메뉴 건너뛰기




Volumn 255, Issue 3, 1998, Pages 755-765

Effect of molybdate and tungstate on the biosynthesis of CO dehydrogenase and the molybdopterin cytosine-dinucleotide-type of molybdenum cofactor in Hydrogenophaga pseudoflava

Author keywords

Biosynthesis; Carbon monoxide; Carbon monoxide dehydrogenase; Molybdenum; Tungsten

Indexed keywords

CARBON MONOXIDE DEHYDROGENASE; MOLYBDENUM; MOLYBDIC ACID; TUNGSTEN DERIVATIVE;

EID: 0032146943     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1998.2550755.x     Document Type: Article
Times cited : (35)

References (60)
  • 1
    • 0030906745 scopus 로고    scopus 로고
    • Molybdenum-cofactor-containing enzymes: Structure and mechanism
    • Kisker, C., Schindelin, H. & Rees, D. C. (1997) Molybdenum-cofactor-containing enzymes: Structure and mechanism, Annu. Rev. Biochem. 66, 233-267.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 233-267
    • Kisker, C.1    Schindelin, H.2    Rees, D.C.3
  • 3
    • 0026485429 scopus 로고
    • A molybdenum and a tungsten isoenzyme of formylmethanofuran dehydrogenase in the thermophilic archaeon Methanobacterium wolfei
    • Schmitz, R. A., Albracht, S. P. J. & Thauer, R. K. (1992) A molybdenum and a tungsten isoenzyme of formylmethanofuran dehydrogenase in the thermophilic archaeon Methanobacterium wolfei, Eur J. Biochem. 209, 1013-1018.
    • (1992) Eur J. Biochem. , vol.209 , pp. 1013-1018
    • Schmitz, R.A.1    Albracht, S.P.J.2    Thauer, R.K.3
  • 4
    • 0028265243 scopus 로고
    • Tungstate can substitute for molybdate in sustaining growth of Methanobacterium thermoautotrophicum. Identification and characterization of a tungsten isoenzyme of formylmethanofuran dehydrogenase
    • Bertram, P. A., Schmitz, R. A., Linder, D. & Thauer, R. K. (1994) Tungstate can substitute for molybdate in sustaining growth of Methanobacterium thermoautotrophicum. Identification and characterization of a tungsten isoenzyme of formylmethanofuran dehydrogenase, Arch. Microbiol. 161, 220-228.
    • (1994) Arch. Microbiol. , vol.161 , pp. 220-228
    • Bertram, P.A.1    Schmitz, R.A.2    Linder, D.3    Thauer, R.K.4
  • 5
    • 0026708343 scopus 로고
    • The role of tungstate and/or molybdate in the formation of aldehyde oxidoreductase in Clostridium thermoaceticum and other acetogens; immunological distances of such enzymes
    • White, H. & Simon, H. (1992) The role of tungstate and/or molybdate in the formation of aldehyde oxidoreductase in Clostridium thermoaceticum and other acetogens; immunological distances of such enzymes, Arch. Microbiol. 158, 81-84.
    • (1992) Arch. Microbiol. , vol.158 , pp. 81-84
    • White, H.1    Simon, H.2
  • 6
    • 0027461140 scopus 로고
    • On a reversible molybdenum-containing aldehyde oxidoreductase from Clostridium formicoaceticum
    • White, H., Huber, C., Feicht, R. & Simon, H. (1993) On a reversible molybdenum-containing aldehyde oxidoreductase from Clostridium formicoaceticum, Arch. Microbiol. 159, 244-249.
    • (1993) Arch. Microbiol. , vol.159 , pp. 244-249
    • White, H.1    Huber, C.2    Feicht, R.3    Simon, H.4
  • 7
    • 0023268434 scopus 로고
    • The molybdenum iron-sulphur protein from Desulfovibrio gigas 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 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
  • 8
    • 0028834243 scopus 로고
    • Purification and characterization of a benzylviologen-linked, tungsten-containing aldehyde oxidoreductase from Desulfovibrio gigas
    • Hensgens, C. M. H., Hagen, W. R. & Hansen, T. A. (1995) Purification and characterization of a benzylviologen-linked, tungsten-containing aldehyde oxidoreductase from Desulfovibrio gigas, J. Bacteriol. 177, 6195-6200.
