메뉴 건너뛰기




Volumn 189, Issue 20, 2007, Pages 7392-7398

Expression and association of group IV nitrogenase NifD and NifH homologs in the non-nitrogen-fixing archaeon Methanocaldococcus jannaschii

Author keywords

[No Author keywords available]

Indexed keywords

NITROGEN; NITROGENASE; PROTEIN BCHL; PROTEIN BCHN; PROTEIN NIFD; PROTEIN NIFH; STRUCTURAL PROTEIN; UNCLASSIFIED DRUG;

EID: 35048881646     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.00876-07     Document Type: Article
Times cited : (49)

References (55)
  • 1
    • 20144364162 scopus 로고    scopus 로고
    • Higher-level classification of the Archaea: Evolution of methanogenesis and methanogens
    • Bapteste, E., C. Brochier, and Y. Boucher. 2005. Higher-level classification of the Archaea: evolution of methanogenesis and methanogens. Archaea 1:353-363.
    • (2005) Archaea , vol.1 , pp. 353-363
    • Bapteste, E.1    Brochier, C.2    Boucher, Y.3
  • 2
    • 0013945221 scopus 로고
    • The nitrogenase system from Azotobacter: Two-enzyme requirement for N2 reduction, ATP-dependent H2 evolution, and ATP hydrolysis
    • Bulen, W. A., and J. R. LeComte. 1966. The nitrogenase system from Azotobacter: two-enzyme requirement for N2 reduction, ATP-dependent H2 evolution, and ATP hydrolysis. Proc. Natl. Acad. Sci. USA 56:979-986.
    • (1966) Proc. Natl. Acad. Sci. USA , vol.56 , pp. 979-986
    • Bulen, W.A.1    LeComte, J.R.2
  • 3
    • 16044367245 scopus 로고    scopus 로고
    • Bult, C. J., O. White, G. J. Olsen, L. Zhou, R. D. Fleischmann, G. G. Sutton, J. A. Blake, L. M. FitzGerald, R. A. Clayton, J. D. Gocayne, A. R. Kerlavage, B. A. Dougherty, J.-F. Tomb, M. D. Adams, C. L. Reich, R. Overbeek, E. F. Kirkness, K. G. Weinstock, J. M. Merrick, A. Glodek, J. L. Scott, N. S. M. Geoghagen, J. F. Weidman, J. L. Fuhrmann, D. Nguyen, T. R. Utterback, J. M. Kelley, J. D. Peterson, P. W. Sadow, M. C. Hanna, M. D. Cotton, K. M. Roberts, M. A. Hurst, B. P. Kaine, M. Borodovsky, H.-P. Klenk, C. M. Fraser, H. O. Smith, C. R. Woese, and J. C. Venter. 1996. Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii. Science 273:1058-1073.
    • Bult, C. J., O. White, G. J. Olsen, L. Zhou, R. D. Fleischmann, G. G. Sutton, J. A. Blake, L. M. FitzGerald, R. A. Clayton, J. D. Gocayne, A. R. Kerlavage, B. A. Dougherty, J.-F. Tomb, M. D. Adams, C. L. Reich, R. Overbeek, E. F. Kirkness, K. G. Weinstock, J. M. Merrick, A. Glodek, J. L. Scott, N. S. M. Geoghagen, J. F. Weidman, J. L. Fuhrmann, D. Nguyen, T. R. Utterback, J. M. Kelley, J. D. Peterson, P. W. Sadow, M. C. Hanna, M. D. Cotton, K. M. Roberts, M. A. Hurst, B. P. Kaine, M. Borodovsky, H.-P. Klenk, C. M. Fraser, H. O. Smith, C. R. Woese, and J. C. Venter. 1996. Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii. Science 273:1058-1073.
  • 4
    • 0025951956 scopus 로고
    • Methanopyrus kandleri: An archaeal methanogen unrelated to all other known methanogens
    • Burggraf, S., K. O. Stetter, P. Rouviere, and C. R. Woese. 1991. Methanopyrus kandleri: an archaeal methanogen unrelated to all other known methanogens. Syst. Appl. Microbiol. 14:346-351.
