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Volumn 260, Issue 2, 1999, Pages 540-548

The strict molybdate-dependence of glucose-degradation by the thermoacidophile Sulfolobus acidocaldarius reveals the first crenarchaeotic molybdenum containing enzyme - An aldehyde oxidoreductase

Author keywords

Aldehyde oxidoreductase; Archaea; Glycolysis; Molybdenum; Sulfolobus acidocaldarius

Indexed keywords

ALDEHYDE DEHYDROGENASE; MOLYBDENUM;

EID: 0001511271     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00201.x     Document Type: Article
Times cited : (29)

References (41)
  • 1
    • 0015275944 scopus 로고
    • Sulfolobus, new genus of sulphur-oxidizing bacteria living at low pH and high temperature
    • Brock, T.D., Brock, K.M., Belly, R.T. & Weiss, R.L. (1972) Sulfolobus, new genus of sulphur-oxidizing bacteria living at low pH and high temperature. Arch. Microbiol. 84, 54-68.
    • (1972) Arch. Microbiol. , vol.84 , pp. 54-68
    • Brock, T.D.1    Brock, K.M.2    Belly, R.T.3    Weiss, R.L.4
  • 2
    • 8844250928 scopus 로고
    • (Kates M., Kushner D. J. & Matheson A. T., eds.), Elsevier, Amsterdam
    • Danson, M.J. (1993) In: The Biochemistry of Archaea (Kates M., Kushner D. J. & Matheson A. T., eds.), pp. 1-24. Elsevier, Amsterdam.
    • (1993) The Biochemistry of Archaea , pp. 1-24
    • Danson, M.J.1
  • 3
    • 0022375122 scopus 로고
    • The respiratory system of Sulfolobus acidocaldarius, a thermophilic archaebacterium
    • Anemüller, S., Lübben, M. & Schäfer, G. (1985) The respiratory system of Sulfolobus acidocaldarius, a thermophilic archaebacterium. FEBS Lett. 193, 83-87.
    • (1985) FEBS Lett. , vol.193 , pp. 83-87
    • Anemüller, S.1    Lübben, M.2    Schäfer, G.3
  • 4
    • 0025311484 scopus 로고
    • Electron transport and energy conservation in the archaebacterium Sulfolobus acidocaldarius
    • Schäfer, G., Anemüller, S., Moll, R., Meyer, W. & Lübben, M. (1990) Electron transport and energy conservation in the archaebacterium Sulfolobus acidocaldarius. FEMS Microbiol. Rev. 75, 335-348.
    • (1990) FEMS Microbiol. Rev. , vol.75 , pp. 335-348
    • Schäfer, G.1    Anemüller, S.2    Moll, R.3    Meyer, W.4    Lübben, M.5
  • 5
    • 0040984441 scopus 로고    scopus 로고
    • On the origin of respiration: Electron transport proteins from archaea to man
    • Schäfer, G., Purschke, W. & Schmidt, C.L. (1996) On the origin of respiration: electron transport proteins from archaea to man. FEMS 18, 173-188.
    • (1996) FEMS , vol.18 , pp. 173-188
    • Schäfer, G.1    Purschke, W.2    Schmidt, C.L.3
  • 6
    • 0031002263 scopus 로고    scopus 로고
    • Comparative analysis of Embden-Meyerhof and Entner-Doudoroff glycolytic pathways in hyperthermophilic archaea and the bacterium thermotoga
    • Selig, M., Xavier, K.B., Santos, H. & Schönheit, P. (1997) Comparative analysis of Embden-Meyerhof and Entner-Doudoroff glycolytic pathways in hyperthermophilic archaea and the bacterium Thermotoga. Arch. Microbiol. 167, 217-232.
    • (1997) Arch. Microbiol. , vol.167 , pp. 217-232
    • Selig, M.1    Xavier, K.B.2    Santos, H.3    Schönheit, P.4
  • 7
    • 7744224797 scopus 로고    scopus 로고
    • Structural basis of biological nitrogen fixation
    • Howard, J.B. & Rees, D.C. (1996) Structural basis of biological nitrogen fixation. Chem. Rev. 96, 2965-2982.
    • (1996) Chem. Rev. , vol.96 , pp. 2965-2982
    • Howard, J.B.1    Rees, D.C.2
  • 8
    • 0000703950 scopus 로고    scopus 로고
    • Mechanism of molybdenum nitrogenase
    • Burgess, B.K. & Lowe, D.J. (1996) Mechanism of molybdenum nitrogenase. Chem. Rev. 96, 2983-3011.
