메뉴 건너뛰기




Volumn 179, Issue 6, 2003, Pages 444-456

The anabolic pyruvate oxidoreductase from Methanococcus maripaludis

Author keywords

Archaea; Methanococcus maripaludis; Methanogen; Pyruvate oxidoreductase

Indexed keywords

2 OXOBUTYRIC ACID; CARBON DIOXIDE; CYSTEINE; CYTOCHROME C; FERREDOXIN; FLAVINE ADENINE NUCLEOTIDE; FLAVINE MONONUCLEOTIDE; ORGANIC CARBON; OXALOACETIC ACID; OXIDOREDUCTASE; OXYGEN; PARAQUAT; POLYPEPTIDE; PYRUVATE SYNTHASE; PYRUVIC ACID; RUBREDOXIN; UNCLASSIFIED DRUG;

EID: 0037861912     PISSN: 03028933     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00203-003-0554-3     Document Type: Article
Times cited : (25)

References (58)
  • 1
    • 0029786383 scopus 로고    scopus 로고
    • Oxidoreductase-type enzymes and redox proteins involved in fermentative metabolisms of hyperthermophilic archaea
    • Adams MWW, Kletzin A (1996) Oxidoreductase-type enzymes and redox proteins involved in fermentative metabolisms of hyperthermophilic archaea. Adv Protein Chem 48:101-180
    • (1996) Adv Protein Chem , vol.48 , pp. 101-180
    • Adams, M.W.W.1    Kletzin, A.2
  • 2
    • 0034680865 scopus 로고    scopus 로고
    • Learning from hydrogenases: Location of a proton pump and of a second FMN in bovine NADH-ubiquinone oxidoreductase (complex I)
    • Albracht SPJ, Hedderich R (2000) Learning from hydrogenases: location of a proton pump and of a second FMN in bovine NADH-ubiquinone oxidoreductase (complex I). FEBS Lett 485:1-6
    • (2000) FEBS Lett , vol.485 , pp. 1-6
    • Albracht, S.P.J.1    Hedderich, R.2
  • 3
    • 0024407488 scopus 로고
    • 420-reducing hydrogenase from Methanobacterium formicicum
    • 420-reducing hydrogenase from Methanobacterium formicicum. J Bacteriol 171:3846-3853
    • (1989) J Bacteriol , vol.171 , pp. 3846-3853
    • Baron, S.F.1    Ferry, J.G.2
  • 4
    • 0027386619 scopus 로고
    • Purification and characterization of pyruvate:Ferredoxin oxidoreductase from the hyperthermophilic archaeon Pyrococcus furiosus
    • Blamey JM, Adams MWW (1993) Purification and characterization of pyruvate:ferredoxin oxidoreductase from the hyperthermophilic archaeon Pyrococcus furiosus. Biochim Biophys Acta 1161:19-27
    • (1993) Biochim Biophys Acta , vol.1161 , pp. 19-27
    • Blamey, J.M.1    Adams, M.W.W.2
  • 5
    • 0028097631 scopus 로고
    • Pyruvate - A novel substrate for growth and methane formation in Methanosarcina barkeri
    • Bock AK, Prieger-Kraft A, Schönheit P (1994) Pyruvate - a novel substrate for growth and methane formation in Methanosarcina barkeri. Arch Microbiol 161:33-46
    • (1994) Arch Microbiol , vol.161 , pp. 33-46
    • Bock, A.K.1    Prieger-Kraft, A.2    Schönheit, P.3
  • 6
    • 0029985246 scopus 로고    scopus 로고
    • Catalytic properties, molecular composition and sequence alignments of pyruvate:Ferredoxin oxidoreductase from the methanogenic archaeon Methanosarcina barkeri (strain Fusaro)
    • Bock AK, Kunow J, Glasemacher J, Schönheit P (1996) Catalytic properties, molecular composition and sequence alignments of pyruvate:ferredoxin oxidoreductase from the methanogenic archaeon Methanosarcina barkeri (strain Fusaro). Eur J Biochem 237:35-44
    • (1996) Eur J Biochem , vol.237 , pp. 35-44
    • Bock, A.K.1    Kunow, J.2    Glasemacher, J.3    Schönheit, P.4
  • 8
    • 0019817227 scopus 로고
    • Electron transport to nitrogenase in Klebsiella pneumonia, purification and properties of the nifJ protein