    • (1995) J. Bacteriol. , vol.177 , pp. 6195-6200
    • Hensgens, C.M.H.1    Hagen, W.R.2    Hansen, T.A.3
  • 9
    • 0015977652 scopus 로고
    • Molecular basis of the biological function of molybdenum. Effect of tungsten on xanthine oxidase and sulfite oxidase in the rat
    • Johnson, J. L., Rajagopalan, K. V. & Cohen, H. J. (1974) Molecular basis of the biological function of molybdenum. Effect of tungsten on xanthine oxidase and sulfite oxidase in the rat, J. Biol. Chem. 249, 859-866.
    • (1974) J. Biol. Chem. , vol.249 , pp. 859-866
    • Johnson, J.L.1    Rajagopalan, K.V.2    Cohen, H.J.3
  • 10
    • 0030064820 scopus 로고    scopus 로고
    • Molybdenum and vanadium do not replace tungsten in the catalytically active forms of the three tungstoenzymes in the hyperthermophilic archaeon Pyrococcus furiosus
    • Mukund, S. & Adams, M. W. W. (1996) Molybdenum and vanadium do not replace tungsten in the catalytically active forms of the three tungstoenzymes in the hyperthermophilic archaeon Pyrococcus furiosus, J. Bacteriol. 178, 163-167.
    • (1996) J. Bacteriol. , vol.178 , pp. 163-167
    • Mukund, S.1    Adams, M.W.W.2
  • 11
    • 0024333565 scopus 로고
    • Hydrogenophaga, a new genus of hydrogen-oxidizing bacteria that includes Hydrogenophaga flava comb.nov. (formerly Pseudomonas flava), Hydrogenophaga palleroni (formerly Pseudomonas palleroni), Hydrogenophaga pseudoflava (formerly Pseudomonas pseudoflava and "Pseudomonas carboxydoflava"), and Hydrogenophaga taeniospiralis (formerly Pseudomonas taeniospiralis)
    • Willems, A., Busse, J., Goor, M., Pot, B., Falsen, E., Jantzen, E., Hoste, B., Gillis, M., Kerstens, K., Auling, G. & De Ley, J. (1989) Hydrogenophaga, a new genus of hydrogen-oxidizing bacteria that includes Hydrogenophaga flava comb.nov. (formerly Pseudomonas flava), Hydrogenophaga palleroni (formerly Pseudomonas palleroni), Hydrogenophaga pseudoflava (formerly Pseudomonas pseudoflava and "Pseudomonas carboxydoflava"), and Hydrogenophaga taeniospiralis (formerly Pseudomonas taeniospiralis), Int. J. Syst. Bacteriol. 39, 319-333.
    • (1989) Int. J. Syst. Bacteriol. , vol.39 , pp. 319-333
    • Willems, A.1    Busse, J.2    Goor, M.3    Pot, B.4    Falsen, E.5    Jantzen, E.6    Hoste, B.7    Gillis, M.8    Kerstens, K.9    Auling, G.10    De Ley, J.11
  • 12
    • 0020653833 scopus 로고
    • Biology of aerobic carbon monoxide-oxidizing bacteria
    • Meyer, O. & Schlegel, H. G. (1983) Biology of aerobic carbon monoxide-oxidizing bacteria, Annu. Rev. Microbiol. 37, 277-310.
    • (1983) Annu. Rev. Microbiol. , vol.37 , pp. 277-310
    • Meyer, O.1    Schlegel, H.G.2
  • 13
    • 0028968003 scopus 로고
    • Molecular characterization of the gene cluster coxMSL 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 coxMSL 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
  • 14
    • 0002913203 scopus 로고    scopus 로고
    • Structure and function of mononuclear molybdenum enzymes
    • Hille, R. (1996) Structure and function of mononuclear molybdenum enzymes, J. Biol. Inorg. Chem. 1, 397-404.
    • (1996) J. Biol. Inorg. Chem. , vol.1 , pp. 397-404
    • Hille, R.1
  • 15
    • 0000260778 scopus 로고
    • Biochemistry and physiology of aerobic carbon monoxide-utilizing bacteria
    • Meyer, O., Jacobitz, S. & Krüger, B. (1986) Biochemistry and physiology of aerobic carbon monoxide-utilizing bacteria, FEMS Microbiol. Rev. 39, 161-179.