    • (1991) Syst. Appl. Microbiol , vol.14 , pp. 346-351
    • Burggraf, S.1    Stetter, K.O.2    Rouviere, P.3    Woese, C.R.4
  • 5
    • 0027205389 scopus 로고
    • Early evolution of photosynthesis: Clues from nitrogenase and chlorophyll iron proteins
    • Burke, D. H., J. E. Hearst, and A. Sidow. 1993. Early evolution of photosynthesis: clues from nitrogenase and chlorophyll iron proteins. Proc. Natl. Acad. Sci. USA 90:7134-7138.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 7134-7138
    • Burke, D.H.1    Hearst, J.E.2    Sidow, A.3
  • 6
    • 34247620868 scopus 로고    scopus 로고
    • Biochemical and structural characterization of mammalian-like purine nucleoside Phosphorylase from the Archaeon Pyrococcus furiosus
    • Cacciapuoti, G., S. Gorassini, M. F. Mazzeo, R. A. Siciliano, V. Carbone, V. Zappia, and M. Porcelli. 2007. Biochemical and structural characterization of mammalian-like purine nucleoside Phosphorylase from the Archaeon Pyrococcus furiosus. FEBS J. 274:2482-2495.
    • (2007) FEBS J , vol.274 , pp. 2482-2495
    • Cacciapuoti, G.1    Gorassini, S.2    Mazzeo, M.F.3    Siciliano, R.A.4    Carbone, V.5    Zappia, V.6    Porcelli, M.7
  • 7
    • 0027159222 scopus 로고
    • The nitrogenase FeMo-cofactor and P-cluster pair: 2.2 A resolution structures
    • Chan, M. K., J. Kim, and D. C. Rees. 1993. The nitrogenase FeMo-cofactor and P-cluster pair: 2.2 A resolution structures. Science 260:792-794.
    • (1993) Science , vol.260 , pp. 792-794
    • Chan, M.K.1    Kim, J.2    Rees, D.C.3
  • 9
    • 0019498708 scopus 로고
    • Nitrogenase of Klebsiella pneumoniae. Hydrazine is a product of azide reduction
    • Dilworth, M. J., and R. N. Thorneley. 1981. Nitrogenase of Klebsiella pneumoniae. Hydrazine is a product of azide reduction. Biochem. J. 193:971-983.
    • (1981) Biochem. J , vol.193 , pp. 971-983
    • Dilworth, M.J.1    Thorneley, R.N.2
  • 10
    • 3943085693 scopus 로고    scopus 로고
    • Spectroscopic investigation of the nickel-containing porphinoid cofactor F(430). Comparison of the free cofactor in the +1, +2 and +3 oxidation states with the cofactor bound to methyl-coenzyme M reductase in the silent, red, and ox forms
    • Duin, E. C., L. Signer, R. Piskorski, F. Mahlert, M. D. Clay, M. Goenrich, R. K. Thauer, B. Jaun, and M. K. Johnson. 2004. Spectroscopic investigation of the nickel-containing porphinoid cofactor F(430). Comparison of the free cofactor in the +1, +2 and +3 oxidation states with the cofactor bound to methyl-coenzyme M reductase in the silent, red, and ox forms. J. Biol. Inorg. Chem. 9:563-576.
    • (2004) J. Biol. Inorg. Chem , vol.9 , pp. 563-576
    • Duin, E.C.1    Signer, L.2    Piskorski, R.3    Mahlert, F.4    Clay, M.D.5    Goenrich, M.6    Thauer, R.K.7    Jaun, B.8    Johnson, M.K.9
  • 11
    • 0015364291 scopus 로고
    • Nitrogenase of Klebsiella pneumoniae. Purification and properties of the component proteins
    • Eady, R. R., B. E. Smith, K. A. Cook, and J. R. Postgate. 1972. Nitrogenase of Klebsiella pneumoniae. Purification and properties of the component proteins. Biochem. J. 128:665-675.