    • (1996) Chem. Rev. , vol.96 , pp. 2983-3011
    • Burgess, B.K.1    Lowe, D.J.2
  • 9
    • 0000273676 scopus 로고    scopus 로고
    • The mononuclear molybdenum enzymes
    • Hill, R. (1996) The mononuclear molybdenum enzymes. Chem. Rev. 96, 2757-2816.
    • (1996) Chem. Rev. , vol.96 , pp. 2757-2816
    • Hill, R.1
  • 10
    • 0029867727 scopus 로고    scopus 로고
    • Purification and characterization of a procaryotic xanthine dehydrogenase from comamoneas acidovorans
    • Xiang, Q. & Edmondson, D.E. (1996) Purification and characterization of a procaryotic xanthine dehydrogenase from Comamoneas acidovorans. Biochemistry 35, 5441-5450.
    • (1996) Biochemistry , vol.35 , pp. 5441-5450
    • Xiang, Q.1    Edmondson, D.E.2
  • 11
    • 0029876533 scopus 로고    scopus 로고
    • Site-directed mutagenesis of recombinant sulfite oxidase
    • Garrett, R.M. & Rajagopalan, K.V. (1996) Site-directed mutagenesis of recombinant sulfite oxidase. J. Biol. Chem. 271, 7387-7391.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7387-7391
    • Garrett, R.M.1    Rajagopalan, K.V.2
  • 12
    • 0030036323 scopus 로고    scopus 로고
    • Dimethylsulfide: Acceptor oxidoreductase from Rhodobacter sulfidophilus. The purified enzyme contains b-type haem and a pterin molybdenum cofactor
    • Hanlon, S.P., Toh, T.-H., Solomon, P.S., Holt, R.A. & McEwans, A.G. (1996) Dimethylsulfide: acceptor oxidoreductase from Rhodobacter sulfidophilus. The purified enzyme contains b-type haem and a pterin molybdenum cofactor. Eur. J. Biochem. 239, 391-396.
    • (1996) Eur. J. Biochem. , vol.239 , pp. 391-396
    • Hanlon, S.P.1    Toh, T.-H.2    Solomon, P.S.3    Holt, R.A.4    McEwans, A.G.5
  • 13
    • 0023268434 scopus 로고
    • The molybdenum iron-sulphur protein from Desulfovibrio gigas as a form of aldehyde oxidase
    • Turner, N., Barata, B., Bray, R.C., Deistung, J., Le Gall, J. & Moura, J.J.G. (1987) The molybdenum iron-sulphur protein from Desulfovibrio gigas as a form of aldehyde oxidase. Biochem. J. 243, 755-761.
    • (1987) Biochem. J. , vol.243 , pp. 755-761
    • Turner, N.1    Barata, B.2    Bray, R.C.3    Deistung, J.4    Le Gall, J.5    Moura, J.J.G.6
  • 14
    • 0027217139 scopus 로고
    • Subunit composition, crystallization and preliminary crystallographic studies of the Desulfovibrio gigas aldehyde oxidoreductase containing molybdenum and [2Fe-2S] centers
    • Romao, M.A., Barata, B.A.S., Archer, M., Lobeck, K., Moura, I., Carrondo, M.A., Le Gall, J., Lottspeich, F., Huber, R. & Moura, J.J.G. (1993) Subunit composition, crystallization and preliminary crystallographic studies of the Desulfovibrio gigas aldehyde oxidoreductase containing molybdenum and [2Fe-2S] centers. Eur. J. Biochem. 215, 729-732.
    • (1993) Eur. J. Biochem. , vol.215 , pp. 729-732
    • Romao, M.A.1    Barata, B.A.S.2    Archer, M.3    Lobeck, K.4    Moura, I.5    Carrondo, M.A.6    Le Gall, J.7    Lottspeich, F.8    Huber, R.9    Moura, J.J.G.10
  • 15
    • 0029786383 scopus 로고    scopus 로고
    • Oxidoreductase-type enzymes and redox proteins involved in fermentative metabolism of hyperthermophilic archaea
    • Adams, M.W.W. & Kletzin, A. (1996) Oxidoreductase-type enzymes and redox proteins involved in fermentative metabolism of hyperthermophilic archaea. Adv. Prot. Chem. 48, 101-180.
