메뉴 건너뛰기




Volumn 193, Issue 5, 2011, Pages 1201-1211

Identification of missing genes and enzymes for autotrophic carbon fixation in Crenarchaeota

Author keywords

[No Author keywords available]

Indexed keywords

3 HYDROXYACYL COENZYME A DEHYDROGENASE; ACETYL COENZYME A; ACETYL COENZYME A ACYLTRANSFERASE; CARBON; DICARBOXYLIC ACID; SUCCINYL COENZYME A;

EID: 79951661281     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.01156-10     Document Type: Article
Times cited : (47)

References (56)
  • 1
    • 33845383207 scopus 로고    scopus 로고
    • Malonyl-coenzyme A reductase in the modified 3-hydroxypropionate cycle for autotrophic carbon fixation in archaeal Metallosphaera and Sulfolobus spp
    • DOI 10.1128/JB.00987-06
    • Alber, B., et al. 2006. Malonyl-coenzyme A reductase in the modified 3-hydroxypropionate cycle for autotrophic carbon fixation in archaeal Metallosphaera and Sulfolobus spp. J. Bacteriol. 188:8551-8559. (Pubitemid 44894056)
    • (2006) Journal of Bacteriology , vol.188 , Issue.24 , pp. 8551-8559
    • Alber, B.1    Olinger, M.2    Rieder, A.3    Kockelkorn, D.4    Jobst, B.5    Hugler, M.6    Fuchs, G.7
  • 4
    • 75749095204 scopus 로고    scopus 로고
    • Physiological versatility of the extremely thermoacidophilic archaeon Metallosphaera sedula supported by transcriptomic analysis of heterotrophic, autotrophic, and mixotrophic growth
    • Auernik, K. S., and R. M. Kelly. 2010. Physiological versatility of the extremely thermoacidophilic archaeon Metallosphaera sedula supported by transcriptomic analysis of heterotrophic, autotrophic, and mixotrophic growth. Appl. Environ. Microbiol. 76:931-935.
    • (2010) Appl. Environ. Microbiol. , vol.76 , pp. 931-935
    • Auernik, K.S.1    Kelly, R.M.2
  • 5
    • 38949170756 scopus 로고    scopus 로고
    • The genome sequence of the metal-mobilizing, extremely thermoacidophilic archaeon Metallosphaera sedula provides insights into bioleaching-associated metabolism
    • Auernik, K. S., Y. Maezato, P. H. Blum, and R. M. Kelly. 2008. The genome sequence of the metal-mobilizing, extremely thermoacidophilic archaeon Metallosphaera sedula provides insights into bioleaching-associated metabolism. Appl. Environ. Microbiol. 74:682-692.
    • (2008) Appl. Environ. Microbiol. , vol.74 , pp. 682-692
    • Auernik, K.S.1    Maezato, Y.2    Blum, P.H.3    Kelly, R.M.4
  • 7
    • 0027303801 scopus 로고
    • Enzymes of the reductive citric acid cycle in the autotrophic eubacterium Aquifex pyrophilus and in the archaebacterium Thermoproteus neutrophilus
    • Beh, M., G. Strauss, R. Huber, K. O. Stetter, and G. Fuchs. 1993. Enzymes of the reductive citric acid cycle in the autotrophic eubacterium Aquifex pyrophilus and in the archebacterium Thermoproteus neutrophilus. Arch. Microbiol. 160:306-311. (Pubitemid 23277991)
    • (1993) Archives of Microbiology , vol.160 , Issue.4 , pp. 306-311
    • Beh, M.1    Strauss, G.2    Huber, R.3    Stetter, K.-O.4    Fuchs, G.5
  • 8
    • 37249052742 scopus 로고    scopus 로고
    • A 3-hydroxypropionate/4-hydroxybutyrate autotrophic carbon dioxide assimilation pathway in Archaea
    • Berg, I. A., D. Kockelkorn, W. Buckel, and G. Fuchs. 2007. A 3-hydroxypropionate/4-hydroxybutyrate autotrophic carbon dioxide assimilation pathway in Archaea. Science 318:1782-1786.
