메뉴 건너뛰기




Volumn 312, Issue 4, 2003, Pages 1011-1018

Sulfur oxidation in Paracoccus pantotrophus: Interaction of the sulfur-binding protein SoxYZ with the dimanganese SoxB protein

Author keywords

FTIR spectroscopy; Paracoccus pantrotrophus; Protein disulfide; Redox properties; SoxYZ protein; Sulfur oxidation

Indexed keywords

BACTERIAL PROTEIN; DIMER; DISULFIDE; MANGANESE DERIVATIVE; POLYACRYLAMIDE; PROTEIN SOXB; PROTEIN SOXYZ; PROTEIN SUBUNIT; SULFUR; UNCLASSIFIED DRUG;

EID: 0344495378     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2003.11.021     Document Type: Article
Times cited : (42)

References (27)
  • 1
    • 0000274380 scopus 로고
    • Anaerobic oxidation of sulfur compounds as electron donors for bacterial photosynthesis
    • Trüper H.G., Fischer U. Anaerobic oxidation of sulfur compounds as electron donors for bacterial photosynthesis. Phil. Trans. R. Soc. London. 298:1982;529-542.
    • (1982) Phil. Trans. R. Soc. London , vol.298 , pp. 529-542
    • Trüper, H.G.1    Fischer, U.2
  • 2
    • 0024968473 scopus 로고
    • Sulfur oxidation by phototrophic bacteria
    • Brune D.C. Sulfur oxidation by phototrophic bacteria. Biochem. Biophys. Acta. 975:1989;189-221.
    • (1989) Biochem. Biophys. Acta , vol.975 , pp. 189-221
    • Brune, D.C.1
  • 3
    • 0002274902 scopus 로고
    • Biochemical aspects of microbial oxidation of inorganic sulfur compounds
    • S. Oae, & T. Okuyama. Boca Raton: CRC Press
    • Takakuwa S. Biochemical aspects of microbial oxidation of inorganic sulfur compounds. Oae S., Okuyama T. Organic Sulfur Chemistry. Biochemical Aspects. 1992;1-43 CRC Press, Boca Raton.
    • (1992) Organic Sulfur Chemistry. Biochemical Aspects , pp. 1-43
    • Takakuwa, S.1
  • 4
    • 0002391630 scopus 로고
    • Chemoautotrophic and methanotrophic endosymbiotic bacteria at deep-sea vents and seeps
    • D.M. Karl. Boca Raton: CRC Press
    • Nelson D.C., Fisher C.R. Chemoautotrophic and methanotrophic endosymbiotic bacteria at deep-sea vents and seeps. Karl D.M. The Microbiology of Deep-Sea Hydrothermal Vents. 1995;125-167 CRC Press, Boca Raton.
    • (1995) The Microbiology of Deep-Sea Hydrothermal Vents , pp. 125-167
    • Nelson, D.C.1    Fisher, C.R.2
  • 5
    • 0030218222 scopus 로고    scopus 로고
    • Isolation and characterization of Methylo-phaga sulfidovorans, sp. nov.: An obligately methylotrophic, aerobic, dimethyl sulfide oxidizing bacterium from a microbial mat
    • deZwart J.M.M., Nelisse P.N., Kuenen J.G. Isolation and characterization of Methylo-phaga sulfidovorans, sp. nov.: an obligately methylotrophic, aerobic, dimethyl sulfide oxidizing bacterium from a microbial mat. FEMS Microbiol. Ecol. 20:1996;261-270.
    • (1996) FEMS Microbiol. Ecol. , vol.20 , pp. 261-270
    • Dezwart, J.M.M.1    Nelisse, P.N.2    Kuenen, J.G.3
  • 8
    • 0001328962 scopus 로고
    • Thiosphaera pantotropha gen. nov. sp. nov., a facultatively anaerobic, facultative autotrophic sulfur bacterium
    • Robertson L.A., Kuenen J.G. Thiosphaera pantotropha gen. nov. sp. nov., a facultatively anaerobic, facultative autotrophic sulfur bacterium. J. Gen. Microbiol. 129:1983;2847-2855.
    • (1983) J. Gen. Microbiol. , vol.129 , pp. 2847-2855
    • Robertson, L.A.1    Kuenen, J.G.2
  • 9
    • 0032943528 scopus 로고    scopus 로고
    • A re-evaluation of the taxonomy of Paracoccus denitrificans and a proposal for the combination Paracoccus pantotrophus comb. nov. Int
    • Rainey F.A., Kelly D.P., Stackebrandt E., Burghardt J., Hiraishi A., Katayama Y., Wood A.P. A re-evaluation of the taxonomy of Paracoccus denitrificans and a proposal for the combination Paracoccus pantotrophus comb. nov. Int. J. Syst. Bacteriol. 49:1999;645-651.
    • (1999) J. Syst. Bacteriol. , vol.49 , pp. 645-651
    • Rainey, F.A.1    Kelly, D.P.2    Stackebrandt, E.3    Burghardt, J.4    Hiraishi, A.5    Katayama, Y.6    Wood, A.P.7
  • 11
    • 0034932333 scopus 로고    scopus 로고
    • Novel genes of the sox gene cluster, mutagenesis of the flavoprotein SoxF, and evidence for a general sulfur oxidizing system in Paracoccus pantotrophus GB17
    • Rother D., Henrich H.-J., Quentmeier A., Bardischewsky F., Friedrich C.G. Novel genes of the sox gene cluster, mutagenesis of the flavoprotein SoxF, and evidence for a general sulfur oxidizing system in Paracoccus pantotrophus GB17. J. Bacteriol. 183:2001;4499-4508.
    • (2001) J. Bacteriol. , vol.183 , pp. 4499-4508
    • Rother, D.1    Henrich, H.-J.2    Quentmeier, A.3    Bardischewsky, F.4    Friedrich, C.G.5
  • 12
    • 0035902915 scopus 로고    scopus 로고