    • (1986) FEMS Microbiol. Rev. , vol.39 , pp. 161-179
    • Meyer, O.1    Jacobitz, S.2    Krüger, B.3
  • 16
    • 0002798821 scopus 로고
    • Biochemistry of the aerobic utilization of carbon monoxide
    • (Murrell, J. C. & Kelly, D. P., eds) Intercept Scientific Publication, Andover, UK
    • 1 compounds (Murrell, J. C. & Kelly, D. P., eds) pp. 433-459, Intercept Scientific Publication, Andover, UK.
    • (1993) 1 Compounds , pp. 433-459
    • Meyer, O.1    Frunzke, K.2    Mörsdorf, G.3
  • 17
    • 0025667193 scopus 로고
    • Isolation and characterization of a second molybdopterin dinucleotide: Molybdopterin cytosine dinucleotide
    • Johnson, J. L., Rajagopalan, K. V. & Meyer, O. (1990) Isolation and characterization of a second molybdopterin dinucleotide: Molybdopterin cytosine dinucleotide, Arch. Biochem. Biophys. 283, 542-545.
    • (1990) Arch. Biochem. Biophys. , vol.283 , pp. 542-545
    • Johnson, J.L.1    Rajagopalan, K.V.2    Meyer, O.3
  • 18
    • 0002849792 scopus 로고
    • The bacterial molybdenum cofactor
    • (Stiefel, E. I., Coucouvanis, D. & Newton, W. E., eds) ACS symposium series 535. American Chemical Society, Washington D. C.
    • Meyer, O., Frunzke, K., Tachil, J. & Volk, M. (1993) The bacterial molybdenum cofactor, in Molybdenum enzymes, cofactors, and model systems (Stiefel, E. I., Coucouvanis, D. & Newton, W. E., eds) pp. 50-68, ACS symposium series 535. American Chemical Society, Washington D. C.
    • (1993) Molybdenum Enzymes, Cofactors, and Model Systems , pp. 50-68
    • Meyer, O.1    Frunzke, K.2    Tachil, J.3    Volk, M.4
  • 19
    • 0020079197 scopus 로고
    • Profitable oxidation of carbon monoxide or hydrogen during heterotrophic growth of Pseudomonas carboxydoflaxa
    • Kiessling, M. & Meyer, O. (1982) Profitable oxidation of carbon monoxide or hydrogen during heterotrophic growth of Pseudomonas carboxydoflaxa, FEMS Microbiol. Lett. 13, 333-338.
    • (1982) FEMS Microbiol. Lett. , vol.13 , pp. 333-338
    • Kiessling, M.1    Meyer, O.2
  • 20
    • 0024352761 scopus 로고
    • Homology and distribution of CO dehydrogenase structural genes in carboxydotrophic bacteria
    • Kraut, M., Hugendieck, I., Herwig, S. & Meyer, O. (1989) Homology and distribution of CO dehydrogenase structural genes in carboxydotrophic bacteria, Arch. Microbiol. 152, 335-341.
    • (1989) Arch. Microbiol. , vol.152 , pp. 335-341
    • Kraut, M.1    Hugendieck, I.2    Herwig, S.3    Meyer, O.4
  • 21
    • 0018343530 scopus 로고
    • Oxidation of carbon monoxide in cell extracts of Pseudomonas carboxydovorans
    • Meyer, O. & Schlegel, H. G. (1979) Oxidation of carbon monoxide in cell extracts of Pseudomonas carboxydovorans, J. Bacteriol. 137, 811-817.
    • (1979) J. Bacteriol. , vol.137 , pp. 811-817
    • Meyer, O.1    Schlegel, H.G.2
  • 22
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 23
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding
    • Bradford, M. M. (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
  • 24
    • 84942490613 scopus 로고
    • Diphosphofructose-Aldolase, Phosphoglycerinaldehyd-Dehydrogenase, MilchsäureDehydrogenase, Glycerophosphat-Dehydrogenase und Pyruvat-Kinase aus Kaninchenmuskel in einem Arbeitsgang
    • Beisenherz, G., Bolze, H. G., Bücher, T., Czok, R., Garbade, K. H., Meyer-Arendt, H. & Pfleiderer, G. (1953) Diphosphofructose-Aldolase, Phosphoglycerinaldehyd-Dehydrogenase, MilchsäureDehydrogenase, Glycerophosphat-Dehydrogenase und Pyruvat-Kinase aus Kaninchenmuskel in einem Arbeitsgang, Z. Naturforsch. 8B, 555-557.