    • (2007) Science , vol.318 , pp. 1782-1786
    • Berg, I.A.1    Kockelkorn, D.2    Buckel, W.3    Fuchs, G.4
  • 9
    • 77952888917 scopus 로고    scopus 로고
    • Autotrophic carbon fixation in Archaea
    • Berg, I. A., et al. 2010. Autotrophic carbon fixation in Archaea. Nat. Rev. Microbiol. 8:447-460.
    • (2010) Nat. Rev. Microbiol. , vol.8 , pp. 447-460
    • Berg, I.A.1
  • 11
    • 0016723542 scopus 로고
    • Neue Werte für die molaren Extinktions-Koeffizienten von NADH und NADPH zum Gebrauch im Routine-Laboratorium
    • Bergmeyer, H. U. 1975. Neue Werte für die molaren Extinktions-Koeffizienten von NADH und NADPH zum Gebrauch im Routine-Laboratorium. Z. Klin. Chem. Klin. Biochem. 13:507-508.
    • (1975) Z. Klin. Chem. Klin. Biochem. , vol.13 , pp. 507-508
    • Bergmeyer, H.U.1
  • 12
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. 1976. A rapid and sensitive method for the quantification 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.1
  • 13
    • 11844296747 scopus 로고    scopus 로고
    • A novel octameric AMP-forming acetyl-CoA synthetase from the hyperthermophilic crenarchaeon Pyrobaculum aerophilum
    • DOI 10.1016/j.febslet.2004.12.016, PII S0014579304015467
    • Bräsen, C., C. Urbanke, and P. Schönheit. 2005. A novel octameric AMP-forming acetyl-CoA synthetase from the hyperthermophilic crenarchaeon Pyrobaculum aerophilum. FEBS Lett. 579:477-482. (Pubitemid 40092430)
    • (2005) FEBS Letters , vol.579 , Issue.2 , pp. 477-482
    • Brasen, C.1    Urbanke, C.2    Schonheit, P.3
  • 15
    • 0000146513 scopus 로고    scopus 로고
    • Two-carbon compounds and fatty acids as carbon sources
    • F. C. Neidhardt et al. (ed.), 2nd ed., ASM Press, Washington, DC
    • Clark, D. P., and J. E. Cronan, Jr. 1996. Two-carbon compounds and fatty acids as carbon sources, p. 343-357. In F. C. Neidhardt et al. (ed.), Escherichia coli and Salmonella, 2nd ed., vol. 1. ASM Press, Washington, DC.
    • (1996) Escherichia coli and Salmonella , vol.1 , pp. 343-357
    • Clark, D.P.1    Cronan Jr., J.E.2
  • 16
    • 73649144200 scopus 로고    scopus 로고
    • IcmF is a fusion between the radical B12 enzyme isobutyryl-CoA mutase and its G-protein chaperone
    • Cracan, V., D. Padovani, and R. Banerjee. 2010. IcmF is a fusion between the radical B12 enzyme isobutyryl-CoA mutase and its G-protein chaperone. J. Biol. Chem. 285:655-666.
    • (2010) J. Biol. Chem. , vol.285 , pp. 655-666
    • Cracan, V.1    Padovani, D.2    Banerjee, R.3
  • 17
    • 77952222270 scopus 로고    scopus 로고
    • Reversible N epsilon-lysine acetylation regulates the activity of acyl-CoA synthetases involved in anaerobic benzoate catabolism in Rhodopseudomonas palustris
    • Crosby, H. A., E. K. Heiniger, C. S. Harwood, and J. C. Escalante-Semerena. 2010. Reversible N epsilon-lysine acetylation regulates the activity of acyl-CoA synthetases involved in anaerobic benzoate catabolism in Rhodopseudomonas palustris. Mol. Microbiol. 76:874-888.
