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Volumn 265, Issue 1, 1999, Pages 325-335

Purification and catalytic properties of Ech hydrogenase from Methanosarcina barkeri

Author keywords

Complex I; Energy conservation; Ferredoxin; Hydrogenase; Iron sulfur protein; Methanosarcina barkeri

Indexed keywords

BACTERIAL ENZYME; FERREDOXIN;

EID: 0033214609     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00738.x     Document Type: Article
Times cited : (125)

References (51)
  • 1
    • 0029967858 scopus 로고    scopus 로고
    • Pathways of energy conservation in methanogenic archaea
    • 1. Deppenmeier, U., Müller, V. & Gottschalk, G. (1996) Pathways of energy conservation in methanogenic archaea. Arch. Microbiol. 165, 149-163.
    • (1996) Arch. Microbiol. , vol.165 , pp. 149-163
    • Deppenmeier, U.1    Müller, V.2    Gottschalk, G.3
  • 2
    • 0033005876 scopus 로고    scopus 로고
    • Enzymology of one-carbon metabolism in methanogenic pathways
    • 2. Ferry, J.G. (1999) Enzymology of one-carbon metabolism in methanogenic pathways. FEMS Microbiol. Rev. 23, 13-38.
    • (1999) FEMS Microbiol. Rev. , vol.23 , pp. 13-38
    • Ferry, J.G.1
  • 3
    • 0031685510 scopus 로고    scopus 로고
    • Biochemistry of methanogenesis: A tribute to Marjory Stephenson
    • 3. Thauer, R.K. (1998) Biochemistry of methanogenesis: a tribute to Marjory Stephenson. Microbiology 144, 2377-2406.
    • (1998) Microbiology , vol.144 , pp. 2377-2406
    • Thauer, R.K.1
  • 4
    • 0024727930 scopus 로고
    • 420-reducing hydrogenase from Methanosarcina barkeri (strain Fusaro)
    • 420-reducing hydrogenase from Methanosarcina barkeri (strain Fusaro). Eur. J. Biochem. 184, 79-88.
    • (1989) Eur. J. Biochem. , vol.184 , pp. 79-88
    • Fiebig, K.1    Friedrich, B.2
  • 5
    • 0028810413 scopus 로고
    • Biochemical characterization of the 8-hydroxy-5-deazaflavin-reactive hydrogenase from Methanosarcina barkeri Fusaro
    • 5. Michel, R., Massanz, C., Kostka, S., Richter, M. & Fiebig, K. (1995) Biochemical characterization of the 8-hydroxy-5-deazaflavin-reactive hydrogenase from Methanosarcina barkeri Fusaro. Eur. J. Biochem. 233, 727-735.
    • (1995) Eur. J. Biochem. , vol.233 , pp. 727-735
    • Michel, R.1    Massanz, C.2    Kostka, S.3    Richter, M.4    Fiebig, K.5
  • 6
    • 0031908850 scopus 로고    scopus 로고
    • 420-reducing hydrogenases in Methanosarcina barkeri
    • 420-reducing hydrogenases in Methanosarcina barkeri. Arch. Microbiol. 169, 201-205.
    • (1998) Arch. Microbiol. , vol.169 , pp. 201-205
    • Vaupel, M.1    Thauer, R.K.2
  • 7
    • 0028009865 scopus 로고
    • Purification and characterization of membrane bound hydrogenase from Methanosarcina barkeri MS
    • 7. Kemner, J.M. & Zeikus, J.G. (1994) Purification and characterization of membrane bound hydrogenase from Methanosarcina barkeri MS. Arch. Microbiol 161, 47-54.
    • (1994) Arch. Microbiol , vol.161 , pp. 47-54
    • Kemner, J.M.1    Zeikus, J.G.2
  • 9
    • 0028890441 scopus 로고
    • Analysis of the vhoGAC and vhtGAC operons from Methanosarcina mazei strain Göl, both encoding a membrane-bound hydrogenase and a cytochrome b
    • 9. Deppenmeier, U., Blaut, M., Lentes, S., Herzberg, C. & Gottschalk, G. (1995) Analysis of the vhoGAC and vhtGAC operons from Methanosarcina mazei strain Göl, both encoding a membrane-bound hydrogenase and a cytochrome b. Eur. J. Biochem. 227, 261-269.