    • (1972) Biochem. J , vol.128 , pp. 665-675
    • Eady, R.R.1    Smith, B.E.2    Cook, K.A.3    Postgate, J.R.4
  • 12
    • 0037031703 scopus 로고    scopus 로고
    • Nitrogenase MoFe-protein at 1.16 A resolution: A central ligand in the FeMo-cofactor
    • Einsle, O., F. A. Tezcan, S. L. Andrade, B. Schmid, M. Yoshida, J. B. Howard, and D. C. Rees. 2002. Nitrogenase MoFe-protein at 1.16 A resolution: a central ligand in the FeMo-cofactor. Science 297:1696-1700.
    • (2002) Science , vol.297 , pp. 1696-1700
    • Einsle, O.1    Tezcan, F.A.2    Andrade, S.L.3    Schmid, B.4    Yoshida, M.5    Howard, J.B.6    Rees, D.C.7
  • 13
    • 0033929164 scopus 로고    scopus 로고
    • Molecular evolution of nitrogen fixation: The evolutionary history of the nifD, nifK, nifE, and nifN genes
    • Fani, R., R. Gallo, and P. Lio. 2000. Molecular evolution of nitrogen fixation: the evolutionary history of the nifD, nifK, nifE, and nifN genes. J. Mol. Evol. 51:1-11.
    • (2000) J. Mol. Evol , vol.51 , pp. 1-11
    • Fani, R.1    Gallo, R.2    Lio, P.3
  • 14
    • 0032039641 scopus 로고    scopus 로고
    • Nitrogen cycle enzymology
    • Ferguson, S. J. 1998. Nitrogen cycle enzymology. Curr. Opin. Chem. Biol. 2:182-193.
    • (1998) Curr. Opin. Chem. Biol , vol.2 , pp. 182-193
    • Ferguson, S.J.1
  • 16
    • 0034604647 scopus 로고    scopus 로고
    • Reconstitution of light-independent protochlorophyllide reductase from purified BchL and BchN-BchB subunits. In vitro confirmation of nitrogenase-like features of a bacteriochlorophyll biosynthesis enzyme
    • Fujita, Y., and C. E. Bauer. 2000. Reconstitution of light-independent protochlorophyllide reductase from purified BchL and BchN-BchB subunits. In vitro confirmation of nitrogenase-like features of a bacteriochlorophyll biosynthesis enzyme. J. Biol. Chem. 275:23583-23588.
    • (2000) J. Biol. Chem , vol.275 , pp. 23583-23588
    • Fujita, Y.1    Bauer, C.E.2
  • 17
    • 0027564158 scopus 로고
    • Identification of a nifDK-like gene (ORF467) involved in the biosynthesis of chlorophyll in the cyanobacterium Plectonema boryanum
    • Fujita, Y., H. Matsumoto, Y. Takahashi, and H. Matsubara. 1993. Identification of a nifDK-like gene (ORF467) involved in the biosynthesis of chlorophyll in the cyanobacterium Plectonema boryanum. Plant Cell Physiol. 34:305-314.
    • (1993) Plant Cell Physiol , vol.34 , pp. 305-314
    • Fujita, Y.1    Matsumoto, H.2    Takahashi, Y.3    Matsubara, H.4
  • 18
    • 0026662162 scopus 로고
    • Crystallographic structure of the nitrogenase iron protein from Azotobacter vinelandii
    • Georgiadis, M. M., H. Komiya, P. Chakrabarti, D. Woo, J. J. Kornuc, and D. C. Rees. 1992. Crystallographic structure of the nitrogenase iron protein from Azotobacter vinelandii. Science 257:1653-1659.
    • (1992) Science , vol.257 , pp. 1653-1659
    • Georgiadis, M.M.1    Komiya, H.2    Chakrabarti, P.3    Woo, D.4    Kornuc, J.J.5    Rees, D.C.6
  • 19
    • 0032555248 scopus 로고    scopus 로고
    • The Azotobacter vinelandii NifEN complex contains two identical [4Fe-4S] clusters
    • Goodwin, P. J., J. N. Agar, J. T. Roll, G. P. Roberts, M. K. Johnson, and D. R. Dean. 1998. The Azotobacter vinelandii NifEN complex contains two identical [4Fe-4S] clusters. Biochemistry 37:10420-10428.