    • Bogusz D, Houmard J, Aubert J-P (1981) Electron transport to nitrogenase in Klebsiella pneumonia, purification and properties of the nifJ protein. Eur J Biochem 120:421-426
    • (1981) Eur J Biochem , vol.120 , pp. 421-426
    • Bogusz, D.1    Houmard, J.2    Aubert, J.-P.3
  • 9
    • 16044367245 scopus 로고    scopus 로고
    • Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii
    • Bult CJ and 39 others (1996) Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii. Science 273:1058-1073
    • (1996) Science , vol.273 , pp. 1058-1073
    • Bult, C.J.1
  • 12
    • 77956989125 scopus 로고
    • The structure and function of quinones in respiratory metabolism
    • Dunphy PJ, Brodie AF (1971) The structure and function of quinones in respiratory metabolism. Methods Enzymol 18C:407-461
    • (1971) Methods Enzymol , vol.18 C , pp. 407-461
    • Dunphy, P.J.1    Brodie, A.F.2
  • 14
    • 0000122573 scopus 로고
    • PHYLIP-phylogeny inference package (version 3.2)
    • Felsenstein J (1989) PHYLIP-phylogeny inference package (version 3.2). Cladistics 5:164-166
    • (1989) Cladistics , vol.5 , pp. 164-166
    • Felsenstein, J.1
  • 15
    • 0037414756 scopus 로고    scopus 로고
    • Mechanism and substrate specificity of the flavin reductase ActVB from Streptomyces coelicolor
    • Filisetti L, Fontecave M, Niviere V (2003) Mechanism and substrate specificity of the flavin reductase ActVB from Streptomyces coelicolor. J Biol Chem 278:296-303
    • (2003) J Biol Chem , vol.278 , pp. 296-303
    • Filisetti, L.1    Fontecave, M.2    Niviere, V.3
  • 16
    • 0034666137 scopus 로고    scopus 로고
    • The role of pyruvate:Ferredoxin oxidoreductase in pyruvate synthesis during autotrophic growth by the Wood-Ljungdahl pathway
    • Furdui C, Ragsdale SW (2000) The role of pyruvate:ferredoxin oxidoreductase in pyruvate synthesis during autotrophic growth by the Wood-Ljungdahl pathway. J Biol Chem 275:28494-28499
    • (2000) J Biol Chem , vol.275 , pp. 28494-28499
    • Furdui, C.1    Ragsdale, S.W.2
  • 17
    • 0344855596 scopus 로고    scopus 로고
    • Expression vectors for Methancoccus maripaludis: Overexpression of acetohydroxyacid synthase and β-galactosidase
    • Gardner WL, Whitman WB (1999) Expression vectors for Methancoccus maripaludis: overexpression of acetohydroxyacid synthase and β-galactosidase. Genetics 152:1439-1447
    • (1999) Genetics , vol.152 , pp. 1439-1447
    • Gardner, W.L.1    Whitman, W.B.2
  • 18
    • 0025255109 scopus 로고
    • One-dimensional gel electrophoresis
    • Garfin DE (1990) One-dimensional gel electrophoresis. Methods Enzymol 182:425-441
    • (1990) Methods Enzymol , vol.182 , pp. 425-441
    • Garfin, D.E.1
  • 19
    • 0014254093 scopus 로고
    • Spectrophotometric determination of microgram quantities of protein without nucleic acid interference
    • Groves WE, Davis FC Jr., Sells BH (1968) Spectrophotometric determination of microgram quantities of protein without nucleic acid interference. Anal Biochem 22:195-210
    • (1968) Anal Biochem , vol.22 , pp. 195-210
    • Groves, W.E.1    Davis F.C., Jr.2    Sells, B.H.3
  • 20
    • 0024673276 scopus 로고
    • Isolation, characterization, and biological activity of the Methanococcus thermolithotrophicus ferredoxin
    • Hatchikian EC, Fardeau ML, Bruschi M, Belaich JP, Chapman A, Cammack R (1989) Isolation, characterization, and biological activity of the Methanococcus thermolithotrophicus ferredoxin. J Bacteriol 171:2384-2390