    • (1953) Z. Naturforsch. , vol.8 B , pp. 555-557
    • Beisenherz, G.1    Bolze, H.G.2    Bücher, T.3    Czok, R.4    Garbade, K.H.5    Meyer-Arendt, H.6    Pfleiderer, G.7
  • 25
    • 0023899855 scopus 로고
    • Rapid colorimetric micromethod for the quantitation of complexed iron in biological samples
    • Fish, W. W. (1988) Rapid colorimetric micromethod for the quantitation of complexed iron in biological samples, Methods Enzymol. 158, 357-364.
    • (1988) Methods Enzymol. , vol.158 , pp. 357-364
    • Fish, W.W.1
  • 26
    • 0016167140 scopus 로고
    • Determination of molybdenum and tungsten in biological materials
    • Cardenas, J. & Mortenson, L. E. (1974) Determination of molybdenum and tungsten in biological materials, Anal. Biochem. 60, 372-381.
    • (1974) Anal. Biochem. , vol.60 , pp. 372-381
    • Cardenas, J.1    Mortenson, L.E.2
  • 27
    • 33947457186 scopus 로고
    • Spectrophotometric determination of hydrogen sulfide
    • Fogo, J. K. & Popowsky, M. (1949) Spectrophotometric determination of hydrogen sulfide, Anal. Chem. 21, 732-734.
    • (1949) Anal. Chem. , vol.21 , pp. 732-734
    • Fogo, J.K.1    Popowsky, M.2
  • 28
    • 0025228504 scopus 로고
    • Molybdopterin guanine dinucleotide: A modified form of molybdopterin identified in the molybdenum cofactor of dimethyl sulfoxide reductase from Rhodobacter sphaeroides 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 dimethyl sulfoxide reductase from Rhodobacter sphaeroides 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
  • 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
  • 30
    • 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
  • 31
    • 0029682807 scopus 로고    scopus 로고
    • Characterization of xanthine dehydrogenase from the anaerobic bacterium Veillonella atypica and identification of a molybdopterin-cytosine-dinucleotide-containing molybdenum cofactor
    • Gremer, L. & Meyer, O. (1996) Characterization of xanthine dehydrogenase from the anaerobic bacterium Veillonella atypica and identification of a molybdopterin-cytosine-dinucleotide-containing molybdenum cofactor, Eur. J. Biochem. 238, 862-866.
    • (1996) Eur. J. Biochem. , vol.238 , pp. 862-866
    • Gremer, L.1    Meyer, O.2
  • 32
    • 0025835008 scopus 로고
    • Molybdenum cofactor biosynthesis in Escherichia coli. Requirement of the chlB gene product for the formation of molyhdopterin guanine dinucleotide
    • Johnson, J. L., Indermaur, L. W. & Rajagopalan, K. V. (1991) Molybdenum cofactor biosynthesis in Escherichia coli. Requirement of the chlB gene product for the formation of molyhdopterin guanine dinucleotide, J. Biol. Chem. 266, 12 140-12 145.
    • (1991) J. Biol. Chem. , vol.266 , pp. 12140-12145
    • Johnson, J.L.1    Indermaur, L.W.2    Rajagopalan, K.V.3
  • 33
    • 0021333871 scopus 로고
    • The pterin component of the molybdenum cofactor. Structural characterization of two fluorescent derivatives
    • Johnson, J. L., Hainline, B. E., Rajagopalan, K. V. & Arison, B. H. (1984) The pterin component of the molybdenum cofactor. Structural characterization of two fluorescent derivatives, J. Biol. Chem. 259, 5414-5422.
    • (1984) J. Biol. Chem. , vol.259 , pp. 5414-5422
    • Johnson, J.L.1    Hainline, B.E.2    Rajagopalan, K.V.3    Arison, B.H.4
  • 34
    • 0020771781 scopus 로고
    • Studies by e.p.r. spectroscopy of carbon monoxide oxidases from Pseudomonas carboxydovorans and Psendomonas carboxydohydrogena
    • Bray, R. C., George, G. N., Lange, R. & Meyer, O. (1983) Studies by e.p.r. spectroscopy of carbon monoxide oxidases from Pseudomonas carboxydovorans and Psendomonas carboxydohydrogena, Biochem. J. 211, 687-694.