    • (1998) Biochemistry , vol.37 , pp. 10420-10428
    • Goodwin, P.J.1    Agar, J.N.2    Roll, J.T.3    Roberts, G.P.4    Johnson, M.K.5    Dean, D.R.6
  • 20
  • 21
    • 0040412793 scopus 로고
    • Nitrogenase and nitrogenase reductase associate and dissociate with each catalytic cycle
    • Hageman, R. V., and R. H. Burris. 1978. Nitrogenase and nitrogenase reductase associate and dissociate with each catalytic cycle. Proc. Natl. Acad. Sci. USA 75:2699-2702.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 2699-2702
    • Hageman, R.V.1    Burris, R.H.2
  • 22
    • 0034108232 scopus 로고    scopus 로고
    • Regulation of biological nitrogen fixation
    • Halbleib, C. M., and P. W. Ludden. 2000. Regulation of biological nitrogen fixation. J. Nutr. 130:1081-1084.
    • (2000) J. Nutr , vol.130 , pp. 1081-1084
    • Halbleib, C.M.1    Ludden, P.W.2
  • 23
    • 0034603137 scopus 로고    scopus 로고
    • Regulation of dinitrogenase reductase ADP-ribosyltransferase and dinitrogenase reductase-activating glycohydrolase by a redox-dependent conformational change of nitrogenase Fe protein
    • Halbleib, C. M., Y. Zhang, and P. W. Ludden. 2000. Regulation of dinitrogenase reductase ADP-ribosyltransferase and dinitrogenase reductase-activating glycohydrolase by a redox-dependent conformational change of nitrogenase Fe protein. J. Biol. Chem. 275:3493-3500.
    • (2000) J. Biol. Chem , vol.275 , pp. 3493-3500
    • Halbleib, C.M.1    Zhang, Y.2    Ludden, P.W.3
  • 24
    • 0001263676 scopus 로고
    • Global methanotrophy at the archaean-proterozoic transition
    • H. Baltscheffsky, S. Bengtson, J. Bergström, G. Vidal, and A. H. Knoll ed, Columbia University Press, New York, NY
    • Hayes, J. 1992. Global methanotrophy at the archaean-proterozoic transition, p. 220-236. In H. Baltscheffsky, S. Bengtson, J. Bergström, G. Vidal, and A. H. Knoll (ed.), Early life on earth, Columbia University Press, New York, NY.
    • (1992) Early life on earth , pp. 220-236
    • Hayes, J.1
  • 25
    • 0023959242 scopus 로고
    • Regulation of nitrogenase gene expression in anaerobic cultures of Anabaena variabilis
    • Helber, J. T., T. R. Johnson, L. R. Yarbrough, and R. Hirschberg. 1988. Regulation of nitrogenase gene expression in anaerobic cultures of Anabaena variabilis. J. Bacteriol. 170:552-557.
    • (1988) J. Bacteriol , vol.170 , pp. 552-557
    • Helber, J.T.1    Johnson, T.R.2    Yarbrough, L.R.3    Hirschberg, R.4
  • 26
    • 0037433228 scopus 로고    scopus 로고
    • Modeling a central ligand in the nitrogenase FeMo cofactor
    • Hinnemann, B., and J. K. Norskov. 2003. Modeling a central ligand in the nitrogenase FeMo cofactor. J. Am. Chem. Soc. 125:1466-1467.
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 1466-1467
    • Hinnemann, B.1    Norskov, J.K.2
  • 27
    • 1642351472 scopus 로고    scopus 로고
    • Chemical activity of the nitrogenase FeMo cofactor with a central nitrogen ligand: Density functional study
    • Hinnemann, B., and J. K. Norskov. 2004. Chemical activity of the nitrogenase FeMo cofactor with a central nitrogen ligand: density functional study. J. Am. Chem. Soc. 126:3920-3927.
    • (2004) J. Am. Chem. Soc , vol.126 , pp. 3920-3927
    • Hinnemann, B.1    Norskov, J.K.2
  • 28
    • 14744279761 scopus 로고    scopus 로고
    • Identification of a nitrogenase FeMo cofactor precursor on NifEN complex
    • Hu, Y., A. W. Fay, and M. W. Ribbe. 2005. Identification of a nitrogenase FeMo cofactor precursor on NifEN complex. Proc. Natl. Acad. Sci. USA 102:3236-3241.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 3236-3241
    • Hu, Y.1    Fay, A.W.2    Ribbe, M.W.3
  • 29
    • 1542276760 scopus 로고    scopus 로고
    • Density functional theory calculations and exploration of a possible mechanism of N2 reduction by nitrogenase
    • Huniar, U., R. Ahlrichs, and D. Coucouvanis. 2004. Density functional theory calculations and exploration of a possible mechanism of N2 reduction by nitrogenase. J. Am. Chem. Soc. 126:2588-2601.