    • (1989) J Bacteriol , vol.171 , pp. 2384-2390
    • Hatchikian, E.C.1    Fardeau, M.L.2    Bruschi, M.3    Belaich, J.P.4    Chapman, A.5    Cammack, R.6
  • 21
    • 0024760701 scopus 로고
    • Pyruvate: NADP+ oxidoreductase from Euglena gracilis: The kinetic properties of the enzyme
    • Inui H, Miyatake K, Nakano Y, Kitaoka S (1989) Pyruvate: NADP+ oxidoreductase from Euglena gracilis: the kinetic properties of the enzyme. Arch Biochem Biophys 274:434-442
    • (1989) Arch Biochem Biophys , vol.274 , pp. 434-442
    • Inui, H.1    Miyatake, K.2    Nakano, Y.3    Kitaoka, S.4
  • 22
    • 0018830278 scopus 로고
    • Reconstitution of a formate-NADP+ oxidoreductase from formate dehydrogenase and a 5-deazaflavin-linked NADP+ reductase isolated from Methanococcus vannielii
    • Jones JB, Stadtman TC (1980) Reconstitution of a formate-NADP+ oxidoreductase from formate dehydrogenase and a 5-deazaflavin-linked NADP+ reductase isolated from Methanococcus vannielii. J Biol Chem 255:1049-1053
    • (1980) J Biol Chem , vol.255 , pp. 1049-1053
    • Jones, J.B.1    Stadtman, T.C.2
  • 23
    • 0002620715 scopus 로고
    • Characterization of Methanococcus maripaludis sp. nov., a new methanogen isolated from salt marsh sediment
    • Jones WJ, Paynter MJB, Gupta R (1983) Characterization of Methanococcus maripaludis sp. nov., a new methanogen isolated from salt marsh sediment. Arch Microbiol 135:91-97
    • (1983) Arch Microbiol , vol.135 , pp. 91-97
    • Jones, W.J.1    Paynter, M.J.B.2    Gupta, R.3
  • 24
    • 0019458899 scopus 로고
    • The catalytic mechanism of 2-oxoacid:Ferredoxin oxidoreductases from Halobacterium halobium: One-electron transfer at two distinct steps of the catalytic cycle
    • Kerscher L, Oesterhelt D (1981) The catalytic mechanism of 2-oxoacid:ferredoxin oxidoreductases from Halobacterium halobium: one-electron transfer at two distinct steps of the catalytic cycle. Eur J Biochem 116:595-600
    • (1981) Eur J Biochem , vol.116 , pp. 595-600
    • Kerscher, L.1    Oesterhelt, D.2
  • 25
    • 0032521598 scopus 로고    scopus 로고
    • An Escherichia coli hydrogenase-3-type hydrogenase in methanogenic archaea
    • Künkel A, Vorholt JA, Thauer RK, Hedderich R (1998) An Escherichia coli hydrogenase-3-type hydrogenase in methanogenic archaea. Eur J Biochem 252:467-476
    • (1998) Eur J Biochem , vol.252 , pp. 467-476
    • Künkel, A.1    Vorholt, J.A.2    Thauer, R.K.3    Hedderich, R.4
  • 27
    • 0037540252 scopus 로고
    • Chapter 3.5 Escherichia coli DNA polymerase I
    • Ausubel FM, Brent R, Kingston RE, Moore DD, Seidman JG, Smith JA, Struhl K (eds). Wiley, New York
    • Lehman IR (1989) Chapter 3.5 Escherichia coli DNA polymerase I, In: Ausubel FM, Brent R, Kingston RE, Moore DD, Seidman JG, Smith JA, Struhl K (eds) Current protocols in molecular biology. Wiley, New York, pp 9-10
    • (1989) Current Protocols in Molecular Biology , pp. 9-10
    • Lehman, I.R.1
  • 29
    • 0024387798 scopus 로고
    • Purification and characterization of the pyruvate-ferredoxin oxidoreductase from Clostridium acetobutylicum
    • Meinecke B, Bertran J, Gottschalk G (1989) Purification and characterization of the pyruvate-ferredoxin oxidoreductase from Clostridium acetobutylicum. Arch Microbiol 152:244-250
    • (1989) Arch Microbiol , vol.152 , pp. 244-250
    • Meinecke, B.1    Bertran, J.2    Gottschalk, G.3
  • 30
    • 0033214609 scopus 로고    scopus 로고