    • (1983) Biochem. J. , vol.211 , pp. 687-694
    • Bray, R.C.1    George, G.N.2    Lange, R.3    Meyer, O.4
  • 35
    • 0029937906 scopus 로고    scopus 로고
    • Characterization of hydrogenase activities associated with the molybdenum CO dehydrogenase from Oligotropha carboxidovorans
    • Santiago, B. & Meyer, O. (1996) Characterization of hydrogenase activities associated with the molybdenum CO dehydrogenase from Oligotropha carboxidovorans, FEMS Microbiol. Lett. 136, 157-162.
    • (1996) FEMS Microbiol. Lett. , vol.136 , pp. 157-162
    • Santiago, B.1    Meyer, O.2
  • 36
    • 0014690512 scopus 로고
    • Electron paramagnetic resonance and circular dichroism studies on milk xanthine oxidase
    • Palmer, G. & Massey, V. (1969) Electron paramagnetic resonance and circular dichroism studies on milk xanthine oxidase, J. Biol. Chem. 244, 2614-2620.
    • (1969) J. Biol. Chem. , vol.244 , pp. 2614-2620
    • Palmer, G.1    Massey, V.2
  • 38
    • 0026086008 scopus 로고
    • Spectroscopic studies of the molybdenum-containing dimethyl sulfoxide reductase from Rhodobacter sphaeroides f. sp. denitrificans
    • Bastian, N. R., Kay, C. J., Barber, M. J. & Rajagopalan, K. V. (1991) Spectroscopic studies of the molybdenum-containing dimethyl sulfoxide reductase from Rhodobacter sphaeroides f. sp. denitrificans, J. Biol. Chem. 266, 45-51.
    • (1991) J. Biol. Chem. , vol.266 , pp. 45-51
    • Bastian, N.R.1    Kay, C.J.2    Barber, M.J.3    Rajagopalan, K.V.4
  • 39
    • 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
  • 40
    • 0017359130 scopus 로고
    • Tryptic cleavage of rat liver sulfite oxidase
    • Johnson, J. L. & Rajagopalan, K. V. (1977) Tryptic cleavage of rat liver sulfite oxidase, J. Biol. Chem. 252, 2017-2025.
    • (1977) J. Biol. Chem. , vol.252 , pp. 2017-2025
    • Johnson, J.L.1    Rajagopalan, K.V.2
  • 41
    • 0029165040 scopus 로고
    • The molybdenum centers of xanthine oxidase and xanthine dehydrogenase
    • Ryan, M. G., Ratnam, K. & Hille, R. (1995) The molybdenum centers of xanthine oxidase and xanthine dehydrogenase, J. Biol. Chem. 270, 19 209-19 212.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19209-19212
    • Ryan, M.G.1    Ratnam, K.2    Hille, R.3
  • 42
    • 0016797607 scopus 로고
    • Transport of molybdate by Clostridium pasteurianum
    • Elliott, B. B. & Mortenson, L. E. (1975) Transport of molybdate by Clostridium pasteurianum, J. Bacteriol. 124, 1295-1301.
    • (1975) J. Bacteriol. , vol.124 , pp. 1295-1301
    • Elliott, B.B.1    Mortenson, L.E.2
  • 43
    • 0023176563 scopus 로고
    • Molybdenum-sensitive transcriptional regulation of the chlD locus of Escherichia coli
    • Miller, J. B., Scott, D. J. & Amy, N. K. (1987) Molybdenum-sensitive transcriptional regulation of the chlD locus of Escherichia coli, J. Bacteriol. 169, 1853-1860.
    • (1987) J. Bacteriol. , vol.169 , pp. 1853-1860
    • Miller, J.B.1    Scott, D.J.2    Amy, N.K.3
  • 44
    • 0024059922 scopus 로고
    • Effect of molybdenum and tungsten on synthesis and composition of formate dehydrogenase in Methanobacterium formicicum
    • May, H. D., Patel, P. S. & Ferry, J. G. (1988) Effect of molybdenum and tungsten on synthesis and composition of formate dehydrogenase in Methanobacterium formicicum, J. Bacteriol. 170, 3384-3389.
    • (1988) J. Bacteriol. , vol.170 , pp. 3384-3389
    • May, H.D.1    Patel, P.S.2    Ferry, J.G.3
  • 45
    • 0027054110 scopus 로고
    • Molybdenum incorporation in denitrifying Azospirillum brasilense Sp.7
    • Chauret, C., Barraquio, W. L. & Knowles, R. (1992) Molybdenum incorporation in denitrifying Azospirillum brasilense Sp.7, Can. J. Microbiol. 38, 1042-1047.