    • (2004) J. Am. Chem. Soc , vol.126 , pp. 2588-2601
    • Huniar, U.1    Ahlrichs, R.2    Coucouvanis, D.3
  • 30
  • 31
    • 0026645255 scopus 로고
    • Regulation of nitrogenase-2 in Azotobacter vinelandii by ammonium, molybdenum, and vanadium
    • Jacobitz, S., and P. E. Bishop. 1992. Regulation of nitrogenase-2 in Azotobacter vinelandii by ammonium, molybdenum, and vanadium. J. Bacteriol. 174:3884-3888.
    • (1992) J. Bacteriol , vol.174 , pp. 3884-3888
    • Jacobitz, S.1    Bishop, P.E.2
  • 32
    • 33644690905 scopus 로고    scopus 로고
    • A new type of sulfite reductase, a novel coenzyme F420-dependent enzyme, from the methanarchaeon Methanocaldococcus jannaschii
    • Johnson, E. F., and B. Mukhopadhyay. 2005. A new type of sulfite reductase, a novel coenzyme F420-dependent enzyme, from the methanarchaeon Methanocaldococcus jannaschii. J. Biol. Chem. 280:38776-38786.
    • (2005) J. Biol. Chem , vol.280 , pp. 38776-38786
    • Johnson, E.F.1    Mukhopadhyay, B.2
  • 33
    • 0027222119 scopus 로고
    • X-ray crystal structure of the nitrogenase molybdenum-iron protein from Clostridium pasteurianum at 3.0-A resolution
    • Kim, J., D. Woo, and D. C. Rees. 1993. X-ray crystal structure of the nitrogenase molybdenum-iron protein from Clostridium pasteurianum at 3.0-A resolution. Biochemistry 32:7104-7115.
    • (1993) Biochemistry , vol.32 , pp. 7104-7115
    • Kim, J.1    Woo, D.2    Rees, D.C.3
  • 34
    • 26444441400 scopus 로고    scopus 로고
    • Functional NifD-K fusion protein in Azotobacter vinelandii is a homodimeric complex equivalent to the native heterotetrameric MoFe protein
    • Lahiri, S., L. Pulakat, and N. Gavini. 2005. Functional NifD-K fusion protein in Azotobacter vinelandii is a homodimeric complex equivalent to the native heterotetrameric MoFe protein. Biochem. Biophys. Res. Commun. 337:677-684.
    • (2005) Biochem. Biophys. Res. Commun , vol.337 , pp. 677-684
    • Lahiri, S.1    Pulakat, L.2    Gavini, N.3
  • 35
    • 0020060467 scopus 로고
    • A rapid, simple and reliable test for the routine identification of urease producing gram-negative bacteria
    • Lee, J. S., and E. H. Sng. 1982. A rapid, simple and reliable test for the routine identification of urease producing gram-negative bacteria. Ann. Acad. Med. Singap. 11:94-97.
    • (1982) Ann. Acad. Med. Singap , vol.11 , pp. 94-97
    • Lee, J.S.1    Sng, E.H.2
  • 36
    • 0037668080 scopus 로고    scopus 로고
    • Structural, spectroscopic, and redox consequences of a central ligand in the FeMoco of nitrogenase: A density functional theoretical study
    • Lovell, T., T. Liu, D. A. Case, and L. Noodleman. 2003. Structural, spectroscopic, and redox consequences of a central ligand in the FeMoco of nitrogenase: a density functional theoretical study. J. Am. Chem. Soc. 125:8377-8383.
