.2 , pp. 171-177
    • Appia-Ayme, C.1    Bengrine, A.2    Cavazza, C.3    Giudici-Orticoni, M.-T.4    Bruschi, M.5    Chippaux, M.6    Bonnefoy, V.7
  • 3
    • 0032755413 scopus 로고    scopus 로고
    • Characterization of an operon encoding two c-type cytochromes, an aa(3)-type cytochrome oxidase, and rusticyanin in Thiobacillus ferrooxidans ATCC 33020
    • Appia-Ayme C, Guiliani N, Ratouchniak J, Bonnefoy V (1999) Characterization of an operon encoding two c-type cytochromes, an aa(3)-type cytochrome oxidase, and rusticyanin in Thiobacillus ferrooxidans ATCC 33020. Appl Environ Microbiol 65:4781-4787
    • (1999) Appl Environ Microbiol , vol.65 , pp. 4781-4787
    • Appia-Ayme, C.1    Guiliani, N.2    Ratouchniak, J.3    Bonnefoy, V.4
  • 4
    • 0037447834 scopus 로고    scopus 로고
    • Microbial communities in acid mine drainage
    • DOI 10.1016/S0168-6496(03)00028-X
    • Baker BJ, Banfield JF (2003) Microbial communities in acid mine drainage. FEMS Microbiol Ecol 44:139-152 (Pubitemid 36423410)
    • (2003) FEMS Microbiology Ecology , vol.44 , Issue.2 , pp. 139-152
    • Baker, B.J.1    Banfield, J.F.2
  • 6
    • 33747750273 scopus 로고    scopus 로고
    • Proteomic and bioinformatic analysis of iron- and sulfur-oxidizing Acidithiobacillus ferrooxidans using immobilized pH gradients and mass spectrometry
    • DOI 10.1002/pmic.200500719
    • Bouchal P, Zdrahal Z, Helanova S, Janiczek O, Hallberg KB, Mandl M (2006) Proteomic and bioinformatic analysis of iron- and sulfur-oxidizing Acidithiobacillus ferrooxidans using immobilized pH gradients and mass spectrometry. Proteomics 6:4278-4285 (Pubitemid 44277030)
    • (2006) Proteomics , vol.6 , Issue.15 , pp. 4278-4285
    • Bouchal, P.1    Zdrahal, Z.2    Helanova, S.3    Janiczek, O.4    Hallberg, K.B.5    Mandl, M.6
  • 8
    • 0344631755 scopus 로고    scopus 로고
    • In vitro characterization of peptidoglycan-associated lipoprotein (PAL)- peptidoglycan and PAL-TolB interactions
    • Bouveret E, Benedetti H, Rigal A, Loret E, Lazdunski C (1999) In vitro characterization of peptidoglycan-associated lipoprotein (PAL)-peptidoglycan and PAL-TolB interactions. J Bacteriol 181:6306-6311 (Pubitemid 29512939)
    • (1999) Journal of Bacteriology , vol.181 , Issue.20 , pp. 6306-6311
    • Bouveret, E.1    Benedetti, H.2    Rigal, A.3    Loret, E.4    Lazdunski, C.5
  • 9
    • 0037056056 scopus 로고    scopus 로고
    • 1 complex?
