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Volumn 180, Issue 6, 2003, Pages 394-401

Purification and properties of the formate dehydrogenase and characterization of the fdhA gene of Sulfurospirillum multivorans

Author keywords

Dehalorespiration; Dehalospirillum multivorans; fdhA; Formate dehydrogenase; Iron sulfur protein; SECIS; Selenocysteine; Sulfurospirillum multivorans; Tetrachloroethene reductive dehalogenase

Indexed keywords

ARGININE; DINUCLEOTIDE; FORMATE DEHYDROGENASE; FORMIC ACID; GUANIDINE; MOLYBDOPTERIN; PARAQUAT; SELENOCYSTEINE; TETRACHLOROETHYLENE;

EID: 0347625653     PISSN: 03028933     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00203-003-0604-x     Document Type: Article
Times cited : (13)

References (37)
  • 3
    • 0025912548 scopus 로고
    • Cloning and nucleotide sequence of the structural genes encoding the formate dehydrogenase of Wolinella succinogenes
    • Bokranz M, Gutmann, M, Koertner C, Kojro E., Fahrenholz F, Lauterbach F, Kröger A (1991) Cloning and nucleotide sequence of the structural genes encoding the formate dehydrogenase of Wolinella succinogenes. Arch Microbiol 156:119-128
    • (1991) Arch Microbiol , vol.156 , pp. 119-128
    • Bokranz, M.1    Gutmann, M.2    Koertner, C.3    Kojro, E.4    Fahrenholz, F.5    Lauterbach, F.6    Kröger, A.7
  • 6
    • 0037286346 scopus 로고    scopus 로고
    • Molecular and biochemical characterization of two tungsten- and selenium-containing formate dehydrogenases from Eubacterium acidaminophilum that are associated with components of an iron-only hydrogenase
    • Graentzdoerffer A, Rauh D, Pich A, Andreesen JR (2003) Molecular and biochemical characterization of two tungsten-and selenium-containing formate dehydrogenases from Eubacterium acidaminophilum that are associated with components of an iron-only hydrogenase. Arch Microbiol 179:116-130
    • (2003) Arch Microbiol , vol.179 , pp. 116-130
    • Graentzdoerffer, A.1    Rauh, D.2    Pich, A.3    Andreesen, J.R.4
  • 8
    • 0032450045 scopus 로고    scopus 로고
    • Reductive dechlorination in the energy metabolism of anaerobic bacteria
    • Holliger C, Wohlfahrt G, Diekert G (1999) Reductive dechlorination in the energy metabolism of anaerobic bacteria. FEMS Microbiol Rev 22:383-398
    • (1999) FEMS Microbiol Rev , vol.22 , pp. 383-398
    • Holliger, C.1    Wohlfahrt, G.2    Diekert, G.3
  • 9
    • 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 JL, Bastian NR, Rajagopalan, KV (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 77:5172-5176
    • (1990) Proc Natl Acad Sci USA , vol.77 , pp. 5172-5176
    • Johnson, J.L.1    Bastian, N.R.2    Rajagopalan, K.V.3
  • 10
    • 0037040613 scopus 로고    scopus 로고
    • Molecular basis of proton motive force generation: Structure of formate dehydrogenase-N
    • Jormakka M, Tornroth S, Byrne B, Iwata S (2002) Molecular basis of proton motive force generation: structure of formate dehydrogenase-N. Science 295:1863-1868
    • (2002) Science , vol.295 , pp. 1863-1868
    • Jormakka, M.1    Tornroth, S.2    Byrne, B.3    Iwata, S.4
  • 11
    • 0032502268 scopus 로고    scopus 로고
    • Selenium-containing formate dehydrogenase H from Escherichia coli: A molybdopterin enzyme that catalyzes formate oxidation without oxygen transfer
    • Khangulov SV, Gladyshev VN, Dismukes GC, Stadtman TC (1998) Selenium-containing formate dehydrogenase H from Escherichia coli: a molybdopterin enzyme that catalyzes formate oxidation without oxygen transfer. Biochemistry 37:3518-3528
    • (1998) Biochemistry , vol.37 , pp. 3518-3528
    • Khangulov, S.V.1    Gladyshev, V.N.2    Dismukes, G.C.3    Stadtman, T.C.4
  • 12
    • 0018366058 scopus 로고
    • The formate dehydrogenase involved in electron transport from formate to fumarate in Vibrio succinogenes
    • Kröger A, Winkler E, Innerhofer A, Hackenberg H, Schägger H (1979) The formate dehydrogenase involved in electron transport from formate to fumarate in Vibrio succinogenes. Eur J Biochem 94:465-475
    • (1979) Eur J Biochem , vol.94 , pp. 465-475
    • Kröger, A.1    Winkler, E.2    Innerhofer, A.3    Hackenberg, H.4    Schägger, H.5
  • 13
    • 0020475449 scopus 로고
    • A simple method for displaying the hydrophatic character of a protein
