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Volumn 478, Issue 7369, 2011, Pages 412-416

Evolution of a new enzyme for carbon disulphide conversion by an acidothermophilic archaeon

Author keywords

[No Author keywords available]

Indexed keywords

CARBON DISULFIDE; CARBONATE DEHYDRATASE; HYDROGEN SULFIDE; HYDROLASE;

EID: 80055000559     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature10464     Document Type: Article
Times cited : (86)

References (51)
  • 1
    • 0026268860 scopus 로고
    • Isotopic study of the origin of sulfur and carbon in solfatara fumaroles, Campi Flegrei Caldera
    • Allard, P.,Maiorani, A., Tedesco, D., Cortecci, G.&Turi, B. Isotopic study of the origin of sulfur and carbon in solfatara fumaroles, Campi Flegrei Caldera. J. Volcanol. Geotherm. Res. 48, 139-159 (1991).
    • (1991) J. Volcanol. Geotherm. Res. , vol.48 , pp. 139-159
    • Allard, P.1    Maiorani, A.2    Tedesco, D.3    Cortecci, G.4    Turi, B.5
  • 4
    • 0029873327 scopus 로고    scopus 로고
    • 16S rDNA-based phylogeny of the archaeal order Sulfolobales and reclassification of Desulfurolobus ambivalens as Acidianus ambivalens comb nov
    • Fuchs, T., Huber, H., Burggraf, S. & Stetter, K. O. 16S rDNA-based phylogeny of the archaeal order Sulfolobales and reclassification of Desulfurolobus ambivalens as Acidianus ambivalens comb nov. Syst. Appl. Microbiol. 19, 56-60 (1996).
    • (1996) Syst. Appl. Microbiol. , vol.19 , pp. 56-60
    • Fuchs, T.1    Huber, H.2    Burggraf, S.3    Stetter, K.O.4
  • 5
    • 0034672173 scopus 로고    scopus 로고
    • Cloning and heterologous expression of a sulfur oxygenase/reductase gene fromthe thermoacidophilic archaeon Acidianus sp. S5 in Escherichia coli
    • He, Z., Li, Y., Zhou, P. & Liu, S.-J. Cloning and heterologous expression of a sulfur oxygenase/reductase gene fromthe thermoacidophilic archaeon Acidianus sp. S5 in Escherichia coli. FEMS Microbiol. Lett. 193, 217-221 (2000).
    • (2000) FEMS Microbiol. Lett. , vol.193 , pp. 217-221
    • He, Z.1    Li, Y.2    Zhou, P.3    Liu, S.-J.4
  • 6
    • 33846845191 scopus 로고    scopus 로고
    • Isolation of a carbon disulfide utilizing Thiomonas sp. and its application in a biotrickling filter
    • DOI 10.1007/s00253-006-0663-4
    • Pol, A., van der Drift, C. & Op den Camp, H. J. M. Isolation of a carbon disulfide utilizing Thiomonas sp and its application in a biotrickling filter. Appl. Microbiol. Biotechnol. 74, 439-446 (2007). (Pubitemid 46204520)
    • (2007) Applied Microbiology and Biotechnology , vol.74 , Issue.2 , pp. 439-446
    • Pol, A.1    Van Der Drift, C.2    Op Den Camp, H.J.M.3
  • 8
    • 0035952128 scopus 로고    scopus 로고
    • 2 fixation by carbonic anhydrase model systems - A new substrate in the catalytic cycle
    • DOI 10.1021/ic001149e
    • Sinnecker, S., Brauer, M., Koch, W.& Anders, E. CS2 fixation by carbonic anhydrase model systems-a new substrate in the catalytic cycle. Inorg. Chem. 40, 1006-1013 (2001). (Pubitemid 32289204)
    • (2001) Inorganic Chemistry , vol.40 , Issue.5 , pp. 1006-1013
    • Sinnecker, S.1    Brauer, M.2    Koch, W.3    Anders, E.4
  • 9
    • 34447641657 scopus 로고    scopus 로고
    • The missing link in COS metabolism: A model study on the reactivation of carbonic anhydrase from its hydrosulfide analogue
    • DOI 10.1002/cbic.200600436
    • Notni, J., Schenk, S., Protoschill-Krebs, G., Kesselmeier, J. & Anders, E. The missing link in COS metabolism: a model study on the reactivation of carbonic anhydrase from its hydrosulfide analogue. ChemBioChem 8, 530-536 (2007). (Pubitemid 47183649)
    • (2007) ChemBioChem , vol.8 , Issue.5 , pp. 530-536
    • Notni, J.1    Schenk, S.2    Protoschill-Krebs, G.3    Kesselmeier, J.4    Anders, E.5
  • 10
    • 3042745176 scopus 로고    scopus 로고
    • Howdoes the exchange ofone oxygenatom with sulfur affect the catalytic cycle of carbonic anhydrase?