    • DOI 10.1016/S0005-2728(02)00251-7, PII S0005272802002517
    • Brasseur G, Bruscella P, Bonnefoy V, Lemesle-Meunier D (2002) The bc1 complex of the iron-grown acidophilic chemolithotrophic bacterium Acidithiobacillus ferrooxidans functions in the reverse but not in the forward direction. Is there a second bc1 complex? Biochim Biophys Acta 1555:37-43 (Pubitemid 35246002)
    • (2002) Biochimica et Biophysica Acta - Bioenergetics , vol.1555 , Issue.1-3 , pp. 37-43
    • Brasseur, G.1    Bruscella, P.2    Bonnefoy, V.3    Lemesle-Meunier, D.4
  • 10
    • 2642582298 scopus 로고    scopus 로고
    • 1 complexes and terminal oxidases in the extremophilic chemolithoautotrophic Acidithiobacillus ferrooxidans
    • DOI 10.1016/j.bbabio.2004.02.008, PII S0005272804000441
    • Brasseur G, Levican G, Bonnefoy V, Holmes DS, Jedlicki E, Lemesle-Meunier D (2004) Apparent redundancy of electron transfer pathways via bc1 complexes and terminal oxidases in the extremophilic chemolithoautotrophic Acidithiobacillus ferrooxidans. Biochim Biophys Acta 1656:114-126 (Pubitemid 38721273)
    • (2004) Biochimica et Biophysica Acta - Bioenergetics , vol.1656 , Issue.2-3 , pp. 114-126
    • Brasseur, G.1    Levican, G.2    Bonnefoy, V.3    Holmes, D.4    Jedlicki, E.5    Lemesle-Meunier, D.6
  • 11
    • 0017013182 scopus 로고
    • Ferric iron reduction by sulfur-and iron- oxidizing bacteria
    • Brock TD, Gustafson J (1976) Ferric iron reduction by sulfur-and iron- oxidizing bacteria. Appl Environ Microbiol 32:567-571
    • (1976) Appl Environ Microbiol , vol.32 , pp. 567-571
    • Brock, T.D.1    Gustafson, J.2
  • 12
    • 33846326537 scopus 로고    scopus 로고
    • 1 complexes in the strict acidophilic chemolithoautotrophic bacterium Acidithiobacillus ferrooxidans suggests a model for their respective roles in iron or sulfur oxidation
    • DOI 10.1099/mic.0.2006/000067-0
    • Bruscella P, Appia-Ayme C, Levican G, Ratouchniak J, Jedlicki E, Holmes DS, Bonnefoy V (2007) Differential expression of two bc1 complexes in the strict acidophilic chemolithoautotrophic bacterium Acidithiobacillus ferrooxidans suggests a model for their respective roles in iron or sulfur oxidation. Microbiol 153:102-110 (Pubitemid 46111825)
    • (2007) Microbiology , vol.153 , Issue.1 , pp. 102-110
    • Bruscella, P.1    Appia-Ayme, C.2    Levican, G.3    Ratouchniak, J.4    Jedlicki, E.5    Holmes, D.S.6    Bonnefoy, V.7
  • 13
    • 0038219647 scopus 로고    scopus 로고
    • Ferritins, iron uptake and storage from the bacterioferritin viewpoint
    • DOI 10.1093/emboj/cdg215
    • Carrondo MA (2003) Ferritins iron uptake and storage from the bacterioferritin viewpoint. EMBO J 22:1959-1968 (Pubitemid 36565522)
    • (2003) EMBO Journal , vol.22 , Issue.9 , pp. 1959-1968
    • Carrondo, M.A.1
  • 14
    • 17944394995 scopus 로고    scopus 로고
    • Kinetic quantitation of sulfur-oxidizing bacteria adsorbed on sulfur
    • DOI 10.1023/A:1005639804334
    • Ceskova P, Mandl M, Hubackova J (2000) Kinetic quantitation of sulfur-oxidizing bacteria adsorbed on sulfur. Biotechnol Lett 22:699-701 (Pubitemid 30265895)
    • (2000) Biotechnology Letters , vol.22 , Issue.8 , pp. 699-701
    • Ceskova, P.1    Mandl, M.2    Hubackova, J.3
  • 17
    • 0026808529 scopus 로고