    • Purification and catalytic properties of Ech hydrogenase from Methanosarcina barkeri
    • Meuer J, Bartoschek S, Koch J, Künkel A, Hedderich R (1999) Purification and catalytic properties of Ech hydrogenase from Methanosarcina barkeri. Eur J Biochem 265:325-335
    • (1999) Eur J Biochem , vol.265 , pp. 325-335
    • Meuer, J.1    Bartoschek, S.2    Koch, J.3    Künkel, A.4    Hedderich, R.5
  • 31
    • 0037117505 scopus 로고    scopus 로고
    • Genetic analysis of the archaeon Methanosarcina barkeri Fusaro reveals a central role for the Ech hydrogenase and ferredoxin in methanogenesis and carbon fixation
    • Meuer J, Kuettner HC, Zhang JK, Hedderich R, Metcalf WM (2002) Genetic analysis of the archaeon Methanosarcina barkeri Fusaro reveals a central role for the Ech hydrogenase and ferredoxin in methanogenesis and carbon fixation. Proc Natl Acad Sci USA 99:5632-5637
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 5632-5637
    • Meuer, J.1    Kuettner, H.C.2    Zhang, J.K.3    Hedderich, R.4    Metcalf, W.M.5
  • 32
    • 0023657294 scopus 로고
    • Purification and characterization of an 8-hydroxy-5-deazaflavin-reducing hydrogenase from the archaebacterium Methanococcus voltae
    • Muth E, Mörschel E, Klein A (1987) Purification and characterization of an 8-hydroxy-5-deazaflavin-reducing hydrogenase from the archaebacterium Methanococcus voltae. Eur J Biochem 169:571-577
    • (1987) Eur J Biochem , vol.169 , pp. 571-577
    • Muth, E.1    Mörschel, E.2    Klein, A.3
  • 33
    • 0021765275 scopus 로고
    • FAD requirement for the reduction of coenzyme F420 by hydrogenase from Methanobacterium formicicum
    • Nelson MJK, Brown DP, Ferry JG (1984) FAD requirement for the reduction of coenzyme F420 by hydrogenase from Methanobacterium formicicum. Biochem Biophys Res Commun 120:775-781
    • (1984) Biochem Biophys Res Commun , vol.120 , pp. 775-781
    • Nelson, M.J.K.1    Brown, D.P.2    Ferry, J.G.3
  • 34
    • 0028324627 scopus 로고
    • Pyruvate as a substrate for growth and methanogenesis for Methanosarcina barkeri
    • Rajagopal BS, LeGall J (1994) Pyruvate as a substrate for growth and methanogenesis for Methanosarcina barkeri. Curr Microbiol 28:307-311
    • (1994) Curr Microbiol , vol.28 , pp. 307-311
    • Rajagopal, B.S.1    LeGall, J.2
  • 35
    • 0017615796 scopus 로고
    • An energy-conserving pyruvate-to-acetate pathway in Entamoeba histolytica: Pyruvate synthase and a new acetate thiokinase
    • Reeves RE, Warren LG, Susskind B, Lo H-S (1977) An energy-conserving pyruvate-to-acetate pathway in Entamoeba histolytica: pyruvate synthase and a new acetate thiokinase. J Biol Chem 252:726-731
    • (1977) J Biol Chem , vol.252 , pp. 726-731
    • Reeves, R.E.1    Warren, L.G.2    Susskind, B.3    Lo, H.-S.4
  • 36
    • 0026009206 scopus 로고
    • Alteration of the iron-sulfur cluster composition of Escherichia coli dimethyl sulfoxide reductase by site-directed mutagenesis
    • Rothery RA, Weiner JH (1991) Alteration of the iron-sulfur cluster composition of Escherichia coli dimethyl sulfoxide reductase by site-directed mutagenesis. Biochemistry 30:8296-8305
    • (1991) Biochemistry , vol.30 , pp. 8296-8305
    • Rothery, R.A.1    Weiner, J.H.2
  • 38
    • 50549178319 scopus 로고
    • Preparation of transforming deoxyribonucleic acid by phenol treatment
    • Saito H, Miura K-I (1963) Preparation of transforming deoxyribonucleic acid by phenol treatment. Biochim Biophys Acta 72:619-629