    • Kyte J, Doolittle RF (1982) A simple method for displaying the hydrophatic character of a protein. J Mol Biol 157:105-132
    • (1982) J Mol Biol , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 14
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (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
  • 15
    • 0037240872 scopus 로고    scopus 로고
    • The tungsten-containing formate dehydrogenase from Methylobacterium extorquens AM1: Purification and properties
    • Laukel M, Chistoserdova L, Lidstrom ME, Vorholt JA (2003) The tungsten-containing formate dehydrogenase from Methylobacterium extorquens AM1: Purification and properties. Eur J Biochem 270:325-333
    • (2003) Eur J Biochem , vol.270 , pp. 325-333
    • Laukel, M.1    Chistoserdova, L.2    Lidstrom, M.E.3    Vorholt, J.A.4
  • 16
    • 0030967062 scopus 로고    scopus 로고
    • Structure and function of a second gene cluster encoding the formate dehydrogenase of Wolinella succinogenes
    • Lenger R, Herrmann U, Gross R, Simon J, Kröger A (1997) Structure and function of a second gene cluster encoding the formate dehydrogenase of Wolinella succinogenes. Eur J Biochem 246: 646-651
    • (1997) Eur J Biochem , vol.246 , pp. 646-651
    • Lenger, R.1    Herrmann, U.2    Gross, R.3    Simon, J.4    Kröger, A.5
  • 17
    • 0021266787 scopus 로고
    • Formate dehydrogenase of Clostridium pasteurianum
    • Liu C-L, Mortenson LE (1984) Formate dehydrogenase of Clostridium pasteurianum. J Bacteriol 159:375-380
    • (1984) J Bacteriol , vol.159 , pp. 375-380
    • Liu, C.-L.1    Mortenson, L.E.2
  • 18
    • 0032519347 scopus 로고    scopus 로고
    • The nature of the minimal 'selenocysteine insertion sequence' (SECIS) in Escherichia coli
    • Liu Z, Reches M, Groisman, I, Engelberg-Kulka H (1998) The nature of the minimal 'selenocysteine insertion sequence' (SECIS) in Escherichia coli. Nucleic Acids Res 26:896-902
    • (1998) Nucleic Acids Res , vol.26 , pp. 896-902
    • Liu, Z.1    Reches, M.2    Groisman, I.3    Engelberg-Kulka, H.4
  • 19
    • 0037640029 scopus 로고    scopus 로고
    • Description of Sulfurospirillum halorespirans sp. nov., an anaerobic, tetrachloroethene-respiring bacterium, and transfer of Dehalospirillum multivorans to the genus Sulfurospirillum as Sulfurospirillum multivorans comb. nov.
    • Luijten MLGC, de Weert J, Smidt H, Boschker HTS, de Vos WM, Schraa G, Stams AJM (2003) Description of Sulfurospirillum halorespirans sp. nov., an anaerobic, tetrachloroethene-respiring bacterium, and transfer of Dehalospirillum multivorans to the genus Sulfurospirillum as Sulfurospirillum multivorans comb. nov. Int J Syst Bacteriol 53: 787-793
    • (2003) Int J Syst Bacteriol , vol.53 , pp. 787-793
    • Luijten, M.L.G.C.1    De Weert, J.2    Smidt, H.3    Boschker, H.T.S.4    De Vos, W.M.5    Schraa, G.6    Stams, A.J.M.7
  • 20
    • 0032546574 scopus 로고    scopus 로고
    • Molybdenum cofactor properties and [FeS] cluster coordination in Escherichia coli nitrate reductase A: Investigation by site-directed mutagenesis of the conserved His-50 residue in the NarG subunit
    • Magalon A, Asso M, Guigliarelli B, Rothery RA, Bertrand P, Giordano G, Blasco F (1998) Molybdenum cofactor properties and [FeS] cluster coordination in Escherichia coli nitrate reductase A: Investigation by site-directed mutagenesis of the conserved His-50 residue in the NarG subunit. Biochemistry 37:7363-7370
    • (1998) Biochemistry , vol.37 , pp. 7363-7370
    • Magalon, A.1    Asso, M.2    Guigliarelli, B.3    Rothery, R.A.4    Bertrand, P.5    Giordano, G.6    Blasco, F.7
  • 21
    • 0030461965 scopus 로고    scopus 로고
    • Studies on tetrachloroethene respiration in Dehalospirillum multivorans
    • Miller E, Wohlfarth G, Diekert G (1997) Studies on tetrachloroethene respiration in Dehalospirillum multivorans. Arch Microbiol 166:379-387
    • (1997) Arch Microbiol , vol.166 , pp. 379-387
    • Miller, E.1    Wohlfarth, G.2    Diekert, G.3
  • 22
    • 0028073774 scopus 로고
    • Tetrachloroethene metabolism of Dehalospirillum multivorans
    • Neumann A, Scholz-Muramatsu H, Diekert G (1994) Tetrachloroethene metabolism of Dehalospirillum multivorans. Arch Microbiol 162:295-301
    • (1994) Arch Microbiol , vol.162 , pp. 295-301