    • Anaerobic growth on elemental sulfur using dissimilar iron reduction by autotrophic Thiobacillus ferrooxidans
    • Das A, Mishra AK, Roy P (1992) Anaerobic growth on elemental sulfur using dissimilar iron reduction by autotrophic Thiobacillus ferrooxidans. FEMS Microbiol Lett 97:167-172
    • (1992) FEMS Microbiol Lett , vol.97 , pp. 167-172
    • Das, A.1    Mishra, A.K.2    Roy, P.3
  • 18
    • 0034123440 scopus 로고    scopus 로고
    • 1 and NADH-Q oxidoreductase complexes of the acidophilic obligate chemolithotrophic ferrous ion-oxidizing bacterium Thiobacillus ferrooxidans
    • DOI 10.1128/JB.182.12.3602-3606.2000
    • Elbehti A, Brasseur G, Lemesle-Meunier D (2000) First evidence for existence of an uphill electron transfer through the bc1 and NADH-Q oxidoreductase complexes of the acidophilic obligate chemolithotrophic ferrous ion-oxidizing bacterium Thiobacillus ferrooxidans. J Bacteriol 182:3602-3606 (Pubitemid 30341628)
    • (2000) Journal of Bacteriology , vol.182 , Issue.12 , pp. 3602-3606
    • Elbehti, A.1    Brasseur, G.2    Lemesle-Meunier, D.3
  • 19
    • 0031866420 scopus 로고    scopus 로고
    • Importance of extracellular polymeric substances from Thiobacillus ferrooxidans for bioleaching
    • Gehrke T, Telegdi J, Thierry D, Sand W (1998) Importance of extracellular polymeric substances from Thiobacillus ferrooxidans for bioleaching. Appl Environ Microbiol 64:2743-2747 (Pubitemid 28303332)
    • (1998) Applied and Environmental Microbiology , vol.64 , Issue.7 , pp. 2743-2747
    • Gehrke, T.1    Telegdi, J.2    Thierry, D.3    Sand, W.4
  • 20
    • 28244436432 scopus 로고    scopus 로고
    • Molecular architecture and function of the Omp85 family of proteins
    • DOI 10.1111/j.1365-2958.2005.04906.x
    • Gentle IE, Burri L, Lithgow T (2005) Molecular architecture and function of the Omp85 family of proteins. Mol Microbiol 58:1216-1225 (Pubitemid 41705404)
    • (2005) Molecular Microbiology , vol.58 , Issue.5 , pp. 1216-1225
    • Gentle, I.E.1    Burri, L.2    Lithgow, T.3
  • 21
    • 72449137084 scopus 로고    scopus 로고
    • Acidithiobacillus ferrivorans, sp. nov.; facultatively anaerobic, psychrotolerant iron-, and sulfur-oxidizing acidophiles isolated from metal mine-impacted environments
    • Hallberg KB, Gonzalez-Toril E, Johnson DB (2010) Acidithiobacillus ferrivorans, sp. nov.; facultatively anaerobic, psychrotolerant iron-, and sulfur-oxidizing acidophiles isolated from metal mine-impacted environments. Extremophiles 14:9-19
    • (2010) Extremophiles , vol.14 , pp. 9-19
    • Hallberg, K.B.1    Gonzalez-Toril, E.2    Johnson, D.B.3
  • 23
    • 26844559000 scopus 로고    scopus 로고
    • Exponentially modified protein abundance index (emPAI) for estimation of absolute protein amount in proteomics by the number of sequenced peptides per protein
    • DOI 10.1074/mcp.M500061-MCP200
    • Ishihama Y, Oda Y, Tabata T, Sato T, Nagasu T, Rappsilber J, MannM(2005) Exponentially modified protein abundance index (emPAI) for estimation of absolute protein amount in proteomics by the number of sequenced peptides per protein. Mol Cell Proteomics 4:1265-1272 (Pubitemid 41448714)
    • (2005) Molecular and Cellular Proteomics , vol.4 , Issue.9 , pp. 1265-1272