    • Schenk, S., Kesselmeier, J.&Anders, E.Howdoes the exchange ofone oxygenatom with sulfur affect the catalytic cycle of carbonic anhydrase? Chem. Eur. J. 10, 3091-3105 (2004).
    • (2004) Chem. Eur. J. , vol.10 , pp. 3091-3105
    • Schenk, S.1    Kesselmeier, J.2    Anders, E.3
  • 11
    • 0029659709 scopus 로고    scopus 로고
    • Consumption of carbonyl sulphide (COS) by higher plant carbonic anhydrase (CA)
    • Protoschill-Krebs, G., Wilhelm, C. & Kesselmeier, J. Consumption of carbonyl sulphide (COS) by higher plant carbonic anhydrase (CA). Atmos. Environ. 30, 3151-3156 (1996).
    • (1996) Atmos. Environ. , vol.30 , pp. 3151-3156
    • Protoschill-Krebs, G.1    Wilhelm, C.2    Kesselmeier, J.3
  • 12
    • 0033956648 scopus 로고    scopus 로고
    • Enzymatic consumption of carbonyl sulfide (COS) by marine algae
    • DOI 10.1023/A:1006134213995
    • Blezinger, S., Wilhelm, C. & Kesselmeier, J. Enzymatic consumption of carbonyl sulfide (COS) by marine algae. Biogeochemistry 48, 185-197 (2000). (Pubitemid 30065336)
    • (2000) Biogeochemistry , vol.48 , Issue.2 , pp. 185-197
    • Blezinger, S.1    Wilhelm, C.2    Kesselmeier, J.3
  • 13
    • 0027878179 scopus 로고
    • 2 and their distributions
    • Chin, M. & Davis, D. D. Global sources and sinks of OCS and CS2 and their distributions. Glob. Biogeochem. Cycles 7, 321-337 (1993). (Pubitemid 24391858)
    • (1993) Global Biogeochemical Cycles , vol.7 , Issue.2 , pp. 321-337
    • Mian Chin1    Davis, D.D.2
  • 14
    • 15744395594 scopus 로고    scopus 로고
    • 2 toward the flour beetle Tribolium castaneum [Coleoptera: Tenebrionidae]
    • DOI 10.1016/j.cca.2005.01.012
    • Haritos, V. S. & Dojchinov, G. Carbonic anhydrase metabolismis a key factor in the toxicity of CO2 and COS but not CS2 toward the flour beetle Tribolium castaneum [Coleoptera: Tenebrionidae]. Comp. Biochem. Physiol. C Toxicol. Pharmacol. 140, 139-147 (2005). (Pubitemid 40409887)
    • (2005) Comparative Biochemistry and Physiology - C Toxicology and Pharmacology , vol.140 , Issue.1 , pp. 139-147
    • Haritos, V.S.1    Dojchinov, G.2
  • 15
    • 0032717842 scopus 로고    scopus 로고
    • A plant-type (β-class) carbonic anhydrase in the thermophilic methanoarchaeon Methanobacterium thermoautotrophicum
    • Smith, K. S. & Ferry, J. G. A plant-type (b-class) carbonic anhydrase in the thermophilic methanoarchaeon Methanobacterium thermoautotrophicum. J. Bacteriol. 181, 6247-6253 (1999). (Pubitemid 29512931)
    • (1999) Journal of Bacteriology , vol.181 , Issue.20 , pp. 6247-6253
    • Smith, K.S.1    Ferry, J.G.2
  • 16
    • 0032856157 scopus 로고    scopus 로고
    • Kinetic and spectroscopic characterization of the c-carbonic anhydrase from the methanoarchaeon Methanosarcina thermophila
    • Alber, B. E. et al. Kinetic and spectroscopic characterization of the c-carbonic anhydrase from the methanoarchaeon Methanosarcina thermophila. Biochemistry 38, 13119-13128 (1999).