    • (1992) Can. J. Microbiol. , vol.38 , pp. 1042-1047
    • Chauret, C.1    Barraquio, W.L.2    Knowles, R.3
  • 46
    • 0029824740 scopus 로고    scopus 로고
    • The modE gene product mediates molybdenum-dependent expression of genes for the high affinity molybdate transporter and modG in Azotobacter vinelandii
    • Mouncey, N. J., Mitchenall, L. A. & Pau, R. N. (1996) The modE gene product mediates molybdenum-dependent expression of genes for the high affinity molybdate transporter and modG in Azotobacter vinelandii, Microbiol. 142, 1997-2004.
    • (1996) Microbiol. , vol.142 , pp. 1997-2004
    • Mouncey, N.J.1    Mitchenall, L.A.2    Pau, R.N.3
  • 47
    • 0030023719 scopus 로고    scopus 로고
    • Properties of the periplasmic ModA molybdate-binding protein of Escherichia coli
    • Rech, S., Wolin, C. & Gunsalus, R. P. (1996) Properties of the periplasmic ModA molybdate-binding protein of Escherichia coli, J. Biol. Chem. 271, 2557-2562.
    • (1996) J. Biol. Chem. , vol.271 , pp. 2557-2562
    • Rech, S.1    Wolin, C.2    Gunsalus, R.P.3
  • 48
    • 0030726129 scopus 로고    scopus 로고
    • Molybdate transport and regulation in bacteria
    • Grunden, A. M. & Shanmugam, K. T. (1997) Molybdate transport and regulation in bacteria, Arch. Microbiol. 168, 345-354.
    • (1997) Arch. Microbiol. , vol.168 , pp. 345-354
    • Grunden, A.M.1    Shanmugam, K.T.2
  • 49
    • 0018958021 scopus 로고
    • Molybdenum-limited growth achieved either phenotypically or genotypically and its effect on the synthesis of formate dehydrogenase and nitrate reductase by Escherichia coli K12
    • Giordano, G., Haddock, B. A. & Boxer, D. H. (1980) Molybdenum-limited growth achieved either phenotypically or genotypically and its effect on the synthesis of formate dehydrogenase and nitrate reductase by Escherichia coli K12, FEMS Microbiol. Lett. 8, 229-235.
    • (1980) FEMS Microbiol. Lett. , vol.8 , pp. 229-235
    • Giordano, G.1    Haddock, B.A.2    Boxer, D.H.3
  • 50
    • 0020380051 scopus 로고
    • Regulation of nitrogenase in the photosynthetic bacterium Rhodopseudomonas capsulata as studied by two-dimensional gel electrophoresis
    • Hallenbeck, P. C., Meyer, C. M. & Vignais, P. M. (1982) Regulation of nitrogenase in the photosynthetic bacterium Rhodopseudomonas capsulata as studied by two-dimensional gel electrophoresis, J. Bacteriol. 151, 1612-1616.
    • (1982) J. Bacteriol. , vol.151 , pp. 1612-1616
    • Hallenbeck, P.C.1    Meyer, C.M.2    Vignais, P.M.3
  • 51
    • 0000549163 scopus 로고
    • Tungstate, a molybdate analog inactivating nitrate reductase, deregulates the expression of the nitrate reductase structural gene
    • Deng, M., Moureaux, T. & Caboche, M. (1989) Tungstate, a molybdate analog inactivating nitrate reductase, deregulates the expression of the nitrate reductase structural gene, Plant Physiol. 91, 304-309.
    • (1989) Plant Physiol. , vol.91 , pp. 304-309
    • Deng, M.1    Moureaux, T.2    Caboche, M.3
  • 52
    • 0023118615 scopus 로고
    • Studies on nitrate reductase of Clostridium perfringens. IV. Identification of metals, molybdenum cofactor, and iron-sulfur cluster
    • Seki, S., Hattori, Y., Hasegawa, T., Haraguchi, H. & Ishimoto, M. (1987) Studies on nitrate reductase of Clostridium perfringens. IV. Identification of metals, molybdenum cofactor, and iron-sulfur cluster, J. Biochem. 101, 503-509.