    • Ishihama, Y.1    Oda, Y.2    Tabata, T.3    Sato, T.4    Nagasu, T.5    Rappsilber, J.6    Mann, M.7
  • 24
    • 0032513717 scopus 로고    scopus 로고
    • Metabolic activity of Thiobacillus ferrooxidans on reduced sulfur compounds detected by capillary isotachophoresis
    • Janiczek O, Mandl M, Ceskova P (1998) Metabolic activity of Thiobacillus ferrooxidans on reduced sulfur compounds detected by capillary isotachophoresis. J Biotechnol 61:225-229
    • (1998) J Biotechnol , vol.61 , pp. 225-229
    • Janiczek, O.1    Mandl, M.2    Ceskova, P.3
  • 25
    • 0026475171 scopus 로고
    • Phosphate starvation affects the synthesis of outer membrane proteins in Thiobacillus ferrooxidans
    • Jerez CA, Seeger M, Amaro AM (1992) Phosphate starvation affects the synthesis of outer membrane proteins in Thiobacillus ferrooxidans. FEMS Microbiol Lett 98:29-34
    • (1992) FEMS Microbiol Lett , vol.98 , pp. 29-34
    • Jerez, C.A.1    Seeger, M.2    Amaro, A.M.3
  • 26
    • 79957999502 scopus 로고    scopus 로고
    • The biogeochemistry of biomining
    • Barton L, Mandl M, Loy A (eds) Springer, Dordrecht
    • Johnson DB (2010) The biogeochemistry of biomining. In: Barton L, Mandl M, Loy A (eds) Geomicrobiology: molecular and environmental perspective. Springer, Dordrecht, pp 401-426
    • (2010) Geomicrobiology: Molecular and Environmental Perspective , pp. 401-426
    • Johnson, D.B.1
  • 27
    • 0035937396 scopus 로고    scopus 로고
    • Control of cell shape in bacteria: Helical, actin-like filaments in Bacillus subtilis
    • DOI 10.1016/S0092-8674(01)00287-2
    • Jones LJ, Carballido-Lopez R, Errington J (2001) Control of cell shape in bacteria: helical, actin-like filaments in Bacillus subtilis. Cell 104:913-922 (Pubitemid 32289283)
    • (2001) Cell , vol.104 , Issue.6 , pp. 913-922
    • Jones, L.J.F.1    Carballido-Lopez, R.2    Errington, J.3
  • 28
    • 0037072870 scopus 로고    scopus 로고
    • Oxygen-independent coproporphyrinogen-III oxidase HemN from Escherichia coli
    • Layer G, Verfurth K, Mahlitz E, Jahn D (2002) Oxygen-independent coproporphyrinogen-III oxidase HemN from Escherichia coli. J Biol Chem 277:34136-34142
    • (2002) J Biol Chem , vol.277 , pp. 34136-34142
    • Layer, G.1    Verfurth, K.2    Mahlitz, E.3    Jahn, D.4
  • 29
    • 72449165371 scopus 로고    scopus 로고
    • Regulation of expression of the petI operon involved in iron oxidation in the biomining bacterium Acidithiobacillus ferrooxidans
    • Lefimil C, Osorio H, Quatrini R, Holmes DS, Jedlicki E (2009) Regulation of expression of the petI operon involved in iron oxidation in the biomining bacterium Acidithiobacillus ferrooxidans. Adv Mater Res 71-73:199-202
    • (2009) Adv Mater Res , vol.71-73 , pp. 199-202
    • Lefimil, C.1    Osorio, H.2    Quatrini, R.3    Holmes, D.S.4    Jedlicki, E.5
  • 31
    • 0010506835 scopus 로고
    • An ultraviolet method for the determination of oxidation of iron sulphide minerals by bacteria
    • Mandl M, Novakova O (1993) An ultraviolet method for the determination of oxidation of iron sulphide minerals by bacteria. Biotechnol Tech 7:573-574
    • (1993) Biotechnol Tech , vol.7 , pp. 573-574
    • Mandl, M.1    Novakova, O.2
  • 32
    • 0033957659 scopus 로고    scopus 로고