    • (1995) Eur. J. Biochem. , vol.227 , pp. 261-269
    • Deppenmeier, U.1    Blaut, M.2    Lentes, S.3    Herzberg, C.4    Gottschalk, G.5
  • 10
    • 0028790975 scopus 로고
    • Different structure and expression of the operons encoding the membrane-bound hydrogenases from Methanosarcina mazei Göl
    • 10. Deppenmeier, U. (1995) Different structure and expression of the operons encoding the membrane-bound hydrogenases from Methanosarcina mazei Göl. Arch. Microbiol. 164, 370-376.
    • (1995) Arch. Microbiol. , vol.164 , pp. 370-376
    • Deppenmeier, U.1
  • 11
    • 0032521598 scopus 로고    scopus 로고
    • An Escherichia coli hydrogenase-3-type hydrogenase in methanogenic archaea
    • 11. Künkel, A., Vorholt, J.A., Thauer, R.K. & 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
  • 12
    • 0031055712 scopus 로고    scopus 로고
    • Heterodisulfide reductase from methanol-grown cells of Methanosarcina barkeri is not a flavoenzyme
    • 12. Künkel, A., Vaupel, M., Heim, S., Thauer, R.K. & Hedderich, R. (1997) Heterodisulfide reductase from methanol-grown cells of Methanosarcina barkeri is not a flavoenzyme. Eur. J. Biochem. 244, 226-234.
    • (1997) Eur. J. Biochem. , vol.244 , pp. 226-234
    • Künkel, A.1    Vaupel, M.2    Heim, S.3    Thauer, R.K.4    Hedderich, R.5
  • 13
    • 0025157053 scopus 로고
    • Nucleotide sequence and expression of an operon in Escherichia coli coding for formate hydrogenlyase components
    • 13. Böhm, R., Sauter, M. & Böck, A. (1990) Nucleotide sequence and expression of an operon in Escherichia coli coding for formate hydrogenlyase components. Mol. Microbiol. 4, 231-243.
    • (1990) Mol. Microbiol. , vol.4 , pp. 231-243
    • Böhm, R.1    Sauter, M.2    Böck, A.3
  • 14
    • 0026725149 scopus 로고
    • Mutational analysis of the operon (hyc) determining hydrogenase 3 formation in Escherichia coli
    • 14. 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
  • 15
    • 0030725104 scopus 로고    scopus 로고
    • A 12-cistron Escherichia coli operon (hyf) encoding a putative proton-translocating formate hydrogenlyase system
    • 15. Andrews, S.C., Berks, B.C., McClay, J., Ambler, A., Quail, M.A., Golby, P. & Guest, J.R. (1997) A 12-cistron Escherichia coli operon (hyf) encoding a putative proton-translocating formate hydrogenlyase system. Microbiology 143, 3633-3647.
    • (1997) Microbiology , vol.143 , pp. 3633-3647
    • Andrews, S.C.1    Berks, B.C.2    McClay, J.3    Ambler, A.4    Quail, M.A.5    Golby, P.6    Guest, J.R.7
  • 16
    • 10344238576 scopus 로고    scopus 로고
    • Characterization of the region encoding the CO-induced hydrogenase of Rhodospirillum rubrum
    • 16. Fox, J.D., He, Y., Shelver, D., Roberts, G.P. & Ludden, P.W. (1996) Characterization of the region encoding the CO-induced hydrogenase of Rhodospirillum rubrum. J. Bacteriol. 178, 6200-6208.
    • (1996) J. Bacteriol. , vol.178 , pp. 6200-6208
    • Fox, J.D.1    He, Y.2    Shelver, D.3    Roberts, G.P.4    Ludden, P.W.5
  • 17
    • 0029915837 scopus 로고    scopus 로고
    • Characterization of the CO-induced, CO-tolerant hydrogenase from Rhodospirillum rubrum and the gene encoding the large subunit of the enzyme
    • 17. Fox, J.D., Kerby, R.L., Roberts, G.P. & Ludden, P.W. (1996) Characterization of the CO-induced, CO-tolerant hydrogenase from Rhodospirillum rubrum and the gene encoding the large subunit of the enzyme. J. Bacteriol. 178, 1515-1524.
