메뉴 건너뛰기




Volumn 47, Issue 26, 2008, Pages 6770-6781

13C NMR characterization of an exchange reaction between CO and CO2 catalyzed by carbon monoxide dehydrogenase

Author keywords

[No Author keywords available]

Indexed keywords

CARBON MONOXIDE (CO) DEHYDROGENASE; REVERSIBLE OXIDATION;

EID: 46049094831     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi8004522     Document Type: Article
Times cited : (47)

References (50)
  • 1
    • 33745930076 scopus 로고
    • Relaxation Effects in Nuclear Magnetic Resonance Absorption
    • Bloembergen, N., Purcell, E. M., and Pound, R. V. (1948) Relaxation Effects in Nuclear Magnetic Resonance Absorption. Phys. Rev. 73, 679-712.
    • (1948) Phys. Rev , vol.73 , pp. 679-712
    • Bloembergen, N.1    Purcell, E.M.2    Pound, R.V.3
  • 2
    • 0034879722 scopus 로고    scopus 로고
    • Two Membrane-Associated NiFeS-Carbon Monoxide Dehydrogenases from the Anaerobic Carbon-Monoxide-Utilizing Eubacterium Carboxydothermus hydrogenoformans
    • Svetlitchnyi, V. P. C. A. G., and Meyer, O. (2001) Two Membrane-Associated NiFeS-Carbon Monoxide Dehydrogenases from the Anaerobic Carbon-Monoxide-Utilizing Eubacterium Carboxydothermus hydrogenoformans. J. Bacteriol. 183, 5134-5144.
    • (2001) J. Bacteriol , vol.183 , pp. 5134-5144
    • Svetlitchnyi, V.P.C.A.G.1    Meyer, O.2
  • 3
    • 0003768271 scopus 로고
    • Chapman & Hall, New York
    • Drake, H. L. (1994) Acetogenesis, Chapman & Hall, New York.
    • (1994) Acetogenesis
    • Drake, H.L.1
  • 5
    • 0346034961 scopus 로고    scopus 로고
    • A novel binuclear [CuSMo] cluster at the active site of carbon monoxide dehydrogenase: Characterization by X-ray absorption spectroscopy
    • Gnida, M., Ferner, R., Gremer, L., Meyer, O., and Meyer-Klaucke, W. (2003) A novel binuclear [CuSMo] cluster at the active site of carbon monoxide dehydrogenase: Characterization by X-ray absorption spectroscopy. Biochemistry 42, 222-230.
    • (2003) Biochemistry , vol.42 , pp. 222-230
    • Gnida, M.1    Ferner, R.2    Gremer, L.3    Meyer, O.4    Meyer-Klaucke, W.5
  • 8
    • 0035834117 scopus 로고    scopus 로고
    • Life on carbon monoxide: X-ray structure of Rhodospirillum rubrum Ni-Fe-S carbon monoxide dehydrogenase
    • Drennan, C. L., Heo, J., Sintchak, M. D., Schreiter, E., and Ludden, P. W. (2001) Life on carbon monoxide: X-ray structure of Rhodospirillum rubrum Ni-Fe-S carbon monoxide dehydrogenase. Proc. Natl. Acad. Sci. U.S.A. 98, 11973-11978.
    • (2001) Proc. Natl. Acad. Sci. U.S.A , vol.98 , pp. 11973-11978
    • Drennan, C.L.1    Heo, J.2    Sintchak, M.D.3    Schreiter, E.4    Ludden, P.W.5
  • 9
    • 36749053439 scopus 로고    scopus 로고
    • Carbon dioxide activation at the Ni,Fe-cluster of anaerobic carbon monoxide dehydrogenase
    • Jeoung, J. H., and Dobbek, H. (2007) Carbon dioxide activation at the Ni,Fe-cluster of anaerobic carbon monoxide dehydrogenase. Science 318, 1461-1464.