    • (1996) Adv. Prot. Chem. , vol.48 , pp. 101-180
    • Adams, M.W.W.1    Kletzin, A.2
  • 16
    • 0025194727 scopus 로고
    • 3 from Sulfolobus acidocaldarius. A single-subunit, quinol-oxidizing archaebacterial terminal oxidase
    • 3 from Sulfolobus acidocaldarius. A single-subunit, quinol-oxidizing archaebacterial terminal oxidase. Eur. J. Biochem. 191, 267-305.
    • (1990) Eur. J. Biochem. , vol.191 , pp. 267-305
    • Anemüller, S.1    Schäfer, G.2
  • 17
    • 0027454258 scopus 로고
    • Aldehyde oxidoreductase activity in Desulfovibrio gigas: In vitro reconstitution of an electron-transfer chain from aldehydes to the production of molecular hydrogen
    • Barata, B.A.S., Le Gall, J. & Moura, J.J.G. (1993) Aldehyde oxidoreductase activity in Desulfovibrio gigas: in vitro reconstitution of an electron-transfer chain from aldehydes to the production of molecular hydrogen. Biochemistry 32, 11559-11568.
    • (1993) Biochemistry , vol.32 , pp. 11559-11568
    • Barata, B.A.S.1    Le Gall, J.2    Moura, J.J.G.3
  • 18
    • 0028821539 scopus 로고
    • Purification and characterization of the Rieske iron-sulfur protein from the thermoacidophilic crenamhaeon Sulfolobus acidocaldarius
    • Schmidt, C.L., Anemüller, S., Teixeira, M. & Schäfer, G. (1995) Purification and characterization of the Rieske iron-sulfur protein from the thermoacidophilic crenamhaeon Sulfolobus acidocaldarius. FEBS Lett. 359, 239-242.
    • (1995) FEBS Lett. , vol.359 , pp. 239-242
    • Schmidt, C.L.1    Anemüller, S.2    Teixeira, M.3    Schäfer, G.4
  • 19
    • 0029150075 scopus 로고
    • EPR Characterization of an archaeal succinate dehydrogenase in the membrane-bound state
    • Anemüller, S., Hettmann, T., Moll, R., Teixeira, M. & Schäfer, G. (1995) EPR Characterization of an archaeal succinate dehydrogenase in the membrane-bound state. Eur. J. Biochem. 232, 563-568.
    • (1995) Eur. J. Biochem. , vol.232 , pp. 563-568
    • Anemüller, S.1    Hettmann, T.2    Moll, R.3    Teixeira, M.4    Schäfer, G.5
  • 20
    • 0029842905 scopus 로고    scopus 로고
    • Three extremely thermostable proteins from Sulfolobus and a reappraisal of the 'Traffic Rules'
    • Schäfer, T., Bönisch, H., Kardinahl, S., Schmidt, C. & Schäfer, G. (1996) Three extremely thermostable proteins from Sulfolobus and a reappraisal of the 'Traffic Rules'. Biol. Chem. 377, 505-512.
    • (1996) Biol. Chem. , vol.377 , pp. 505-512
    • Schäfer, T.1    Bönisch, H.2    Kardinahl, S.3    Schmidt, C.4    Schäfer, G.5
  • 21
    • 0018065357 scopus 로고
    • Micro methods for the quantitative determination of iron and copper in biological material
    • Beinert, H. (1978) Micro methods for the quantitative determination of iron and copper in biological material. Meth. Enzym. 54, 435-445.
    • (1978) Meth. Enzym. , vol.54 , pp. 435-445
    • Beinert, H.1
  • 22
    • 0343879238 scopus 로고
    • Assay of inorganic phosphate, total phosphate and phosphatases
    • Ames, B.N. (1966) Assay of inorganic phosphate, total phosphate and phosphatases. Meth. Enzym. 8, 115-118.
    • (1966) Meth. Enzym. , vol.8 , pp. 115-118
    • Ames, B.N.1
  • 23
    • 0038323637 scopus 로고
    • The absorption spectra of iron-flavoproteins
    • Rajagopalan, K.V. & Handler, P. (1963) The absorption spectra of iron-flavoproteins. J. Biol. Chem. 239, 1509-1514.
    • (1963) J. Biol. Chem. , vol.239 , pp. 1509-1514
    • Rajagopalan, K.V.1    Handler, P.2
  • 24
    • 0029117622 scopus 로고
    • Molybdate and regulation of mod (molybdate transport), fdhF, and hyc (formate hydrogenase) operons in Escherichia coli
    • Rosentel, J.K., Healy, F., Maupin-Furlow, J.A., Lee, J.H. & Shanmugam, K.T. (1995) Molybdate and regulation of mod (molybdate transport), fdhF, and hyc (formate hydrogenase) operons in Escherichia coli. J. Bacteriol. 177, 4857-4864.