    • (1996) J. Bacteriol. , vol.178 , pp. 1515-1524
    • Fox, J.D.1    Kerby, R.L.2    Roberts, G.P.3    Ludden, P.W.4
  • 18
    • 0031582715 scopus 로고    scopus 로고
    • Modular evolution of the respiratory NADH:Ubiquinone oxidoreductase and the origin of its modules
    • 18. Friedrich, T. & Weiss, H. (1997) Modular evolution of the respiratory NADH:ubiquinone oxidoreductase and the origin of its modules. J. Theor. Biol. 187, 529-540.
    • (1997) J. Theor. Biol. , vol.187 , pp. 529-540
    • Friedrich, T.1    Weiss, H.2
  • 19
    • 0000549132 scopus 로고
    • Carbonic anhydrase activity in acetate grown Methanosarcina barkeri
    • 19. Karrasch, M., Bott, M. & Thauer, R.K. (1989) Carbonic anhydrase activity in acetate grown Methanosarcina barkeri. Arch. Microbiol. 151, 137-142.
    • (1989) Arch. Microbiol. , vol.151 , pp. 137-142
    • Karrasch, M.1    Bott, M.2    Thauer, R.K.3
  • 21
    • 84981751839 scopus 로고
    • Zur Kenntnis der o-Chinone
    • 21. Willstätter, R. & Müller, F. (1911) Zur Kenntnis der o-Chinone. Chem. Ber. 44, 2171-2185.
    • (1911) Chem. Ber. , vol.44 , pp. 2171-2185
    • Willstätter, R.1    Müller, F.2
  • 22
    • 0025045750 scopus 로고
    • Ferredoxin-dependent methane formation from acetate in cell extracts of Methanosarcina barkeri (strain MS)
    • 22. Fischer, R. & Thauer, R.K. (1990) Ferredoxin-dependent methane formation from acetate in cell extracts of Methanosarcina barkeri (strain MS). FEBS Lett. 269, 368-372.
    • (1990) FEBS Lett. , vol.269 , pp. 368-372
    • Fischer, R.1    Thauer, R.K.2
  • 23
    • 0025787641 scopus 로고
    • Catalysis of acetyl-CoA cleavage and tetrahydrosarcinapterin methylation by a carbon monoxide dehydrogenase-corrinoid enzyme complex
    • 23. Grahame, D.A. (1991) Catalysis of acetyl-CoA cleavage and tetrahydrosarcinapterin methylation by a carbon monoxide dehydrogenase-corrinoid enzyme complex. J. Biol. Chem. 266, 22227-22233.
    • (1991) J. Biol. Chem. , vol.266 , pp. 22227-22233
    • Grahame, D.A.1
  • 24
    • 33847088763 scopus 로고
    • Low-pressure solubility of gases in liquid water
    • 24. Wilhelm, E., Battino, R. & Wilcock, R.J. (1977) Low-pressure solubility of gases in liquid water. Chem. Rev. 77, 219-238.
    • (1977) Chem. Rev. , vol.77 , pp. 219-238
    • Wilhelm, E.1    Battino, R.2    Wilcock, R.J.3
  • 25
    • 0018437933 scopus 로고
    • A simple hydrogenase-linked assay for ferredoxin and flavodoxin
    • 25. Chen, J.-S. & Blanchard, D.K. (1979) A simple hydrogenase-linked assay for ferredoxin and flavodoxin. Anal. Biochem. 93, 216-222.
    • (1979) Anal. Biochem. , vol.93 , pp. 216-222
    • Chen, J.-S.1    Blanchard, D.K.2
  • 26
    • 0023899855 scopus 로고
    • Rapid colorimetric micromethod for the quantitation of complexed iron in biological samples
    • (Riordan, J.F. & Vallee, B.L., eds), Academic Press, New York, USA
    • 26. Fish, W.W. (1988) Rapid colorimetric micromethod for the quantitation of complexed iron in biological samples. In Methods in Enzymology (Riordan, J.F. & Vallee, B.L., eds), pp. 357-364. Academic Press, New York, USA.