    • (2007) Science , vol.318 , pp. 1461-1464
    • Jeoung, J.H.1    Dobbek, H.2
  • 10
    • 0003113587 scopus 로고    scopus 로고
    • The Eastern and Western branches of the Wood/Ljungdahl pathway: How the East and West were won
    • Ragsdale, S. W. (1997) The Eastern and Western branches of the Wood/Ljungdahl pathway: How the East and West were won. BioFactors 9, 1-9.
    • (1997) BioFactors , vol.9 , pp. 1-9
    • Ragsdale, S.W.1
  • 11
    • 0037133256 scopus 로고    scopus 로고
    • The Ni-containing Carbon Monoxide Dehydrogenase Family: Light at the End of the Tunnel
    • Lindahl, P. A. (2002) The Ni-containing Carbon Monoxide Dehydrogenase Family: Light at the End of the Tunnel. Biochemistry 41, 2097-2105.
    • (2002) Biochemistry , vol.41 , pp. 2097-2105
    • Lindahl, P.A.1
  • 12
    • 0037374820 scopus 로고    scopus 로고
    • Ni-Zn-[Fe4-S4] and Ni-Ni-[Fe4-S4] clusters in closed and open subunits of acetyl-CoA synthase/carbon monoxide dehydrogenase
    • Darnault, C., Volbeda, A., Kim, E. J., Legrand, P., Vernede, X., Lindahl, P. A., and Fontecilla-Camps, J. C. (2003) Ni-Zn-[Fe4-S4] and Ni-Ni-[Fe4-S4] clusters in closed and open subunits of acetyl-CoA synthase/carbon monoxide dehydrogenase. Nat. Struct. Biol. 10, 271-279.
    • (2003) Nat. Struct. Biol , vol.10 , pp. 271-279
    • Darnault, C.1    Volbeda, A.2    Kim, E.J.3    Legrand, P.4    Vernede, X.5    Lindahl, P.A.6    Fontecilla-Camps, J.C.7
  • 13
    • 0037131241 scopus 로고    scopus 로고
    • A Ni-Fe-Cu center in a bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase
    • Doukov, T. I., Iverson, T. M., Seravalli, J., Ragsdale, S. W., and Drennan, C. L. (2002) A Ni-Fe-Cu center in a bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase. Science 298, 567-572.
    • (2002) Science , vol.298 , pp. 567-572
    • Doukov, T.I.1    Iverson, T.M.2    Seravalli, J.3    Ragsdale, S.W.4    Drennan, C.L.5
  • 14
    • 0035902973 scopus 로고    scopus 로고
    • Crystal structure of a carbon monoxide dehydrogenase reveals a [Ni-4Fe-5S] cluster
    • Dobbek, H. S. V., Gremer, L., Huber, R., and Meyer, O. (2001) Crystal structure of a carbon monoxide dehydrogenase reveals a [Ni-4Fe-5S] cluster. Science 203, 1281-1285.
    • (2001) Science , vol.203 , pp. 1281-1285
    • Dobbek, H.S.V.1    Gremer, L.2    Huber, R.3    Meyer, O.4
  • 15
    • 0033777079 scopus 로고    scopus 로고
    • Nitrogenase standing at the crossroads
    • Rees, D. C., and Howard, J. B. (2000) Nitrogenase standing at the crossroads. Curr. Opin. Chem. Biol. 4, 559-566.
    • (2000) Curr. Opin. Chem. Biol , vol.4 , pp. 559-566
    • Rees, D.C.1    Howard, J.B.2
  • 16
    • 33751256876 scopus 로고    scopus 로고
    • How many metals does it take to fix N2? A mechanistic overview of biological nitrogen fixation
    • Howard, J. B., and Rees, D. C. (2006) How many metals does it take to fix N2? A mechanistic overview of biological nitrogen fixation. Proc. Natl. Acad. Sci. U.S.A. 103, 17088-17093.