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 8377-8383
    • Lovell, T.1    Liu, T.2    Case, D.A.3    Noodleman, L.4
  • 37
    • 0024973013 scopus 로고
    • Kinetics and mechanism of the reaction of cyanide with molybdenum nitrogenase from Azotobacter vinelandii
    • Lowe, D. J., K. Fisher, R. N. Thorneley, S. A. Vaughn, and B. K. Burgess. 1989. Kinetics and mechanism of the reaction of cyanide with molybdenum nitrogenase from Azotobacter vinelandii. Biochemistry 28:8460-8466.
    • (1989) Biochemistry , vol.28 , pp. 8460-8466
    • Lowe, D.J.1    Fisher, K.2    Thorneley, R.N.3    Vaughn, S.A.4    Burgess, B.K.5
  • 38
    • 0024832910 scopus 로고
    • Regulation of nitrogenase activity by reversible ADP-ribosylation
    • B. Horecker, E. Stadtman, P. Boon Chock, and A. Levitzki, ed, Academic Press, Inc, Orlando, FL
    • Ludden, P. W., and G. P. Roberts. 1989. Regulation of nitrogenase activity by reversible ADP-ribosylation, p. 23-55. In B. Horecker, E. Stadtman, P. Boon Chock, and A. Levitzki, (ed.), Current topics in cellular regulation, vol. 30. Academic Press, Inc., Orlando, FL.
    • (1989) Current topics in cellular regulation , vol.30 , pp. 23-55
    • Ludden, P.W.1    Roberts, G.P.2
  • 40
    • 0032731169 scopus 로고    scopus 로고
    • Reactor-scale cultivation of the hyperthermophilic methanarchaeon Methanococcus jannaschii to high cell densities
    • Mukhopadhyay, B., E. F. Johnson, and R. S. Wolfe. 1999. Reactor-scale cultivation of the hyperthermophilic methanarchaeon Methanococcus jannaschii to high cell densities. Appl. Environ. Microbiol. 65:5059-5065.
    • (1999) Appl. Environ. Microbiol , vol.65 , pp. 5059-5065
    • Mukhopadhyay, B.1    Johnson, E.F.2    Wolfe, R.S.3
  • 41
    • 0034633401 scopus 로고    scopus 로고
    • A novel pH2 control on the expression of flagella in the hyperthermophilic strictly hydrogenotrophic methanarchaeaon Methanococcus jannaschii
    • Mukhopadhyay, B., E. F. Johnson, and R. S. Wolfe. 2000. A novel pH2 control on the expression of flagella in the hyperthermophilic strictly hydrogenotrophic methanarchaeaon Methanococcus jannaschii. Proc. Natl. Acad. Sci. USA 97:11522-11527.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 11522-11527
    • Mukhopadhyay, B.1    Johnson, E.F.2    Wolfe, R.S.3
  • 43
    • 0017795338 scopus 로고
    • The chemistry and biochemistry of nitrogen
    • Pratt, J. M. 1978. The chemistry and biochemistry of nitrogen. Horiz. Biochem. Biophys. 5:119-160.
    • (1978) Horiz. Biochem. Biophys , vol.5 , pp. 119-160
    • Pratt, J.M.1
  • 45
    • 0023281127 scopus 로고
    • Use of subunits of the methylreductase protein for taxonomy of methanogenic bacteria
    • Rouviere, P. E., and R. S. Wolfe. 1987. Use of subunits of the methylreductase protein for taxonomy of methanogenic bacteria. Arch. Microbiol. 148:253-259.
    • (1987) Arch. Microbiol , vol.148 , pp. 253-259
    • Rouviere, P.E.1    Wolfe, R.S.2
  • 46
    • 0021109062 scopus 로고
    • Nitrogenase reactivity: Methyl isocyanide as substrate and inhibitor
    • Rubinson, J. F., J. L. Corbin, and B. K. Burgess. 1983. Nitrogenase reactivity: methyl isocyanide as substrate and inhibitor. Biochemistry 22:6260-6268.
    • (1983) Biochemistry , vol.22 , pp. 6260-6268
    • Rubinson, J.F.1    Corbin, J.L.2    Burgess, B.K.3
  • 47
    • 0034431669 scopus 로고    scopus 로고
    • Geology and geochemistry of paleosols developed on the Hekpoort Basalt, Pretoria Group
    • Rye, R., and H. D. Holland. 2000. Geology and geochemistry of paleosols developed on the Hekpoort Basalt, Pretoria Group, South Africa. Geology 28:483-486.