    • (2010) Mol. Microbiol. , vol.76 , pp. 874-888
    • Crosby, H.A.1    Heiniger, E.K.2    Harwood, C.S.3    Escalante-Semerena, J.C.4
  • 18
    • 34547542453 scopus 로고    scopus 로고
    • 2-units involving crotonyl-CoA carboxylase/reductase: The ethylmalonyl-CoA pathway
    • 2-units involving crotonyl-CoA carboxylase/reductase: the ethylmalonyl-CoA pathway. Proc. Natl. Acad. Sci. U. S. A. 104:10631-10636.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 10631-10636
    • Erb, T.J.1
  • 19
    • 79951642402 scopus 로고    scopus 로고
    • Labeling and enzyme studies of the central carbon metabolism in Metallosphaera sedula
    • Estelmann, S., et al. 2011. Labeling and enzyme studies of the central carbon metabolism in Metallosphaera sedula. J. Bacteriol. 193:1191-1200.
    • (2011) J. Bacteriol. , vol.193 , pp. 1191-1200
    • Estelmann, S.1
  • 20
    • 34248178641 scopus 로고    scopus 로고
    • New processes and players in the nitrogen cycle: The microbial ecology of anaerobic and archaeal ammonia oxidation
    • Francis, C. A., J. M. Beman, and M. M. Kuypers. 2007. New processes and players in the nitrogen cycle: the microbial ecology of anaerobic and archaeal ammonia oxidation. ISME J. 1:19-27.
    • (2007) ISME J. , vol.1 , pp. 19-27
    • Francis, C.A.1    Beman, J.M.2    Kuypers, M.M.3
  • 21
    • 0033849869 scopus 로고    scopus 로고
    • Fermentation of 4-aminobutyrate by Clostridium aminobutyricum: Cloning of two genes involved in the formation and dehydration of 4-hydroxybutyryl-CoA
    • Gerhardt, A., I. Cinkaya, D. Linder, G. Huisman, and W. Buckel. 2000. Fermentation of 4-aminobutyrate by Clostridium aminobutyricum: cloning of two genes involved in the formation and dehydration of 4-hydroxybutyryl-CoA. Arch. Microbiol. 174:189-199.
    • (2000) Arch. Microbiol. , vol.174 , pp. 189-199
    • Gerhardt, A.1    Cinkaya, I.2    Linder, D.3    Huisman, G.4    Buckel, W.5
  • 23
    • 33646260901 scopus 로고    scopus 로고
    • Pathways of carbon assimilation and ammonia oxidation suggested by environmental genomic analyses of marine crenarchaeota
    • Hallam, S. J., et al. 2006. Pathways of carbon assimilation and ammonia oxidation suggested by environmental genomic analyses of marine crenarchaeota. PloS Biol. 4:e95.
    • (2006) PloS Biol. , vol.4
    • Hallam, S.J.1
  • 26
    • 0001960079 scopus 로고
    • Metallosphaera sedula gen. and sp. nov. represents a new genus of aerobic, metal-mobilizing, thermoacidophilic archaebacteria
    • Huber, G., C. Spinnler, A. Gambacorta, and K. O. Stetter. 1989. Metallosphaera sedula gen. and sp. nov. represents a new genus of aerobic, metal-mobilizing, thermoacidophilic archaebacteria. Syst. Appl. Microbiol. 12:38-47.
    • (1989) Syst. Appl. Microbiol. , vol.12 , pp. 38-47
    • Huber, G.1    Spinnler, C.2    Gambacorta, A.3    Stetter, K.O.4
  • 27
    • 0012947189 scopus 로고    scopus 로고
    • Sulfolobales
    • D. R. Boone and R. W. Castenholz (ed.), 2nd ed., Springer, New York, NY
    • Huber, H., K. O. Stetter, and A. L. Reysenbach. 2001. Sulfolobales, p. 198-210. In D. R. Boone and R. W. Castenholz (ed.), Bergey's manual of systematic bacteriology, 2nd ed., vol. 1. Springer, New York, NY.