    • (2006) Proc. Natl. Acad. Sci. U.S.A , vol.103 , pp. 17088-17093
    • Howard, J.B.1    Rees, D.C.2
  • 17
    • 0029020516 scopus 로고
    • Mechanism of CO oxidation by carbon monoxide dehydrogenase from Clostridium thermoaceticum and its inhibition by anions
    • Seravalli, J., Kumar, M., Lu, W. P., and Ragsdale, S. W. (1995) Mechanism of CO oxidation by carbon monoxide dehydrogenase from Clostridium thermoaceticum and its inhibition by anions. Biochemistry 34, 7879-7888.
    • (1995) Biochemistry , vol.34 , pp. 7879-7888
    • Seravalli, J.1    Kumar, M.2    Lu, W.P.3    Ragsdale, S.W.4
  • 18
    • 0030057102 scopus 로고    scopus 로고
    • 2 reduction active site of carbon monoxide dehydrogenase and mechanistic implications
    • 2 reduction active site of carbon monoxide dehydrogenase and mechanistic implications. Biochemistry 35, 8371-8380.
    • (1996) Biochemistry , vol.35 , pp. 8371-8380
    • Anderson, M.E.1    Lindahl, P.A.2
  • 19
    • 0030885194 scopus 로고    scopus 로고
    • The mechanism of carbon monoxide oxidation by the carbon monoxide dehydrogenase/acetyl-CoA synthase from Clostridium thermoaceticum: Kinetic characterization of the intermediates
    • Seravalli, J., Kumar, M., Lu, W. P., and Ragsdale, S. (1997) The mechanism of carbon monoxide oxidation by the carbon monoxide dehydrogenase/acetyl-CoA synthase from Clostridium thermoaceticum: Kinetic characterization of the intermediates. Biochemistry 36, 11241-11251.
    • (1997) Biochemistry , vol.36 , pp. 11241-11251
    • Seravalli, J.1    Kumar, M.2    Lu, W.P.3    Ragsdale, S.4
  • 20
    • 33748630485 scopus 로고    scopus 로고
    • Metals and their scaffolds to promote difficult enzymatic reactions
    • Ragsdale, S. W. (2006) Metals and their scaffolds to promote difficult enzymatic reactions. Chem. Rev. 106, 3317-3337.
    • (2006) Chem. Rev , vol.106 , pp. 3317-3337
    • Ragsdale, S.W.1
  • 21
    • 0033619709 scopus 로고    scopus 로고
    • 2 active site of acetyl-CoA synthase (carbon monoxide dehydrogenase) from Clostridium thermoaceticum
    • 2 active site of acetyl-CoA synthase (carbon monoxide dehydrogenase) from Clostridium thermoaceticum. Biochemistry 38, 15706-15711.
    • (1999) Biochemistry , vol.38 , pp. 15706-15711
    • Fraser, D.M.L.P.A.1
  • 25
    • 0018332553 scopus 로고
    • 3 Exchange Catalyzed by Human Carbonic Anhydrase C at Chemical Equilibrium
    • 3 Exchange Catalyzed by Human Carbonic Anhydrase C at Chemical Equilibrium. Eur. J. Biochem. 93, 409-417.
    • (1979) Eur. J. Biochem , vol.93 , pp. 409-417
    • Simonsson, I.1    Jonsson, B.H.2    Lindskog, S.3
  • 28
    • 0000829041 scopus 로고
    • 2 Catalyzed by Human Carbonic Anhydrase II
    • 2 Catalyzed by Human Carbonic Anhydrase II. J. Am. Chem. Soc. 104, 6737-6741.
    • (1982) J. Am. Chem. Soc , vol.104 , pp. 6737-6741
    • Rowlett, R.1    Silverman, D.2
  • 29
    • 4244186877 scopus 로고
    • Kinetics of the Isotopic Exchange Reaction between Carbon Monoxide and Carbon Dioxide
    • Brandner, J. D., and Urey, H. C. (1945) Kinetics of the Isotopic Exchange Reaction between Carbon Monoxide and Carbon Dioxide. J. Chem. Phys. 13, 351-362.