    • (1999) Biochemistry , vol.38 , pp. 13119-13128
    • Alber, B.E.1
  • 17
    • 0015239422 scopus 로고
    • The carbon dioxide hydration activity of carbonic anhydrase
    • Khalifah, R. G. The carbon dioxide hydration activity of carbonic anhydrase. J. Biol. Chem. 246, 2561-2573 (1971).
    • (1971) J. Biol. Chem. , vol.246 , pp. 2561-2573
    • Khalifah, R.G.1
  • 18
    • 18544380806 scopus 로고    scopus 로고
    • A cadmiumenzyme froma marine diatom
    • Lane, T. W. et al.A cadmiumenzyme froma marine diatom. Nature435, 42 (2005).
    • (2005) Nature , vol.435 , pp. 42
    • Lane, T.W.1
  • 19
    • 61449255522 scopus 로고    scopus 로고
    • The archetype c-class carbonic anhydrase (Cam) contains iron when synthesized in vivo
    • MacAuley, S. R. et al. The archetype c-class carbonic anhydrase (Cam) contains iron when synthesized in vivo. Biochemistry 48, 817-819 (2009).
    • (2009) Biochemistry , vol.48 , pp. 817-819
    • MacAuley, S.R.1
  • 20
    • 0034599484 scopus 로고    scopus 로고
    • The active site architecture of Pisum sativum β-carbonic anhydrase is a mirror image of that of α-carbonic anhydrases
    • Kimber, M. S. & Pai, E. F. The active site architecture of Pisum sativum b-carbonic anhydrase is a mirror image of that of a-carbonic anhydrases. EMBO J. 19, 1407-1418 (2000). (Pubitemid 30182148)
    • (2000) EMBO Journal , vol.19 , Issue.7 , pp. 1407-1418
    • Kimber, M.S.1    Pai, E.F.2
  • 21
    • 27644443951 scopus 로고    scopus 로고
    • Bovine mitochondrial peroxiredoxin III forms a two-ring catenane
    • DOI 10.1016/j.str.2005.07.021, PII S0969212605003126
    • Cao, Z., Roszak, A. W., Gourlay, L. J., Lindsay, J. G. & Isaacs, N. W. Bovine mitochondrial peroxiredoxin III forms a two-ring catenane. Structure 13, 1661-1664 (2005). (Pubitemid 41571829)
    • (2005) Structure , vol.13 , Issue.11 , pp. 1661-1664
    • Cao, Z.1    Roszak, A.W.2    Gourlay, L.J.3    Lindsay, J.G.4    Isaacs, N.W.5
  • 22
    • 0034703226 scopus 로고    scopus 로고
    • Topologically linked protein rings in the bacteriophage HK97 capsid
    • Wikoff, W. R. et al. Topologically linked protein rings in the bacteriophage HK97 capsid. Science 289, 2129-2133 (2000).