    • A region of the Agrobacterium tumefaciens chromosome containing genes required for virulence and attachment to host cells
    • DOI 10.1016/S0167-4781(99)00250-X, PII S016747819900250X
    • Matthysse AG, Yarnall H, Boles SB, McMahan S (2000) A region of the Agrobacterium tumefaciens chromosome containing genes required for virulence and attachment to host cells. Biochim Biophys Acta 1490:208-212 (Pubitemid 30070155)
    • (2000) Biochimica et Biophysica Acta - Gene Structure and Expression , vol.1490 , Issue.1-2 , pp. 208-212
    • Matthysse, A.G.1    Yarnall, H.2    Boles, S.B.3    McMahan, S.4
  • 35
    • 0036202033 scopus 로고    scopus 로고
    • 2in the chemolithoautotrophic bacterium Acidithiobacillus ferrooxidans
    • 2 in the chemolithoautotrophic bacterium Acidithiobacillus ferrooxidans. J Bacteriol 184:2081-2087
    • (2002) J Bacteriol , vol.184 , pp. 2081-2087
    • Ohmura, N.1    Sasaki, K.2    Matsumoto, N.3    Saiki, H.4
  • 36
    • 58249106634 scopus 로고    scopus 로고
    • Microbial iron management mechanisms in extremely acidic environments: Comparative genomics evidence for diversity and versatility
    • Osorio H, Martinez V, Nieto PA, Holmes DS, Quatrini R (2008) Microbial iron management mechanisms in extremely acidic environments: comparative genomics evidence for diversity and versatility. BMC Microbiol 8:203
    • (2008) BMC Microbiol , vol.8 , pp. 203
    • Osorio, H.1    Martinez, V.2    Nieto, P.A.3    Holmes, D.S.4    Quatrini, R.5
  • 37
    • 72449169512 scopus 로고    scopus 로고
    • Prediction of FNR regulated genes and metabolic pathways potentially involved in anaerobic growth of Acidithiobacillus ferrooxidans
    • Osorio H, Cardenas JP, Valdes J, Holmes DS (2009) Prediction of FNR regulated genes and metabolic pathways potentially involved in anaerobic growth of Acidithiobacillus ferrooxidans. Adv Mater Res 71-73:195-198
    • (2009) Adv Mater Res , vol.71-73 , pp. 195-198
    • Osorio, H.1    Cardenas, J.P.2    Valdes, J.3    Holmes, D.S.4
  • 40
    • 0025899288 scopus 로고
    • Energy transduction by anaerobic ferric iron respiration in Thiobacillus ferrooxidans
    • Pronk JT, Liem K, Bos P, Kuenen JG (1991) Energy transduction by anaerobic ferric iron respiration in Thiobacillus ferrooxidans. Appl Environ Microbiol 57:2063-2068
    • (1991) Appl Environ Microbiol , vol.57 , pp. 2063-2068
    • Pronk, J.T.1    Liem, K.2    Bos, P.3    Kuenen, J.G.4
  • 42
    • 34249844266 scopus 로고    scopus 로고
    • Bioinformatic prediction and experimental verification of Fur-regulated genes in the extreme acidophile Acidithiobacillus ferrooxidans
    • DOI 10.1093/nar/gkm068
    • Quatrini R, Lefimil C, Veloso FA, Pedroso I, Holmes DS, Jedlicki E (2007) Bioinformatic prediction and experimental verification of Fur-regulated genes in the extreme acidophile Acidithiobacillus ferrooxidans. Nucleic Acids Res 35:2153-2166 (Pubitemid 47078744)
    • (2007) Nucleic Acids Research , vol.35 , Issue.7 , pp. 2153-2166
    • Quatrini, R.1    Lefimil, C.2    Veloso, F.A.3    Pedroso, I.4    Holmes, D.S.5    Jedlicki, E.6
  • 43
    • 70350445731 scopus 로고    scopus 로고
    • Extending the models for iron and sulfur oxidation in the extreme acidophile Acidithiobacillus ferrooxidans