    • (1945) J. Chem. Phys , vol.13 , pp. 351-362
    • Brandner, J.D.1    Urey, H.C.2
  • 30
    • 36849128314 scopus 로고
    • Kinetics of the Isotope Exchange Reaction between Carbon Monoxide and Carbon Dioxide
    • Norris, T. H., and Ruben, S. (1950) Kinetics of the Isotope Exchange Reaction between Carbon Monoxide and Carbon Dioxide. J. Chem. Phys. 18, 1595-1600.
    • (1950) J. Chem. Phys , vol.18 , pp. 1595-1600
    • Norris, T.H.1    Ruben, S.2
  • 31
    • 3142777049 scopus 로고    scopus 로고
    • CO-induced structural rearrangement of the C-cluster in Carboxydothermus hydrogenoformans CO dehydrogenase: Evidence from Ni K-edge X-ray absorption spectroscopy
    • Gu, W. S. J., Ragsdale, S. W., and Cramer, S. P. (2004) CO-induced structural rearrangement of the C-cluster in Carboxydothermus hydrogenoformans CO dehydrogenase: Evidence from Ni K-edge X-ray absorption spectroscopy. Biochemistry 43, 9029-9035.
    • (2004) Biochemistry , vol.43 , pp. 9029-9035
    • Gu, W.S.J.1    Ragsdale, S.W.2    Cramer, S.P.3
  • 32
    • 0018130673 scopus 로고
    • The inactivation of yeast enolase by 2,3-butanedione
    • Elliott, J. I., and Brewer, J. M. (1978) The inactivation of yeast enolase by 2,3-butanedione. Arch. Biochem. Biophys. 190, 351-357.
    • (1978) Arch. Biochem. Biophys , vol.190 , pp. 351-357
    • Elliott, J.I.1    Brewer, J.M.2
  • 34
    • 0037031291 scopus 로고    scopus 로고
    • NMR Identification and Characterization of the Flexible Regions in the 160 kDa Molten Globule-Like Aggregate of Barstar at Low pH
    • Juneja, J., Bhavesh, N. S., Udgaonkar, J. B., and Hosur, R. V. (2002) NMR Identification and Characterization of the Flexible Regions in the 160 kDa Molten Globule-Like Aggregate of Barstar at Low pH. Biochemistry 41, 9885-9899.
    • (2002) Biochemistry , vol.41 , pp. 9885-9899
    • Juneja, J.1    Bhavesh, N.S.2    Udgaonkar, J.B.3    Hosur, R.V.4
  • 35
    • 0028021651 scopus 로고
    • Binding of carbon disufide to the site of acetyl-CoA synthesis by the nickel-iron-sulfur protein, CO dehydrogenase, from Clostridium thermoaceticum
    • Kumar, M., Lu, W.-P., and Ragsdale, S. W. (1994) Binding of carbon disufide to the site of acetyl-CoA synthesis by the nickel-iron-sulfur protein, CO dehydrogenase, from Clostridium thermoaceticum. Biochemistry 33, 9769-9777.
    • (1994) Biochemistry , vol.33 , pp. 9769-9777
    • Kumar, M.1    Lu, W.-P.2    Ragsdale, S.W.3
  • 36
    • 2442532229 scopus 로고    scopus 로고
    • Evidence for a Proton Transfer Network and a Required Persulfide-Bond-Forming Cysteine Residue in Ni-Containing Carbon Monoxide Dehydrogenases
    • Kim, E. J., Feng, J., Bramlett, M. R., and Lindahl, P. A. (2004) Evidence for a Proton Transfer Network and a Required Persulfide-Bond-Forming Cysteine Residue in Ni-Containing Carbon Monoxide Dehydrogenases. Biochemistry 43, 5728-5734.