    • (2000) Science , vol.289 , pp. 2129-2133
    • Wikoff, W.R.1
  • 23
    • 0035971165 scopus 로고    scopus 로고
    • Crystal structure of the "cab"-type b class carbonic anhydrase from the archaeon Methanobacterium thermoautotrophicum
    • Strop, P.,Smith, K. S., Iverson, T. M., Ferry, J. G.& Rees, D. C. Crystal structure of the "cab"-type b class carbonic anhydrase from the archaeon Methanobacterium thermoautotrophicum. J. Biol. Chem. 276, 10299-10305 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 10299-10305
    • Strop, P.1    Smith, K.S.2    Iverson, T.M.3    Ferry, J.G.4    Rees, D.C.5
  • 24
    • 21444449107 scopus 로고    scopus 로고
    • Structure and function of carbonic anhydrases from Mycobacterium tuberculosis
    • Suarez Covarrubias, A. et al. Structure and function of carbonic anhydrases from Mycobacterium tuberculosis. J. Biol. Chem. 280, 18782-18789 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 18782-18789
    • Suarez Covarrubias, A.1
  • 25
    • 72249101494 scopus 로고    scopus 로고
    • Structural insights into the substrate tunnel of Saccharomyces cerevisiae carbonic anhydrase Nce103
    • Teng, Y. B. et al. Structural insights into the substrate tunnel of Saccharomyces cerevisiae carbonic anhydrase Nce103. BMC Struct. Biol. 9, 67-76 (2009).
    • (2009) BMC Struct. Biol. , vol.9 , pp. 67-76
    • Teng, Y.B.1
  • 26
    • 58149330109 scopus 로고    scopus 로고
    • Structure and inhibition of the CO2-sensing carbonic anhydrase Can2 from the pathogenic fungus Cryptococcus neoformans
    • Schlicker, C. et al. Structure and inhibition of the CO2-sensing carbonic anhydrase Can2 from the pathogenic fungus Cryptococcus neoformans. J. Mol. Biol. 385, 1207-1220 (2009).
    • (2009) J. Mol. Biol. , vol.385 , pp. 1207-1220
    • Schlicker, C.1
  • 27
    • 56649103902 scopus 로고    scopus 로고
    • Searching protein structure databases with DaliLite v.3
    • DOI 10.1093/bioinformatics/btn507
    • Holm, L., Kaarlainen, S., Rosenstrom, P. & Schenkel, A. Searching protein structure databases with DaliLite v.3. Bioinformatics 25, 2780-2781 (2008). (Pubitemid 352722625)
    • (2008) Bioinformatics , vol.24 , Issue.23 , pp. 2780-2781
    • Holm, L.1    Kaariainen, S.2    Rosenstrom, P.3    Schenkel, A.4
  • 28
    • 74449087953 scopus 로고    scopus 로고
    • Structure and catalytic mechanism of the b-carbonic anhydrases
    • Rowlett, R. S. Structure and catalytic mechanism of the b-carbonic anhydrases. Biochim. Biophys. Acta 1804, 362-373 (2010).
    • (2010) Biochim. Biophys. Acta , vol.1804 , pp. 362-373
    • Rowlett, R.S.1
  • 31
    • 0000132232 scopus 로고
    • Studies with Cyanidium caldarium, an anomalously pigmented chlorophyte
    • Allen, M. B. Studies with Cyanidium caldarium, an anomalously pigmented chlorophyte. Arch. Mikrobiol. 32, 270-277 (1959).
    • (1959) Arch. Mikrobiol. , vol.32 , pp. 270-277
    • Allen, M.B.1
  • 36
    • 34547781750 scopus 로고    scopus 로고
    • MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0
    • DOI 10.1093/molbev/msm092
    • Tamura, K.,Dudley, J., Nei, M.&Kumar, S.MEGA4:molecular evolutionary genetics analysis (MEGA) software version 4.0. Mol. Biol. Evol. 24, 1596-1599 (2007). (Pubitemid 47236692)
    • (2007) Molecular Biology and Evolution , vol.24 , Issue.8 , pp. 1596-1599
    • Tamura, K.1    Dudley, J.2    Nei, M.3    Kumar, S.4
  • 37
    • 0023375195 scopus 로고
    • The neighbor-joining method: A new method for reconstructing phylogenetic trees
    • Saitou, N. & Nei, M. The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol. Biol. Evol. 4, 406-425 (1987).