    • Quatrini R, Appia-Ayme C, Denis Y, Jedlicki E, Holmes DS, Bonnefoy V (2009) Extending the models for iron and sulfur oxidation in the extreme acidophile Acidithiobacillus ferrooxidans. BMC Genomics 10:394
    • (2009) BMC Genomics , vol.10 , pp. 394
    • Quatrini, R.1    Appia-Ayme, C.2    Denis, Y.3    Jedlicki, E.4    Holmes, D.S.5    Bonnefoy, V.6
  • 44
    • 4143137531 scopus 로고    scopus 로고
    • Differential protein expression during growth of Acidithiobacillus ferooxidans on ferrous iron, sulfur compounds, or metal sulfides
    • DOI 10.1128/AEM.70.8.4491-4498.2004
    • Ramirez P, Guiliani N, Valenzuela L, Beard S, Jerez CA (2004) Differential protein expression during growth of Acidithiobacillus ferrooxidans on ferrous iron, sulfur compounds, or metal sulfides. Appl Environ Microbiol 70:4491-4498 (Pubitemid 39095467)
    • (2004) Applied and Environmental Microbiology , vol.70 , Issue.8 , pp. 4491-4498
    • Ramirez, P.1    Guiliani, N.2    Valenzuela, L.3    Beard, S.4    Jerez, C.A.5
  • 45
    • 2942672652 scopus 로고    scopus 로고
    • Microbially assisted dissolution of minerals and its use in the mining industry
    • Rawlings DE (2004) Microbially assisted dissolution of minerals and its use in the mining industry. Pure Appl Chem 76:847-859
    • (2004) Pure Appl Chem , vol.76 , pp. 847-859
    • Rawlings, D.E.1
  • 47
    • 23644462281 scopus 로고
    • Studies on the chemoautotrophic iron bacterium Ferrobacillus ferrooxidans
    • Silverman MP, Lungred DG (1959) Studies on the chemoautotrophic iron bacterium Ferrobacillus ferrooxidans. J Bacteriol 77:642-647
    • (1959) J Bacteriol , vol.77 , pp. 642-647
    • Silverman, M.P.1    Lungred, D.G.2
  • 48
    • 0021837699 scopus 로고
    • Role of a ferric ion-reducing system in sulfur oxidation of Thiobacillus ferrooxidans
    • Sugio T, Domatsu C, Munakato O, Tano T, Imai K (1985) Role of a ferric ion-reducing system in sulfur oxidation of Thiobacillus-ferrooxidans. Appl Environ Microbiol 49:1401-1406 (Pubitemid 15021137)
    • (1985) Applied and Environmental Microbiology , vol.49 , Issue.6 , pp. 1401-1406
    • Sugio, T.1    Domatsu, C.2    Munakata, O.3
  • 49
    • 0023449864 scopus 로고
    • Purification and some properties of sulfur:ferric ion oxidoreductase from Thiobacillus ferrooxidans
    • Sugio T, Mizunashi W, Inagaki K, Tano T (1987) Purification and some properties of sulfur:ferric ion oxidoreductase from Thiobacillus ferrooxidans. J Bacteriol 169:4916-4922
    • (1987) J Bacteriol , vol.169 , pp. 4916-4922
    • Sugio, T.1    Mizunashi, W.2    Inagaki, K.3    Tano, T.4
  • 50
    • 3543029368 scopus 로고
    • Synthesis of an iron-oxidizing system during growth of Thiobacillus ferrooxidans on sulfur-basal salts medium
    • Sugio T, Wada K, Mori M, Inagaki K, Tano T (1988) Synthesis of an iron-oxidizing system during growth of Thiobacillus ferrooxidans on sulfur-basal salts medium. Appl Environ Microbiol 54:150-152
    • (1988) Appl Environ Microbiol , vol.54 , pp. 150-152
    • Sugio, T.1    Wada, K.2    Mori, M.3    Inagaki, K.4    Tano, T.5
  • 51
    • 0026723646 scopus 로고
    • Purification and some properties of sulfite:ferric ion oxidoreductase from Thiobacillus ferrooxidans
    • Sugio T, Hirose T, Zhen YL, Tano T (1992) Purification and some properties of sulfite:ferric ion oxidoreductase from Thiobacillus ferrooxidans. J Bacteriol 174:4189-4192