    • (1988) Methods in Enzymology , pp. 357-364
    • Fish, W.W.1
  • 27
    • 84944816274 scopus 로고
    • Spectrophotometric determination of hydrogen sulfide in natural waters
    • 27. Cline, J.D. (1969) Spectrophotometric determination of hydrogen sulfide in natural waters. Limnol. Oceanogr. 14, 454-458.
    • (1969) Limnol. Oceanogr. , vol.14 , pp. 454-458
    • Cline, J.D.1
  • 28
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • 28. 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
  • 31
    • 0028933835 scopus 로고
    • Substrate and accessory protein requirements and thermodynamics of acetyl-CoA synthesis and cleavage in Methanosarcina barkeri
    • 31. Grahame, D.A. & DeMoll, E. (1995) Substrate and accessory protein requirements and thermodynamics of acetyl-CoA synthesis and cleavage in Methanosarcina barkeri. Biochemistry 34, 4617-4624.
    • (1995) Biochemistry , vol.34 , pp. 4617-4624
    • Grahame, D.A.1    DeMoll, E.2
  • 32
    • 0028124489 scopus 로고
    • Regulation and function of ferredoxin-linked versus cytochrome b-linked hydrogenase in electron transfer and energy metabolism of Methanosarcina barkeri MS
    • 32. Kemner, J.M. & Zeikus, J.G. (1994) Regulation and function of ferredoxin-linked versus cytochrome b-linked hydrogenase in electron transfer and energy metabolism of Methanosarcina barkeri MS. Arch. Microbiol. 162, 26-32.
    • (1994) Arch. Microbiol. , vol.162 , pp. 26-32
    • Kemner, J.M.1    Zeikus, J.G.2
  • 33
    • 0025297235 scopus 로고
    • The same domain motif for ubiquinone reduction in mitochondrial or chloroplast NADH dehydrogenase and bacterial glucose dehydrogenase
    • 33. Friedrich, T., Strohdeicher, M., Hofhaus, G., Preis, D., Sahm, H. & Weiss, H. (1990) The same domain motif for ubiquinone reduction in mitochondrial or chloroplast NADH dehydrogenase and bacterial glucose dehydrogenase. FEBS Lett. 265, 37-40.
    • (1990) FEBS Lett. , vol.265 , pp. 37-40
    • Friedrich, T.1    Strohdeicher, M.2    Hofhaus, G.3    Preis, D.4    Sahm, H.5    Weiss, H.6
  • 34
    • 0031921345 scopus 로고    scopus 로고
    • Isolation and characterization of methanophenazine and function of phenazines in membrane-bound electron transport of Methanosarcina mazei Göl
    • 34. Abken, H.J., Tietze, M., Brodersen, J., Bäumer, S., Beifuss, U. & Deppenmeier, U. (1998) Isolation and characterization of methanophenazine and function of phenazines in membrane-bound electron transport of Methanosarcina mazei Göl. J. Bacteriol. 180, 2027-2032.
    • (1998) J. Bacteriol. , vol.180 , pp. 2027-2032
    • Abken, H.J.1    Tietze, M.2    Brodersen, J.3    Bäumer, S.4    Beifuss, U.5    Deppenmeier, U.6
  • 35
    • 0023653187 scopus 로고
    • 8-Hydroxy-5-deazaflavin-reducing hydrogenase from Methanobacterium thermoautotrophicum: 1. Purification and characterization
    • 35. Fox, J.A., Livingston, D.J., Orme-Johnson, W.H. & Walsh, C.T. (1987) 8-Hydroxy-5-deazaflavin-reducing hydrogenase from Methanobacterium thermoautotrophicum: 1. Purification and characterization. Biochemistry 26, 4219-4227.