    • (2001) Bergey's Manual of Systematic Bacteriology , vol.1 , pp. 198-210
    • Huber, H.1    Stetter, K.O.2    Reysenbach, A.L.3
  • 30
    • 0037294946 scopus 로고    scopus 로고
    • Characterization of acetyl-CoA/propionyl-CoA carboxylase in Metallosphaera sedula. Carboxylating enzyme in the 3-hydroxypropionate cycle for autotrophic carbon fixation
    • Hügler, M., R. S. Krieger, M. Jahn, and G. Fuchs. 2003. Characterization of acetyl-CoA/propionyl-CoA carboxylase in Metallosphaera sedula. Carboxylating enzyme in the 3-hydroxypropionate cycle for autotrophic carbon fixation. Eur. J. Biochem. 270:736-744.
    • (2003) Eur. J. Biochem. , vol.270 , pp. 736-744
    • Hügler, M.1    Krieger, R.S.2    Jahn, M.3    Fuchs, G.4
  • 31
    • 34249798717 scopus 로고    scopus 로고
    • 2 fixation pathway of the archaeon Ignicoccus hospitalis: Comprehensive analysis of the central carbon metabolism
    • 2 fixation pathway of the archaeon Ignicoccus hospitalis: comprehensive analysis of the central carbon metabolism. J. Bacteriol. 189:4108-4119.
    • (2007) J. Bacteriol. , vol.189 , pp. 4108-4119
    • Jahn, U.1    Huber, H.2    Eisenreich, W.3    Hügler, M.4    Fuchs, G.5
  • 32
    • 34547429681 scopus 로고    scopus 로고
    • Metabolism of inorganic sulfur compounds in Archaea
    • R. A. Garrett and H. P. Klenk (ed.), Blackwell Publishing, Malden, MA
    • Kletzin, A. 2007. Metabolism of inorganic sulfur compounds in Archaea, p. 261-276. In R. A. Garrett and H. P. Klenk (ed.), Archaea: evolution, physiology, and molecular biology. Blackwell Publishing, Malden, MA.
    • (2007) Archaea: Evolution, Physiology, and Molecular Biology , pp. 261-276
    • Kletzin, A.1
  • 33
    • 70350459999 scopus 로고    scopus 로고
    • Malonic semialdehyde reductase, succinic semialdehyde reductase, and succinyl-coenzyme A reductase from Metallosphaera sedula: Enzymes of the autotrophic 3-hydroxypropionate/4-hydroxybutyrate cycle in Sulfolobales
    • Kockelkorn, D., and G. Fuchs. 2009. Malonic semialdehyde reductase, succinic semialdehyde reductase, and succinyl-coenzyme A reductase from Metallosphaera sedula: enzymes of the autotrophic 3-hydroxypropionate/4- hydroxybutyrate cycle in Sulfolobales. J. Bacteriol. 191:6352-6362.
    • (2009) J. Bacteriol. , vol.191 , pp. 6352-6362
    • Kockelkorn, D.1    Fuchs, G.2
  • 35
    • 77955902997 scopus 로고    scopus 로고
    • Genomic signatures of fifth autotrophic carbon assimilation pathway in bathypelagic Crenarchaeota
    • La Cono, V., et al. 2010. Genomic signatures of fifth autotrophic carbon assimilation pathway in bathypelagic Crenarchaeota. Microb. Biotechnol. 3:595-606.
    • (2010) Microb. Biotechnol. , vol.3 , pp. 595-606
    • La Cono, V.1
  • 36
    • 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
  • 37
    • 8144230590 scopus 로고    scopus 로고
    • Crystal structure of 4-hydroxybutyryl-CoA dehydratase: Radical catalysis involving a [4Fe-4S] cluster and flavin
    • Martins, B. M., H. Dobbek, I. Cinkaya, W. Buckel, and A. Messerschmidt. 2004. Crystal structure of 4-hydroxybutyryl-CoA dehydratase: radical catalysis involving a [4Fe-4S] cluster and flavin. Proc. Natl. Acad. Sci. U. S. A. 101:15645-15649.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 15645-15649
    • Martins, B.M.1    Dobbek, H.2    Cinkaya, I.3    Buckel, W.4    Messerschmidt, A.5
  • 38
    • 55749111081 scopus 로고    scopus 로고
    • A soluble NADH-dependent fumarate reductase in the reductive tricarboxylic acid cycle of Hydrogenobacter thermophilus TK-6
    • Miura, A., M. Kameya, H. Arai, M. Ishii, and Y. Igarashi. 2008. A soluble NADH-dependent fumarate reductase in the reductive tricarboxylic acid cycle of Hydrogenobacter thermophilus TK-6. J. Bacteriol. 190:7170-7177.