    • (1987) Mol. Biol. Evol. , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 38
    • 0000461280 scopus 로고
    • Confidence imits on phylogenies: An approach using the bootstrap
    • Felsenstein, J. Confidence imits on phylogenies: an approach using the bootstrap. Evolution 39, 783-791 (1985).
    • (1985) Evolution , vol.39 , pp. 783-791
    • Felsenstein, J.1
  • 39
    • 0013776758 scopus 로고
    • Molecules as documents of evolutionary history
    • Zuckerkandl, E. & Pauling, L. Molecules as documents of evolutionary history. J. Theor. Biol. 8, 357-366 (1965).
    • (1965) J. Theor. Biol. , vol.8 , pp. 357-366
    • Zuckerkandl, E.1    Pauling, L.2
  • 40
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch, W. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Cryst. 26, 795-800 (1993).
    • (1993) J. Appl. Cryst. , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 42
    • 36549027357 scopus 로고    scopus 로고
    • Automated structure solution with autoSHARP
    • DOI 10.1385/1-59745-266-1:215, Macromolecular Crystallography Protocols, Volume 2: Structure Determination
    • Vonrhein, C., Blanc, E., Roversi, P.&Bricogne, G. Automated structure solution with autoSHARP. Methods Mol. Biol. 364, 215-230 (2007). (Pubitemid 350183137)
    • (2007) Methods in Molecular Biology , vol.364 , pp. 215-230
    • Vonrhein, C.1    Blanc, E.2    Roversi, P.3    Bricogne, G.4
  • 43
    • 13244281317 scopus 로고    scopus 로고
    • Model-building tools for molecular graphics
    • Emsley, P. & Cowtan, K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D 60, 2126-2132 (2004).
    • (2004) Acta Crystallogr. D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Coot, C.K.2
  • 44
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography and NMR system (CNS): A new software system for macromolecular structure determination
    • Brünger, A. T. et al. Crystallography and NMR system (CNS): a new software system for macromolecular structure determination. Acta Crystallogr. D 54, 905-921 (1998).
    • (1998) Acta Crystallogr. D , vol.54 , pp. 905-921
    • Brünger, A.T.1
  • 47
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies fromcrystalline state
    • DOI 10.1016/j.jmb.2007.05.022, PII S0022283607006420
    • Krissinel, E.&Henrick, K. Inference ofmacromolecular assemblies fromcrystalline state. J. Mol. Biol. 372, 774-797 (2007). (Pubitemid 47321791)
    • (2007) Journal of Molecular Biology , vol.372 , Issue.3 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 48
    • 0034009520 scopus 로고    scopus 로고
    • Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling
    • Schuck, P. Size distribution analysis ofmacromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling. Biophys. J. 78, 1606-1619 (2000). (Pubitemid 30141584)
    • (2000) Biophysical Journal , vol.78 , Issue.3 , pp. 1606-1619
    • Schuck, P.1
  • 49
    • 0001229341 scopus 로고    scopus 로고
    • Calculation of hydrodynamic properties of globular proteins from their atomic-level structure
    • Garća de la Torre, J., Huertas, M. L. & Carrasco, B. Calculation of hydrodynamic properties of globular proteins from their atomic-level structure. Biophys. J. 78, 719-730 (2000). (Pubitemid 30211830)
    • (2000) Biophysical Journal , vol.78 , Issue.2 , pp. 719-730
    • Garcia De La Torre, J.1    Huertas, M.L.2    Carrasco, B.3
  • 50
    • 0029185933 scopus 로고
    • CRYSOL - A program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates
    • DOI 10.1107/S0021889895007047
    • Svergun, D. I., Barberato, C. & Koch, M. CRYSOL-a program to evaluate X-ray solution scattering of biologicalmacromolecules fromatomic coordinates. J. Appl. Crystallogr. 28, 768-773 (1995). (Pubitemid 3014671)
    • (1995) Journal of Applied Crystallography , vol.28 , Issue.6 , pp. 768-773
    • Svergun, D.1    Barberato, C.2    Koch, M.H.3


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