    • (1992) J Bacteriol , vol.174 , pp. 4189-4192
    • Sugio, T.1    Hirose, T.2    Zhen, Y.L.3    Tano, T.4
  • 52
    • 0025315440 scopus 로고
    • Ferrous iron and sulfur oxidation and ferric iron reduction activities of Thiobacillus ferrooxidans are affected by growth on ferrous iron, sulfur, or a sulfide ore
    • Suzuki I, Takeuchi TL, Yuthasastrakosol TD, Oh JK (1990) Ferrous iron and sulfur oxidation and ferric iron reduction activities of Thiobacillus ferrooxidans are affected by growth on ferrous iron, sulfur, or a sulfide ore. Appl Environ Microbiol 56:1620-1626 (Pubitemid 20202121)
    • (1990) Applied and Environmental Microbiology , vol.56 , Issue.6 , pp. 1620-1626
    • Suzuki, I.1    Takeuchi, T.L.2    Yuthasastrakosol, T.D.3    Oh, J.K.4
  • 53
    • 49549150346 scopus 로고
    • Spectrophotometric determination of iron (II) with 1, 10-phenanthroline in the presence of large amounts of iron(III)
    • Tamura H, Goto K (1974) Spectrophotometric determination of iron (II) with 1, 10-phenanthroline in the presence of large amounts of iron(III). Talanta 21:314-318
    • (1974) Talanta , vol.21 , pp. 314-318
    • Tamura, H.1    Goto, K.2
  • 55
    • 51049109397 scopus 로고    scopus 로고
    • Structure of YraM, a protein essential for growth of Haemophilus influenzae
    • Vijayalakshmi J, Akerley BJ, Saper MA (2008) Structure of YraM, a protein essential for growth of Haemophilus influenzae. Proteins 73:204-217
    • (2008) Proteins , vol.73 , pp. 204-217
    • Vijayalakshmi, J.1    Akerley, B.J.2    Saper, M.A.3
  • 56
    • 36448937490 scopus 로고    scopus 로고
    • Purification and characterization of sulfide:quinone oxidoreductase from an acidophilic iron-oxidizing bacterium, Acidithiobacillus ferrooxidans
    • DOI 10.1271/bbb.70332
    • Wakai S, Tsujita M, Kikumoto M, Manchur MA, Kanao T, Kamimura K (2007) Purification and characterization of sulfide:quinone oxidoreductase from an acidophilic iron-oxidizing bacterium Acidithiobacillus ferrooxidans. Biosci Biotechnol Biochem 71:2735-2742 (Pubitemid 350164254)
    • (2007) Bioscience, Biotechnology and Biochemistry , vol.71 , Issue.11 , pp. 2735-2742
    • Wakai, S.1    Tsujita, M.2    Kikumoto, M.3    Manchur, M.A.4    Kanao, T.5    Kamimura, K.6
  • 57
  • 58
    • 17944400111 scopus 로고    scopus 로고
    • Rusticyanin gene expression of Acidithiobacillus ferrooxidans ATCC 33020 in sulfur- and in ferrous iron media
    • Yarzabal A, Dusquesne K, Bonnefoy V (2003) Rusticyanin gene expression of Acidithiobacillus ferrooxidans ATCC 33020 in sulfur- and in ferrous iron media. Hydrometallurgy 71:107-114
    • (2003) Hydrometallurgy , vol.71 , pp. 107-114
    • Yarzabal, A.1    Dusquesne, K.2    Bonnefoy, V.3
  • 59
    • 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, Bonnefoy V (2004) Regulation of the expression of the Acidithiobacillus ferrooxidans rus operon encoding two cytochromes c, a cytochrome oxidase and rusticyanin. Microbiology 150: 2113-2123 (Pubitemid 39117625)
    • (2004) Microbiology , vol.150 , Issue.7 , pp. 2113-2123
    • Yarzabal, A.1    Appia-Ayme, C.2    Ratouchniak, J.3    Bonnefoy, V.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.