    • The cysteine residue of the SoxY protein as the active site of protein-bound sulfur oxidation of Paracoccus pantotrophus GB17
    • Quentmeier A., Friedrich C.G. The cysteine residue of the SoxY protein as the active site of protein-bound sulfur oxidation of Paracoccus pantotrophus GB17. FEBS Lett. 503:2001;168-172.
    • (2001) FEBS Lett. , vol.503 , pp. 168-172
    • Quentmeier, A.1    Friedrich, C.G.2
  • 14
    • 0033976381 scopus 로고    scopus 로고
    • Characterization of a new type of sulfite dehydrogenase from Paracoccus pantotrophus GB17
    • Quentmeier A., Kraft R., Kostka S., Klockenkämper R., Friedrich C.G. Characterization of a new type of sulfite dehydrogenase from Paracoccus pantotrophus GB17. Arch. Microbiol. 173:2000;117-125.
    • (2000) Arch. Microbiol. , vol.173 , pp. 117-125
    • Quentmeier, A.1    Kraft, R.2    Kostka, S.3    Klockenkämper, R.4    Friedrich, C.G.5
  • 17
    • 0000694228 scopus 로고
    • Molecular weight estimations of proteins by electrophoresis in polyacrylamide gels of graded porosity
    • Andersson L.O., Borg H., Mikaelsson M. Molecular weight estimations of proteins by electrophoresis in polyacrylamide gels of graded porosity. FEBS Lett. 20:1972;199-202.
    • (1972) FEBS Lett. , vol.20 , pp. 199-202
    • Andersson, L.O.1    Borg, H.2    Mikaelsson, M.3
  • 18
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 19
    • 0015437962 scopus 로고
    • Measurements of the molecular weights by electrophoresis on SDS-polyacrylamide gels
    • Weber K., Pringle J.R., Osborn M. Measurements of the molecular weights by electrophoresis on SDS-polyacrylamide gels. Methods Enzymol. 26:1972;3-27.
    • (1972) Methods Enzymol. , vol.26 , pp. 3-27
    • Weber, K.1    Pringle, J.R.2    Osborn, M.3
  • 20
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA. 76:1979;4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 21
    • 0029885477 scopus 로고    scopus 로고
    • Purification and characterization of the hydrogenase from Thiobacillus ferrooxidans
    • Fischer J., Quentmeier A., Kostka S., Kraft R., Friedrich C.G. Purification and characterization of the hydrogenase from Thiobacillus ferrooxidans. Arch. Microbiol. 165:1996;289-296.
    • (1996) Arch. Microbiol. , vol.165 , pp. 289-296
    • Fischer, J.1    Quentmeier, A.2    Kostka, S.3    Kraft, R.4    Friedrich, C.G.5
  • 22
    • 0343995779 scopus 로고
    • Methods to identify and avoid artificial formation of interchain disulfide bonds when analyzing proteins by SDS-PAGE
    • Kumar M.A., Davidson V.L. Methods to identify and avoid artificial formation of interchain disulfide bonds when analyzing proteins by SDS-PAGE. BioTechniques. 12:1992;198-202.
    • (1992) BioTechniques , vol.12 , pp. 198-202
    • Kumar, M.A.1    Davidson, V.L.2
  • 23
    • 0022463740 scopus 로고
    • Resolution-enhanced Fourier transform infrared spectroscopy of enzymes
    • Susi H., Byler D.M. Resolution-enhanced Fourier transform infrared spectroscopy of enzymes. Methods Enzymol. 130:1986;290-311.
    • (1986) Methods Enzymol. , vol.130 , pp. 290-311
    • Susi, H.1    Byler, D.M.2
  • 24
    • 0025005940 scopus 로고
    • Secondary structure and dosage of soluble and membrane proteins by attenuated total reflection Fourier-transform infrared spectroscopy on hydrated films
    • Goormaghtigh E., Cabiaux V., Ruysschaert J.M. Secondary structure and dosage of soluble and membrane proteins by attenuated total reflection Fourier-transform infrared spectroscopy on hydrated films. Eur. J. Biochem. 193:1990;409-420.
    • (1990) Eur. J. Biochem. , vol.193 , pp. 409-420
    • Goormaghtigh, E.1    Cabiaux, V.2    Ruysschaert, J.M.3
  • 25
    • 0029829590 scopus 로고    scopus 로고
    • A common export pathway for proteins binding complex redox cofactors ?
    • Berks B.C. A common export pathway for proteins binding complex redox cofactors ? Mol. Microbiol. 22:1996;393-404.
    • (1996) Mol. Microbiol. , vol.22 , pp. 393-404
    • Berks, B.C.1
  • 26
    • 0028149485 scopus 로고
    • Identification and sequence analysis of the soxB gene essential for sulfur oxidation of Paracoccus denitrificans GB17
    • Wodara C., Kostka S., Egert M., Kelly D.P., Friedrich C.G. Identification and sequence analysis of the soxB gene essential for sulfur oxidation of Paracoccus denitrificans GB17. J. Bacteriol. 176:1994;6188-6191.
    • (1994) J. Bacteriol. , vol.176 , pp. 6188-6191
    • Wodara, C.1    Kostka, S.2    Egert, M.3    Kelly, D.P.4    Friedrich, C.G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.