    • (1995) J. Bacteriol. , vol.177 , pp. 4857-4864
    • Rosentel, J.K.1    Healy, F.2    Maupin-Furlow, J.A.3    Lee, J.H.4    Shanmugam, K.T.5
  • 25
    • 0028968003 scopus 로고
    • Molecular characterization of the gene cluster cox MSL encoding the molybdenum-containing carbon monoxide dehydrogenase of Oligotropha carboxidovorans
    • Schübel, U., Kraut, M., Mörsdorf, G. & Meyer, O. (1995) Molecular characterization of the gene cluster cox MSL encoding the molybdenum-containing carbon monoxide dehydrogenase of Oligotropha carboxidovorans. J. Bacteriol. 177, 2197-2203.
    • (1995) J. Bacteriol. , vol.177 , pp. 2197-2203
    • Schübel, U.1    Kraut, M.2    Mörsdorf, G.3    Meyer, O.4
  • 26
    • 0017802882 scopus 로고
    • 2 oxidoreductase from Clostridium pasteurianum, a molybdenum iron-sulfur-protein
    • 2 oxidoreductase from Clostridium pasteurianum, a molybdenum iron-sulfur-protein. Eur. J. Biochem. 85, 125-135.
    • (1977) Eur. J. Biochem. , vol.85 , pp. 125-135
    • Scherer, P.A.1    Thauer, R.K.2
  • 27
    • 0000720562 scopus 로고
    • + cycling across the plasma of the thermoacidophilic archaebacterium Sulfolobus acidocaldarius
    • + cycling across the plasma 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
  • 28
    • 0026036047 scopus 로고
    • Enzymes depending on the pterin molybdenum cofactor: Sequence families, spectroscopic properties of molybdenum and possible cofactor-binding domains
    • Wootton, J.C., Nicolson, R.E., Cock, J.M., Walters, D.E., Burke, J.F., Doyle, W.A. & Bray, R.C. (1990) Enzymes depending on the pterin molybdenum cofactor: sequence families, spectroscopic properties of molybdenum and possible cofactor-binding domains. Biochim. Biophys. Acta 1057, 157-185.
    • (1990) Biochim. Biophys. Acta , vol.1057 , pp. 157-185
    • Wootton, J.C.1    Nicolson, R.E.2    Cock, J.M.3    Walters, D.E.4    Burke, J.F.5    Doyle, W.A.6    Bray, R.C.7
  • 29
    • 0347392877 scopus 로고
    • Structural and metabolic relationship between the molybdenum cofactor and urothione
    • Johnson, J.L. & Rajagopalan, K.V. (1982) Structural and metabolic relationship between the molybdenum cofactor and urothione. Proc. Natl Acad. Sci. USA 79, 6856-6860.
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 6856-6860
    • Johnson, J.L.1    Rajagopalan, K.V.2
  • 31
    • 0020083365 scopus 로고
    • Chemical and spectral properties of carbon monoxide: Methylene blue oxidoreductase
    • Meyer, O. (1982) Chemical and spectral properties of carbon monoxide: methylene blue oxidoreductase. J. Biol. Chem. 257, 1333-1341.
    • (1982) J. Biol. Chem. , vol.257 , pp. 1333-1341
    • Meyer, O.1
  • 32
    • 0020123907 scopus 로고
    • Studies by electron-paramagnetic-resonance spectroscopy of the molybdenum center of aldehyde oxidase
    • Bray, R.C., George, G.N., Gutteridge, S., Norlander, L., Stell, J.G.P. & Stubley, C. (1982) Studies by electron-paramagnetic-resonance spectroscopy of the molybdenum center of aldehyde oxidase. Biochem. J. 203, 263-267.
    • (1982) Biochem. J. , vol.203 , pp. 263-267
    • Bray, R.C.1    George, G.N.2    Gutteridge, S.3    Norlander, L.4    Stell, J.G.P.5    Stubley, C.6
  • 34
    • 0020487554 scopus 로고
    • Properties of the prosthetic groups of rabbit liver aldehyde oxidase: A comparison of molybdenum hydroxylase enzymes
    • Barber, M.J., Coughlan, M.P., Rajagopalan, K.V. & Siegel, L.M. (1982) Properties of the prosthetic groups of rabbit liver aldehyde oxidase: a comparison of molybdenum hydroxylase enzymes. Biochemistry 21, 3561-3568.