    • (1987) Biochemistry , vol.26 , pp. 4219-4227
    • Fox, J.A.1    Livingston, D.J.2    Orme-Johnson, W.H.3    Walsh, C.T.4
  • 36
    • 0033555715 scopus 로고    scopus 로고
    • Inhibition of membrane-bound electron transport of the methanogenic archaeon Methanosarcina mazei Göl by diphenyleneiodonium
    • 36. Brodersen, J., Bäumer, S., Abken, H.J., Gottschalk, G. & Deppenmeier, U. (1999) Inhibition of membrane-bound electron transport of the methanogenic archaeon Methanosarcina mazei Göl by diphenyleneiodonium. Eur. J. Biochem. 259, 218-224.
    • (1999) Eur. J. Biochem. , vol.259 , pp. 218-224
    • Brodersen, J.1    Bäumer, S.2    Abken, H.J.3    Gottschalk, G.4    Deppenmeier, U.5
  • 37
    • 0022779582 scopus 로고
    • 2 with the phosphorylation of ADP in acetate-grown Methanosarcina barkeri
    • 2 with the phosphorylation of ADP in acetate-grown Methanosarcina barkeri. Eur. J. Biochem. 159, 393-398.
    • (1986) Eur. J. Biochem. , vol.159 , pp. 393-398
    • Bott, M.1    Eikmanns, B.2    Thauer, R.K.3
  • 38
    • 0021930747 scopus 로고
    • Production and consumption of hydrogen during growth of Methanosarcina-spp on acetate
    • 38. Lovley, D.R. & Ferry, J.G. (1985) Production and consumption of hydrogen during growth of Methanosarcina-spp on acetate. Appl. Environ. Microbiol. 49, 247-249.
    • (1985) Appl. Environ. Microbiol. , vol.49 , pp. 247-249
    • Lovley, D.R.1    Ferry, J.G.2
  • 39
    • 0023107043 scopus 로고
    • Hydrogen metabolism during methanogenesis from acetate by Methanosarcina barkeri
    • 39. Krzycki, J.A., Morgan, J.B., Conrad, R. & Zeikus, J.G. (1987) Hydrogen metabolism during methanogenesis from acetate by Methanosarcina barkeri. FEMS Microbiol. Lett. 40, 193-198.
    • (1987) FEMS Microbiol. Lett. , vol.40 , pp. 193-198
    • Krzycki, J.A.1    Morgan, J.B.2    Conrad, R.3    Zeikus, J.G.4
  • 40
    • 0025986217 scopus 로고
    • Hydrogen inhibition of acetate metabolism and kinetics of hydrogen consumption by Methanosarcina thermophila TM-1
    • 40. Ahring, B.K., Westermann, P. & Mah, R.A. (1991) Hydrogen inhibition of acetate metabolism and kinetics of hydrogen consumption by Methanosarcina thermophila TM-1. Arch. Microbiol. 157, 38-42.
    • (1991) Arch. Microbiol. , vol.157 , pp. 38-42
    • Ahring, B.K.1    Westermann, P.2    Mah, R.A.3
  • 42
    • 0023932844 scopus 로고
    • Ferredoxin requirement for electron transport from the carbon monoxide dehydrogenase complex to a membrane-bound hydrogenase in acetate-grown Methanosarcina thermophila
    • 42. Terlesky, K.C. & Ferry, J.G. (1988) Ferredoxin requirement for electron transport from the carbon monoxide dehydrogenase complex to a membrane-bound hydrogenase in acetate-grown Methanosarcina thermophila. J. Biol. Chem. 263, 4075-4079.
    • (1988) J. Biol. Chem. , vol.263 , pp. 4075-4079
    • Terlesky, K.C.1    Ferry, J.G.2
  • 43
    • 0028130513 scopus 로고
    • Characterization of a CO:Heterodisulfide oxidoreductase system from acetate-grown Methanosarcina thermophila
    • 43. Peer, C.W., Painter, M.H., Rasche, M.E. & Ferry, J.G. (1994) Characterization of a CO:heterodisulfide oxidoreductase system from acetate-grown Methanosarcina thermophila. J. Bacteriol. 176, 6974-6979.