    • (2000) South Africa. Geology , vol.28 , pp. 483-486
    • Rye, R.1    Holland, H.D.2
  • 49
    • 0030925197 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray diffraction studies of methyl-coenzyme M reductase from Methanobacterium thermoautotrophicum
    • Shima, S., M. Goubeaud, D. Vinzenz, R. K. Thauer, and U. Ermler. 1997. Crystallization and preliminary X-ray diffraction studies of methyl-coenzyme M reductase from Methanobacterium thermoautotrophicum. J. Biochem. (Tokyo) 121:829-830.
    • (1997) J. Biochem. (Tokyo) , vol.121 , pp. 829-830
    • Shima, S.1    Goubeaud, M.2    Vinzenz, D.3    Thauer, R.K.4    Ermler, U.5
  • 50
    • 0028726343 scopus 로고
    • Biosynthesis of coenzyme F430, a nickel porphinoid involved in methanogenesis
    • Thauer, R. K., and L. G. Bonacker. 1994. Biosynthesis of coenzyme F430, a nickel porphinoid involved in methanogenesis. Ciba Found. Symp. 180:210-222.
    • (1994) Ciba Found. Symp , vol.180 , pp. 210-222
    • Thauer, R.K.1    Bonacker, L.G.2
  • 51
    • 0001574458 scopus 로고
    • Detection of EPR signals assigned to the 1-equiv-oxidized P-clusters of the nitrogenase MoFe-protein from Azotobacter vinelandii
    • Tittsworth, R. C., and B. J. Hales. 1993. Detection of EPR signals assigned to the 1-equiv-oxidized P-clusters of the nitrogenase MoFe-protein from Azotobacter vinelandii. J. Am. Chem. Soc. 115:9763-9767.
    • (1993) J. Am. Chem. Soc , vol.115 , pp. 9763-9767
    • Tittsworth, R.C.1    Hales, B.J.2
  • 52
    • 0016221002 scopus 로고
    • Some properties of the nitrogenase proteins from Clostridium pasteurianum
    • Tso, M. Y. 1974. Some properties of the nitrogenase proteins from Clostridium pasteurianum. Arch. Microbiol. 99:71-80.
    • (1974) Arch. Microbiol , vol.99 , pp. 71-80
    • Tso, M.Y.1
  • 53
    • 0034096321 scopus 로고    scopus 로고
    • Regulation of nitrogenase activity in Rhodobacter capsulatus under dark microxic conditions
    • Yakunin, A. F., and P. C. Hallenbeck. 2000. Regulation of nitrogenase activity in Rhodobacter capsulatus under dark microxic conditions. Arch. Microbiol. 173:366-372.
    • (2000) Arch. Microbiol , vol.173 , pp. 366-372
    • Yakunin, A.F.1    Hallenbeck, P.C.2
  • 54
    • 0020490898 scopus 로고
    • Iron-molybdenum cofactor from nitrogenase. Modified extraction methods as probes for composition
    • Yang, S., W.-H. Pan, G. D. Friesen, B. K. Burgess, J. L. Corbin, E. I. Stiefel, and W. E. Newton. 1982. Iron-molybdenum cofactor from nitrogenase. Modified extraction methods as probes for composition. J. Biol. Chem. 257:8042-8048.
    • (1982) J. Biol. Chem , vol.257 , pp. 8042-8048
    • Yang, S.1    Pan, W.-H.2    Friesen, G.D.3    Burgess, B.K.4    Corbin, J.L.5    Stiefel, E.I.6    Newton, W.E.7
  • 55
    • 0347089202 scopus 로고    scopus 로고
    • Birth of the domains Bacteria, Archaea and Eucarya and of major taxa within them: A hypothesis
    • Zorzopulos, J. 2003. Birth of the domains Bacteria, Archaea and Eucarya and of major taxa within them: a hypothesis. Rev. Argent. Microbiol. 35:175-182.
    • (2003) Rev. Argent. Microbiol , vol.35 , pp. 175-182
    • Zorzopulos, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.