    • (1982) Biochemistry , vol.21 , pp. 3561-3568
    • Barber, M.J.1    Coughlan, M.P.2    Rajagopalan, K.V.3    Siegel, L.M.4
  • 35
    • 0017810940 scopus 로고
    • Oxidation-reduction studies of the Mo-(2Fe-2S) protein from Desulfovibrio gigas
    • Moura, J.J.G., Xavier, A.V., Cammack, R., Hall, D.O., Bruschi, M. & Le Gall, J. (1977) Oxidation-reduction studies of the Mo-(2Fe-2S) protein from Desulfovibrio gigas. Biochem. J. 173, 419-425.
    • (1977) Biochem. J. , vol.173 , pp. 419-425
    • Moura, J.J.G.1    Xavier, A.V.2    Cammack, R.3    Hall, D.O.4    Bruschi, M.5    Le Gall, J.6
  • 36
    • 0025228504 scopus 로고
    • Molybdopterin guanine dinucleotide: A modified form of molybdopterin identified in the molybdenum cofactor of dimethylsulfoxide reductase from Rhodobacter spaeroides forma specialis denitrificans
    • Johnson, J.L., Bastian, N.R. & Rajagopalan, K.V. (1990) Molybdopterin guanine dinucleotide: a modified form of molybdopterin identified in the molybdenum cofactor of dimethylsulfoxide reductase from Rhodobacter spaeroides forma specialis denitrificans. Proc. Natl Acad. Sci. USA 87, 3190-3194.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 3190-3194
    • Johnson, J.L.1    Bastian, N.R.2    Rajagopalan, K.V.3
  • 37
    • 0028961901 scopus 로고
    • Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase
    • Chan, M.K., Mukund, S., Kletzin, A., Adams, M.W.W. & Rees, D.C. (1995) Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase. Science 267, 1463-1469.
    • (1995) Science , vol.267 , pp. 1463-1469
    • Chan, M.K.1    Mukund, S.2    Kletzin, A.3    Adams, M.W.W.4    Rees, D.C.5
  • 38
    • 0026321415 scopus 로고
    • The novel tungsten-iron-sulfur protein of the hyperthermophilic archaebacterium, Pyrococcus furiosus, is an aldehyde ferredoxin oxidoreductase
    • Mukund, S. & Adams, M.W.W. (1991) The novel tungsten-iron-sulfur protein of the hyperthermophilic archaebacterium, Pyrococcus furiosus, is an aldehyde ferredoxin oxidoreductase. J. Biol. Chem. 266, 14208-14216.
    • (1991) J. Biol. Chem. , vol.266 , pp. 14208-14216
    • Mukund, S.1    Adams, M.W.W.2
  • 39
    • 0024351039 scopus 로고
    • Phenotopic characterization of the archaebacterial genus Sulfolobus: Comparison of five wild-type strains
    • Grogan, D.W. (1989) Phenotopic characterization of the archaebacterial genus Sulfolobus: comparison of five wild-type strains. J. Bacteriol. 171 (12), 6710-6719.
    • (1989) J. Bacteriol. , vol.171 , Issue.12 , pp. 6710-6719
    • Grogan, D.W.1
  • 40
    • 0015421657 scopus 로고
    • Spin-spin interaction between molybdenum and one of the iron-sulphur systems of xanthine oxidase and its relevance to the enzymic mechanism
    • Lowe, D.J., Lynden-Bell, R.M. & Bray, R.C. (1977) Spin-spin interaction between molybdenum and one of the iron-sulphur systems of xanthine oxidase and its relevance to the enzymic mechanism. Biochem. J. 130, 239-249.
    • (1977) Biochem. J. , vol.130 , pp. 239-249
    • Lowe, D.J.1    Lynden-Bell, R.M.2    Bray, R.C.3
  • 41
    • 0017133697 scopus 로고
    • Oxidation-reduction potentials of molybdenum, flavin and iron-sulphur centres in milk xanthine oxidase
    • Cammack, R., Barber, M.J. & Bray, R.C. (1976) Oxidation-reduction potentials of molybdenum, flavin and iron-sulphur centres in milk xanthine oxidase. Biochem. J. 157, 469-478.
    • (1976) Biochem. J. , vol.157 , pp. 469-478
    • Cammack, R.1    Barber, M.J.2    Bray, R.C.3


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