    • (2008) J. Bacteriol. , vol.190 , pp. 7170-7177
    • Miura, A.1    Kameya, M.2    Arai, H.3    Ishii, M.4    Igarashi, Y.5
  • 39
    • 34248174940 scopus 로고    scopus 로고
    • Ignicoccus hospitalis sp. nov., the host of "Nanoarchaeum equitans"
    • Paper, W., et al. 2007. Ignicoccus hospitalis sp. nov., the host of "Nanoarchaeum equitans". Int. J. Syst. Evol. Microbiol. 57:803-808.
    • (2007) Int. J. Syst. Evol. Microbiol. , vol.57 , pp. 803-808
    • Paper, W.1
  • 40
    • 15844365305 scopus 로고    scopus 로고
    • A psychrophilic crenarchaeon inhabits a marine sponge: Cenarchaeum symbiosum gen. nov., sp. nov.
    • Preston, C. M., K. Y. Wu, T. F. Molinski, and E. F. DeLong. 1996. A psychrophilic crenarchaeon inhabits a marine sponge: Cenarchaeum symbiosum gen. nov., sp. nov. Proc. Natl. Acad. Sci. U. S. A. 93:6241-6246.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 6241-6246
    • Preston, C.M.1    Wu, K.Y.2    Molinski, T.F.3    DeLong, E.F.4
  • 41
    • 67649413349 scopus 로고    scopus 로고
    • Autotrophic carbon dioxide assimilation in Thermoproteales revisited
    • Ramos-Vera, W. H., I. A. Berg, and G. Fuchs. 2009. Autotrophic carbon dioxide assimilation in Thermoproteales revisited. J. Bacteriol. 191:4286-4297.
    • (2009) J. Bacteriol. , vol.191 , pp. 4286-4297
    • Ramos-Vera, W.H.1    Berg, I.A.2    Fuchs, G.3
  • 43
    • 0022895194 scopus 로고
    • Carbon assimilation by the autotrophic thermophilic archaebacterium Thermoproteus neutrophilus
    • DOI 10.1007/BF00403234
    • Schäfer, S., C. Barkowski, and G. Fuchs. 1986. Carbon assimilation by the autotrophic thermophilic archaebacterium Thermoproteus neutrophilus. Arch. Microbiol. 146:301-308. (Pubitemid 17003215)
    • (1986) Archives of Microbiology , vol.146 , Issue.3 , pp. 301-308
    • Schafer, S.1    Barkowski, C.2    Fuchs, G.3
  • 47
    • 0025938528 scopus 로고
    • Stygiolobus azoricus gen. nov., sp. nov. represents a novel genus of anaerobic, extremely thermoacidophilic archaebacteria of the order Sulfolobales
    • Segerer, A. H., A. Trincone, M. Gahrtz, and K. O. Stetter. 1991. Stygiolobus azoricus gen. nov., sp. nov. represents a novel genus of anaerobic, extremely thermoacidophilic archaebacteria of the order Sulfolobales. Int. J. Syst. Bacteriol. 41:495-501.
    • (1991) Int. J. Syst. Bacteriol. , vol.41 , pp. 495-501
    • Segerer, A.H.1    Trincone, A.2    Gahrtz, M.3    Stetter, K.O.4
  • 48
    • 0000060558 scopus 로고
    • The preparation of S-succinyl coenzyme-A
    • Simon, E. J., and D. Shemin. 1953. The preparation of S-succinyl coenzyme-A. J. Am. Chem. Soc. 75:2520-2520.