    • (2004) Biochemistry , vol.43 , pp. 5728-5734
    • Kim, E.J.1    Feng, J.2    Bramlett, M.R.3    Lindahl, P.A.4
  • 37
    • 0024968419 scopus 로고
    • Nickel is required for the transfer of electrons from carbon monoxide to the iron-sulfur center(s) of carbon monoxide dehydrogenase from Rhodospirillum rubrum
    • Ensign, S. A., Bonam, D., and Ludden, P. W. (1989) Nickel is required for the transfer of electrons from carbon monoxide to the iron-sulfur center(s) of carbon monoxide dehydrogenase from Rhodospirillum rubrum. Biochemistry 28, 4968-4973.
    • (1989) Biochemistry , vol.28 , pp. 4968-4973
    • Ensign, S.A.1    Bonam, D.2    Ludden, P.W.3
  • 38
    • 34249849252 scopus 로고    scopus 로고
    • Interaction of Potassium Cyanide with the [Ni-4Fe-5S] Active Site Cluster of CO Dehydrogenase from Carboxydothermus hydrogenoformans
    • Ha, S.-H., Korbas, M., Klepsch, M., Meyer-Klaucke, W., Meyer, O., and Svetlitchnyi, V. (2007) Interaction of Potassium Cyanide with the [Ni-4Fe-5S] Active Site Cluster of CO Dehydrogenase from Carboxydothermus hydrogenoformans. J. Biol. Chem. 282, 10639-10646.
    • (2007) J. Biol. Chem , vol.282 , pp. 10639-10646
    • Ha, S.-H.1    Korbas, M.2    Klepsch, M.3    Meyer-Klaucke, W.4    Meyer, O.5    Svetlitchnyi, V.6
  • 39
    • 0024968417 scopus 로고
    • Nickel-specific, slow binding inhibition of carbon monoxide dehydrogenase from Rhodospirillum rubrum by cyanide
    • Ensign, S. A., Hyman, M. R., and Ludden, P. W. (1989) Nickel-specific, slow binding inhibition of carbon monoxide dehydrogenase from Rhodospirillum rubrum by cyanide. Biochemistry 28, 4973-4979.
    • (1989) Biochemistry , vol.28 , pp. 4973-4979
    • Ensign, S.A.1    Hyman, M.R.2    Ludden, P.W.3
  • 40
    • 0028110887 scopus 로고
    • Organization of clusters and internal electron pathways in CO dehydrogenase from Clostrid ium thermoaceticum: Relevance to the mechanism of catalysis and cyanide inhibition
    • Anderson, M. E., and Lindahl, P. A. (1994) Organization of clusters and internal electron pathways in CO dehydrogenase from Clostrid ium thermoaceticum: Relevance to the mechanism of catalysis and cyanide inhibition. Biochemistry 33, 8702-8711.
    • (1994) Biochemistry , vol.33 , pp. 8702-8711
    • Anderson, M.E.1    Lindahl, P.A.2
  • 41
    • 0032475404 scopus 로고    scopus 로고
    • A Multinuclear ENDOR Study of the C-Cluster in CO Dehydrogenase from Clostridium thermoaceticum: Evidence for HxO and Histidine Coordination to the [Fe4S4]
    • DeRose, V. J., Telser, J., Anderson, M. E., Lindahl, P. A., and Hoffman, B. M. (1998) A Multinuclear ENDOR Study of the C-Cluster in CO Dehydrogenase from Clostridium thermoaceticum: Evidence for HxO and Histidine Coordination to the [Fe4S4] Center. J. Am. Chem. Soc. 120, 8767-8776.
    • (1998) Center. J. Am. Chem. Soc , vol.120 , pp. 8767-8776
    • DeRose, V.J.1    Telser, J.2    Anderson, M.E.3    Lindahl, P.A.4    Hoffman, B.M.5
  • 43
    • 0142072511 scopus 로고    scopus 로고
    • Ultrafast microfluidic mixer and freeze-quenching device
    • Lin, Y., Gerfen, G. J., Rousseau, D. L., and Yeh, S. R. (2003) Ultrafast microfluidic mixer and freeze-quenching device. Anal. Chem. 75, 5381-5386.