    • (1963) Biochim Biophys Acta , vol.72 , pp. 619-629
    • Saito, H.1    Miura, K.-I.2
  • 39
    • 0026725149 scopus 로고
    • Mutational analysis of the operon (hyc) determining hydrogenase 3 formation in Escherichia coli
    • Sauter M, Böhm R, Böck A (1992) Mutational analysis of the operon (hyc) determining hydrogenase 3 formation in Escherichia coli. Mol Microbiol 6:1523-1532
    • (1992) Mol Microbiol , vol.6 , pp. 1523-1532
    • Sauter, M.1    Böhm, R.2    Böck, A.3
  • 40
    • 0020805952 scopus 로고
    • 420 by formate dehydrogenase from Methanobacterium formicicum
    • 420 by formate dehydrogenase from Methanobacterium formicicum. J Bacteriol 155:467-472
    • (1983) J Bacteriol , vol.155 , pp. 467-472
    • Schauer, N.L.1    Ferry, J.G.2
  • 41
    • 0023447129 scopus 로고
    • Pathway of acetate assimilation in autotrophic and heterotrophic methanococci
    • Shieh JS, Whitman WB (1987) Pathway of acetate assimilation in autotrophic and heterotrophic methanococci. J Bacteriol 169:5327-5329
    • (1987) J Bacteriol , vol.169 , pp. 5327-5329
    • Shieh, J.S.1    Whitman, W.B.2
  • 42
    • 0024040652 scopus 로고
    • Autotrophic acetyl coenzyme A biosynthesis in Methanococcus maripaludis
    • Shieh JS, Whitman WB (1988) Autotrophic acetyl coenzyme A biosynthesis in Methanococcus maripaludis. J Bacteriol 170:3072-3079
    • (1988) J Bacteriol , vol.170 , pp. 3072-3079
    • Shieh, J.S.1    Whitman, W.B.2
  • 43
    • 0030937675 scopus 로고    scopus 로고
    • Structures and functions of four anabolic 2-oxoacid oxidoreductases in Methanobacterium thermoautotrophicum
    • Tersteegen A, Linder D, Thauer RK, Hedderich R (1997) Structures and functions of four anabolic 2-oxoacid oxidoreductases in Methanobacterium thermoautotrophicum. Eur J Biochem 244:862-868
    • (1997) Eur J Biochem , vol.244 , pp. 862-868
    • Tersteegen, A.1    Linder, D.2    Thauer, R.K.3    Hedderich, R.4
  • 44
    • 0042181939 scopus 로고
    • Glyoxylate inhibition of clostridial pyruvate synthase
    • Thauer RK, Rupprecht E, Jungermann K (1970) Glyoxylate inhibition of clostridial pyruvate synthase. FEBS Lett 9:271-273
    • (1970) FEBS Lett , vol.9 , pp. 271-273
    • Thauer, R.K.1    Rupprecht, E.2    Jungermann, K.3
  • 45
    • 0017343370 scopus 로고
    • Energy conservation in chemotrophic anaerobic bacteria
    • Thauer RK, Jungermann K, Decker K (1977) Energy conservation in chemotrophic anaerobic bacteria. Bacteriol Rev 41:100-180
    • (1977) Bacteriol Rev , vol.41 , pp. 100-180
    • Thauer, R.K.1    Jungermann, K.2    Decker, K.3
  • 46
    • 0015239525 scopus 로고
    • Pyruvate-ferredoxin oxidoreductase. III. Purification and properties of the enzyme
    • Uyeda K, Rabinowitz JC (1971) Pyruvate-ferredoxin oxidoreductase. III. Purification and properties of the enzyme. J Biol Chem 246:3111-3119
    • (1971) J Biol Chem , vol.246 , pp. 3111-3119
    • Uyeda, K.1    Rabinowitz, J.C.2
  • 47
    • 0032951727 scopus 로고    scopus 로고
    • Glutamate synthase: A complex iron-sulfur flavoprotein
    • Vanoni MA, Curti B (1999) Glutamate synthase: a complex iron-sulfur flavoprotein. Cell Mol Life Sci 55:617-638
    • (1999) Cell Mol Life Sci , vol.55 , pp. 617-638
    • Vanoni, M.A.1    Curti, B.2
  • 48
    • 0009865535 scopus 로고    scopus 로고
    • Genus I. Methanococcus
    • Boone DR, Castenholz RW, Garrity GM (eds). Springer, Berlin Heidelberg New York