    • (1953) J. Am. Chem. Soc. , vol.75 , pp. 2520-2520
    • Simon, E.J.1    Shemin, D.2
  • 49
    • 0027400198 scopus 로고
    • Purification and characterization of a coenzyme-A-dependent succinate-semialdehyde dehydrogenase from Clostridium kluyveri
    • Söhling, B., and G. Gottschalk. 1993. Purification and characterization of a coenzyme-A-dependent succinate-semialdehyde dehydrogenase from Clostridium kluyveri. Eur. J. Biochem. 212:121-127. (Pubitemid 23064608)
    • (1993) European Journal of Biochemistry , vol.212 , Issue.1 , pp. 121-127
    • Sohling, B.1    Gottschalk, G.2
  • 50
    • 0001308240 scopus 로고
    • Preparation and assay of acyl coenzyme A and other thiol esters; use of hydroxylamine
    • Stadtman, E. R. 1957. Preparation and assay of acyl coenzyme A and other thiol esters; use of hydroxylamine. Methods Enzymol. 3:931-941.
    • (1957) Methods Enzymol. , vol.3 , pp. 931-941
    • Stadtman, E.R.1
  • 51
    • 0026611716 scopus 로고
    • 2 fixation pathways in the sulphur-reducing archaebacterium Thermoproteus neutrophilus and in the phototrophic eubacterium Chloroflexus aurantiacus
    • 2 fixation pathways in the sulphur-reducing archaebacterium Thermoproteus neutrophilus and in the phototrophic eubacterium Chloroflexus aurantiacus. Eur. J. Biochem. 205:853-866.
    • (1992) Eur. J. Biochem. , vol.205 , pp. 853-866
    • Strauss, G.1    Eisenreich, W.2    Bacher, A.3    Fuchs, G.4
  • 52
    • 0021919826 scopus 로고
    • A bacteriophage-T7 RNA-polymerase promoter system for controlled exclusive expression of specific genes
    • Tabor, S., and C. C. Richardson. 1985. A bacteriophage-T7 RNA-polymerase promoter system for controlled exclusive expression of specific genes. Proc. Natl. Acad. Sci. U. S. A. 82:1074-1078.
    • (1985) Proc. Natl. Acad. Sci. U. S. A. , vol.82 , pp. 1074-1078
    • Tabor, S.1    Richardson, C.C.2
  • 53
    • 67650302869 scopus 로고    scopus 로고
    • 3-Hydroxypropionyl-coenzyme A dehydratase and acryloyl-coenzyme A reductase, enzymes of the autotrophic 3-hydroxypropionate/4-hydroxybutyrate cycle in sulfolobales
    • Teufel, R., J. W. Kung, D. Kockelkorn, B. E. Alber, and G. Fuchs. 2009. 3-Hydroxypropionyl-coenzyme A dehydratase and acryloyl-coenzyme A reductase, enzymes of the autotrophic 3-hydroxypropionate/4-hydroxybutyrate cycle in sulfolobales. J. Bacteriol. 191:4572-4581.
    • (2009) J. Bacteriol. , vol.191 , pp. 4572-4581
    • Teufel, R.1    Kung, J.W.2    Kockelkorn, D.3    Alber, B.E.4    Fuchs, G.5
  • 54
    • 0017343370 scopus 로고
    • Energy conservation in chemotrophic anaerobic bacteria
    • Thauer, R. K., K. Jungermann, and K. Decker. 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
  • 55
    • 0027968068 scopus 로고
    • Clustal W-improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., D. G. Higgins, and T. J. Gibson. 1994. Clustal W-improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-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
  • 56
    • 77952739182 scopus 로고    scopus 로고
    • Nitrosopumilus maritimus genome reveals unique mechanisms for nitrification and autotrophy in globally distributed marine crenarchaea
    • Walker, C. B., et al. 2010. Nitrosopumilus maritimus genome reveals unique mechanisms for nitrification and autotrophy in globally distributed marine crenarchaea. Proc. Natl. Acad. Sci. U. S. A. 107:8818-8823.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 8818-8823
    • Walker, C.B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.