    • (1987) J. Biochem. , vol.101 , pp. 503-509
    • Seki, S.1    Hattori, Y.2    Hasegawa, T.3    Haraguchi, H.4    Ishimoto, M.5
  • 53
    • 0028936979 scopus 로고
    • Association of molybdopterin guanine dinucleotide with Escherichia coli dimethyl sulfoxide reductase: Effect of tungstate and a mob mutation
    • Rothery, R. A., Simala Grant, J. L., Johnson, J. L., Rajagopalan, K. V. & Weiner, J. H. (1995) Association of molybdopterin guanine dinucleotide with Escherichia coli dimethyl sulfoxide reductase: Effect of tungstate and a mob mutation, J. Bacteriol. 177, 2057-2063.
    • (1995) J. Bacteriol. , vol.177 , pp. 2057-2063
    • Rothery, R.A.1    Simala Grant, J.L.2    Johnson, J.L.3    Rajagopalan, K.V.4    Weiner, J.H.5
  • 54
    • 0000678343 scopus 로고    scopus 로고
    • Biosynthesis of riboflavin
    • (Neidhardt, F. C., ed.) ASM Press, Washington, D. C.
    • Bacher, A., Eberhardt, S. & Richter, G. (1996) Biosynthesis of riboflavin, in Escherichia coli and Salmonella (Neidhardt, F. C., ed.) pp. 657-664. ASM Press, Washington, D. C.
    • (1996) Escherichia Coli and Salmonella , pp. 657-664
    • Bacher, A.1    Eberhardt, S.2    Richter, G.3
  • 55
    • 0000991019 scopus 로고    scopus 로고
    • Biosynthesis of pantothenic acid and coenzyme A
    • (Neidhardt, F. C., ed) ASM Press, Washington, D. C.
    • Jackowski, S. (1996) Biosynthesis of pantothenic acid and coenzyme A, in Escherichia coli and Salmonella (Neidhardt, F. C., ed) pp. 687-694. ASM Press, Washington, D. C.
    • (1996) Escherichia Coli and Salmonella , pp. 687-694
    • Jackowski, S.1
  • 56
    • 0000397680 scopus 로고    scopus 로고
    • Biosynthesis and recycling of NAD
    • (Neidhardt, F. C., ed.) ASM Press, Washington, D. C.
    • Penfound, T. & Foster, J. W. (1996) Biosynthesis and recycling of NAD, in Escherichia coli and Salmonella (Neidhardt, F. C., ed.) pp. 721-730, ASM Press, Washington, D. C.
    • (1996) Escherichia Coli and Salmonella , pp. 721-730
    • Penfound, T.1    Foster, J.W.2
  • 57
    • 0026743356 scopus 로고
    • Molybdoenzyme biosynthesis in Escherichia coli: In vitro activation of purified nitrate reductase from a chlB mutant
    • Santini, C.-L., Iobbi-Nivol, C., Romane, C., Boxer, D. H. & Giordano, G. (1992) Molybdoenzyme biosynthesis in Escherichia coli: In vitro activation of purified nitrate reductase from a chlB mutant, J. Bacteriol. 174, 7934-7940.
    • (1992) J. Bacteriol. , vol.174 , pp. 7934-7940
    • Santini, C.-L.1    Iobbi-Nivol, C.2    Romane, C.3    Boxer, D.H.4    Giordano, G.5
  • 58
    • 0031005344 scopus 로고    scopus 로고
    • The product of the molybdenum cofactor gene mobB of Escherichia coli is a GTP-binding protein
    • Eaves, D. J., Palmer, T. & Boxer, D. H. (1997) The product of the molybdenum cofactor gene mobB of Escherichia coli is a GTP-binding protein, Eur. J. Biochem. 246, 690-697.
    • (1997) Eur. J. Biochem. , vol.246 , pp. 690-697
    • Eaves, D.J.1    Palmer, T.2    Boxer, D.H.3
  • 60
    • 0031446005 scopus 로고    scopus 로고
    • The molybdenum site in the xanthine oxidase-related aldehyde oxidoreductase from Desulfovibrio gigas and a catalytic mechanism for this class of enzymes
    • Romão, M. J., Rösch, N. & Huber, R. (1997) The molybdenum site in the xanthine oxidase-related aldehyde oxidoreductase from Desulfovibrio gigas and a catalytic mechanism for this class of enzymes, J. Biol. Inorg. Chem. 2, 782-785.
    • (1997) J. Biol. Inorg. Chem. , vol.2 , pp. 782-785
    • Romão, M.J.1    Rösch, N.2    Huber, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.