    • Whitman WB (2001) Genus I. Methanococcus- In: Boone DR, Castenholz RW, Garrity GM (eds) Bergey's manual of systematic bacteriology, 2nd edn, vol 1. Springer, Berlin Heidelberg New York, pp 236-240
    • (2001) Bergey's Manual of Systematic Bacteriology, 2nd Edn. , vol.1 , pp. 236-240
    • Whitman, W.B.1
  • 49
    • 0020051044 scopus 로고
    • Nutrition and carbon metabolism of Methanococcus voltae
    • Whitman WB, Ankwanda E, Wolfe RS (1982) Nutrition and carbon metabolism of Methanococcus voltae. J Bacteriol 149:852-863
    • (1982) J Bacteriol , vol.149 , pp. 852-863
    • Whitman, W.B.1    Ankwanda, E.2    Wolfe, R.S.3
  • 51
    • 0023404189 scopus 로고
    • Purification and characterization of pyruvate:Ferredoxin oxidoreductase from the anaerobic protozoon Trichomonas vaginalis
    • Williams K, Lowe PN, Leadlay PF (1987) Purification and characterization of pyruvate:ferredoxin oxidoreductase from the anaerobic protozoon Trichomonas vaginalis. Biochem J 246:529-536
    • (1987) Biochem J , vol.246 , pp. 529-536
    • Williams, K.1    Lowe, P.N.2    Leadlay, P.F.3
  • 52
    • 0026501143 scopus 로고
    • Characterization of amino acid aminotransferases of Methanococcus aeolicus
    • Xing R, Whitman WB (1992) Characterization of amino acid aminotransferases of Methanococcus aeolicus. J Bacteriol 174:541-548
    • (1992) J Bacteriol , vol.174 , pp. 541-548
    • Xing, R.1    Whitman, W.B.2
  • 54
    • 0030958588 scopus 로고    scopus 로고
    • Carboxylation reactions of pyruvate:Ferredoxin oxidoreductase and 2-oxoglutarate:Ferredoxin oxidoreductase from Hydrogenobacter thermophilus TK-6
    • Yoon K-S, Ishii M, Kodama T, Igarashi Y (1997) Carboxylation reactions of pyruvate:ferredoxin oxidoreductase and 2-oxoglutarate:ferredoxin oxidoreductase from Hydrogenobacter thermophilus TK-6. Biosci Biotechnol Biochem 61:510-513
    • (1997) Biosci Biotechnol Biochem , vol.61 , pp. 510-513
    • Yoon, K.-S.1    Ishii, M.2    Kodama, T.3    Igarashi, Y.4
  • 55
    • 0033570050 scopus 로고    scopus 로고
    • Rubredoxin from the green sulfur bacterium Chlorobium tepidum functions as an electron acceptor for pyruvate ferredoxin oxidoreductase
    • Yoon K-S, Hille R, Hemann C, Tabita FR (1999) Rubredoxin from the green sulfur bacterium Chlorobium tepidum functions as an electron acceptor for pyruvate ferredoxin oxidoreductase. J Biol Chem 274:29772-29778
    • (1999) J Biol Chem , vol.274 , pp. 29772-29778
    • Yoon, K.-S.1    Hille, R.2    Hemann, C.3    Tabita, F.R.4
  • 56
    • 0035941189 scopus 로고    scopus 로고
    • Spectroscopic and functional properties of novel 2[4Fe-4S] cluster-containing ferredoxins from the green sulfur bacterium Chlorobium tepidum
    • Yoon K-S, Bobst C, Hemann CF, Hille R, Tabita FR (2001) Spectroscopic and functional properties of novel 2[4Fe-4S] cluster-containing ferredoxins from the green sulfur bacterium Chlorobium tepidum. J Biol Chem 276:44027-44036
    • (2001) J Biol Chem , vol.276 , pp. 44027-44036
    • Yoon, K.-S.1    Bobst, C.2    Hemann, C.F.3    Hille, R.4    Tabita, F.R.5
  • 57
    • 0017709116 scopus 로고
    • Oxidoreductase involved in cell carbon synthesis of Methanobacterium thermoautotrophicum
    • Zeikus, JG, Fuchs G, Kenealy W, Thauer RK (1977) Oxidoreductase involved in cell carbon synthesis of Methanobacterium thermoautotrophicum. J Bacteriol 132:604-613
    • (1977) J Bacteriol , vol.132 , pp. 604-613
    • Zeikus, J.G.1    Fuchs, G.2    Kenealy, W.3    Thauer, R.K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.