    • Neumann, A.1    Scholz-Muramatsu, H.2    Diekert, G.3
  • 23
    • 0029895362 scopus 로고    scopus 로고
    • Purification and characterization of tetrachloroethene reductive dehalogenase from Dehalospirillum multivorans
    • Neumann A, Wohlfarth G, Diekert G (1996) Purification and characterization of tetrachloroethene reductive dehalogenase from Dehalospirillum multivorans. J Biol Chem 271:16515-16519
    • (1996) J Biol Chem , vol.271 , pp. 16515-16519
    • Neumann, A.1    Wohlfarth, G.2    Diekert, G.3
  • 24
    • 0031859044 scopus 로고    scopus 로고
    • Tetrachloroethene dehalogenase from Dehalospirillum multivorans: Cloning, sequencing of the encoding genes, and expression of the pceA gene in Escherichia coli
    • Neumann A, Wohlfarth G, Diekert G (1998) Tetrachloroethene dehalogenase from Dehalospirillum multivorans: Cloning, sequencing of the encoding genes, and expression of the pceA gene in Escherichia coli. J Bacteriol 180:4140-4145
    • (1998) J Bacteriol , vol.180 , pp. 4140-4145
    • Neumann, A.1    Wohlfarth, G.2    Diekert, G.3
  • 25
    • 0032500616 scopus 로고    scopus 로고
    • +-linked formate dehydrogenase of Ralstonia eutropha
    • +-linked formate dehydrogenase of Ralstonia eutropha. J Biol Chem 273:26349-60
    • (1998) J Biol Chem , vol.273 , pp. 26349-26360
    • Oh, J.I.1    Bowien, B.2
  • 30
    • 0036311769 scopus 로고    scopus 로고
    • Assembly of membrane-bound respiratory complexes by the Tat protein-transport system
    • Sargent F, Berks BC, Palmer T (2002) Assembly of membrane-bound respiratory complexes by the Tat protein-transport system. Arch Microbiol 178:77-84
    • (2002) Arch Microbiol , vol.178 , pp. 77-84
    • Sargent, F.1    Berks, B.C.2    Palmer, T.3
  • 31
    • 0020046215 scopus 로고
    • Properties of a formate dehydrogenase in Methanobacterium formicicum
    • Schauer NL, Ferry JG (1982) Properties of a formate dehydrogenase in Methanobacterium formicicum. J Bacteriol 50:1-7
    • (1982) J Bacteriol , vol.50 , pp. 1-7
    • Schauer, N.L.1    Ferry, J.G.2
  • 32
    • 0028831324 scopus 로고
    • Isolation and characterization of Dehalospirillum multivorans gen. nov. sp. nov., a tetrachloroethene-utilizing, strictly anaerobic bacterium
    • Scholz-Muramatsu H, Neumann A, Meßmer M, Moore E, Diekert G (1995) Isolation and characterization of Dehalospirillum multivorans gen. nov. sp. nov., a tetrachloroethene-utilizing, strictly anaerobic bacterium. Arch Microbiol 163:48-56
    • (1995) Arch Microbiol , vol.163 , pp. 48-56
    • Scholz-Muramatsu, H.1    Neumann, A.2    Meßmer, M.3    Moore, E.4    Diekert, G.5
  • 33
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence align-ment through sequence weighting, positions-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence align-ment through sequence weighting, positions-specific gap penalties and weight matrix choice. Nucleic Acids Res 22:4673-4680
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 34
    • 0034734296 scopus 로고    scopus 로고
    • A universal system for the transport of redox proteins: Early roots and latest developments
    • Voordouw G (2000) A universal system for the transport of redox proteins: early roots and latest developments. Biophys Chem 86:131-140
    • (2000) Biophys Chem , vol.86 , pp. 131-140
    • Voordouw, G.1
  • 36
    • 0017036833 scopus 로고
    • Titanium (III) citrate as a non-toxic, oxidation-reduction buffering system for the culture of obligate anaerobes
    • Zehnder AJB, Wuhrmann K (1976) Titanium (III) citrate as a non-toxic, oxidation-reduction buffering system for the culture of obligate anaerobes. Science 194:1165-1166
    • (1976) Science , vol.194 , pp. 1165-1166
    • Zehnder, A.J.B.1    Wuhrmann, K.2
  • 37
    • 0006385397 scopus 로고
    • Cotranslational insertion of selenocysteine into formate dehydrogenase from E. coli directed by a UGA codon
    • Zinoni F, Birkmann A, Leinfelder W, Böck A (1987) Cotranslational insertion of selenocysteine into formate dehydrogenase from E. coli directed by a UGA codon. Proc Natl Acad Sci USA 84:3156-3160
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 3156-3160
    • Zinoni, F.1    Birkmann, A.2    Leinfelder, W.3    Böck, A.4


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