    • (1994) J. Bacteriol. , vol.176 , pp. 6974-6979
    • Peer, C.W.1    Painter, M.H.2    Rasche, M.E.3    Ferry, J.G.4
  • 44
    • 0032516483 scopus 로고    scopus 로고
    • Purification and properties of the heme-and iron-sulfur-containing heterodisulfide reductase from Methanosarcina thermophila
    • 44. Simianu, M., Murakami, E., Brewer, J.M. & Ragsdale, S.W. (1998) Purification and properties of the heme-and iron-sulfur-containing heterodisulfide reductase from Methanosarcina thermophila. Biochemistry 37, 10027-10039.
    • (1998) Biochemistry , vol.37 , pp. 10027-10039
    • Simianu, M.1    Murakami, E.2    Brewer, J.M.3    Ragsdale, S.W.4
  • 45
    • 0025979785 scopus 로고
    • 2:Heterodisulfide oxidoreductase a second energy-conserving system in the methanogenic strain Göl
    • 2:heterodisulfide oxidoreductase a second energy-conserving system in the methanogenic strain Göl. Arch. Microbiol. 155, 272-277.
    • (1991) Arch. Microbiol. , vol.155 , pp. 272-277
    • Deppenmeier, U.1    Blaut, M.2    Gottschalk, G.3
  • 47
    • 0033568398 scopus 로고    scopus 로고
    • Methanobacterium thermoautotrophicum encodes two multi-subunit membrane-bound [NiFe] hydrogenases. Transcription of the operons and sequence analysis of the deduced proteins
    • in press
    • 47. Tersteegen, A. & Hedderich, R. (1999) Methanobacterium thermoautotrophicum encodes two multi-subunit membrane-bound [NiFe] hydrogenases. Transcription of the operons and sequence analysis of the deduced proteins. Eur. J. Biochem. (in press).
    • (1999) Eur. J. Biochem.
    • Tersteegen, A.1    Hedderich, R.2
  • 48
    • 0029075136 scopus 로고
    • Isolation and characterization of the proton-translocating NADH: Ubiquinone oxidoreductase from Escherichia coli
    • 48. Leif, H., Sled, V.D., Ohnishi, T., Weiss, H. & Friedrich, T. (1995) Isolation and characterization of the proton-translocating NADH: ubiquinone oxidoreductase from Escherichia coli. Eur. J. Biochem. 230, 538-548.
    • (1995) Eur. J. Biochem. , vol.230 , pp. 538-548
    • Leif, H.1    Sled, V.D.2    Ohnishi, T.3    Weiss, H.4    Friedrich, T.5
  • 49
    • 0019324533 scopus 로고
    • An analysis of some thermodynamic properties of iron-sulphur centres in site i of mitochondria
    • 49. Ingledew, W.J. & Ohnishi, T. (1980) An analysis of some thermodynamic properties of iron-sulphur centres in site I of mitochondria. Biochem. J. 186, 111-117.
    • (1980) Biochem. J. , vol.186 , pp. 111-117
    • Ingledew, W.J.1    Ohnishi, T.2
  • 50
    • 0031046751 scopus 로고    scopus 로고
    • The iron-sulfur clusters 2 and ubisemiquinone radicals of NADH:Ubiquinone oxidoreductase are involved in energy coupling in submitochondrial particles
    • 50. van Belzen, R., Kotlyar, A.B., Moon, N., Dunham, W.R. & Albracht, S.P.J. (1997) The iron-sulfur clusters 2 and ubisemiquinone radicals of NADH:ubiquinone oxidoreductase are involved in energy coupling in submitochondrial particles. Biochemistry 36, 886-893.
    • (1997) Biochemistry , vol.36 , pp. 886-893
    • Van Belzen, R.1    Kotlyar, A.B.2    Moon, N.3    Dunham, W.R.4    Albracht, S.P.J.5
  • 51
    • 0009741233 scopus 로고
    • LXXVII. Hydrogenlyases. IV. The synthesis of formic acid by bacteria
    • 51. Woods, D.D. (1936) LXXVII. Hydrogenlyases. IV. The synthesis of formic acid by bacteria. Biochem. J. 30, 515-527.
    • (1936) Biochem. J. , vol.30 , pp. 515-527
    • Woods, D.D.1


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