    • (2003) Anal. Chem , vol.75 , pp. 5381-5386
    • Lin, Y.1    Gerfen, G.J.2    Rousseau, D.L.3    Yeh, S.R.4
  • 44
    • 0346995022 scopus 로고    scopus 로고
    • Infrared studies of carbon monoxide binding to carbon monoxide dehydrogenase/acetyl-CoA synthase from Moorella thermoacetica
    • Cheng, J., Huang, S., Seravalli, J., Gutzman, H.-J., Schwartz, D., Ragsdale, S. W., and Bagley, K. (2003) Infrared studies of carbon monoxide binding to carbon monoxide dehydrogenase/acetyl-CoA synthase from Moorella thermoacetica. Biochemistry 42, 14822-14830.
    • (2003) Biochemistry , vol.42 , pp. 14822-14830
    • Cheng, J.1    Huang, S.2    Seravalli, J.3    Gutzman, H.-J.4    Schwartz, D.5    Ragsdale, S.W.6    Bagley, K.7
  • 46
    • 13444269025 scopus 로고    scopus 로고
    • Structural and kinetic characterization of active-site histidine as a proton shuttle in catalysis by human carbonic anhydrase II
    • Fisher, S. Z., Hernandez-Prada, J. A., Duda, D., Yoshioka, C., An, H., Govindasamy, L., Silverman, D. N., and McKenna, R. (2005) Structural and kinetic characterization of active-site histidine as a proton shuttle in catalysis by human carbonic anhydrase II. Biochemistry 44, 1097-1105.
    • (2005) Biochemistry , vol.44 , pp. 1097-1105
    • Fisher, S.Z.1    Hernandez-Prada, J.A.2    Duda, D.3    Yoshioka, C.4    An, H.5    Govindasamy, L.6    Silverman, D.N.7    McKenna, R.8
  • 47
    • 0024421430 scopus 로고
    • Role of histidine 64 in the catalytic mechanism of human carbonic anhydrase II studied with a site-specific mutant
    • Tu, C. K., Silverman, D., Forsman, C., Jonsson, B. H., and Lindskog, S. (1989) Role of histidine 64 in the catalytic mechanism of human carbonic anhydrase II studied with a site-specific mutant. Biochemistry 28, 7913-7918.
    • (1989) Biochemistry , vol.28 , pp. 7913-7918
    • Tu, C.K.1    Silverman, D.2    Forsman, C.3    Jonsson, B.H.4    Lindskog, S.5
  • 48
    • 0035852857 scopus 로고    scopus 로고
    • Structural and kinetic analysis of the chemical rescue of the proton transfer function of carbonic anhydrase II
    • Duda, D., Tu, C., Qian, M., Laipis, P., Agbandje-McKenna, M., Silverman, D. N., and McKenna, R. (2001) Structural and kinetic analysis of the chemical rescue of the proton transfer function of carbonic anhydrase II. Biochemistry 40, 1741-1748.
    • (2001) Biochemistry , vol.40 , pp. 1741-1748
    • Duda, D.1    Tu, C.2    Qian, M.3    Laipis, P.4    Agbandje-McKenna, M.5    Silverman, D.N.6    McKenna, R.7
  • 50
    • 0033523919 scopus 로고    scopus 로고
    • Natural engineering principles of electron tunnelling in biological oxidation-reduction
    • Page, C. C., Moser, C. C., Chen, X., and Dutton, L. (1999) Natural engineering principles of electron tunnelling in biological oxidation-reduction. Nature 402, 47-52.
    • (1999) Nature , vol.402 , pp. 47-52
    • Page, C.C.1    Moser, C.C.2    Chen, X.3    Dutton, L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.