메뉴 건너뛰기




Volumn 269, Issue 22, 2002, Pages 5712-5721

Purification and catalytic properties of a CO-oxidizing: H2-evolving enzyme complex from Carboxydothermus hydrogenoformans

Author keywords

Carbon monoxide dehydrogenase; Complex I; Iron sulfur protein; Membrane bound hydrogenase

Indexed keywords

CARBON DIOXIDE; CARBON MONOXIDE; CARBON MONOXIDE DEHYDROGENASE; HYDROGENASE; IRON; NICKEL; OXIDOREDUCTASE; PARAQUAT; PROTEIN SUBUNIT; PROTON; QUINONE DERIVATIVE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; SULFUR;

EID: 0036436922     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2002.03282.x     Document Type: Article
Times cited : (103)

References (38)
  • 3
    • 0033529852 scopus 로고    scopus 로고
    • Crystal structure and mechanism of CO dehydrogenase, a molybdo iron-sulfur flavoprotein containing S-selanylcysteine
    • Dobbek, H., Gremer, L., Meyer, O. & Huber, R. (1999) Crystal structure and mechanism of CO dehydrogenase, a molybdo iron-sulfur flavoprotein containing S-selanylcysteine. Proc. Natl Acad. Sci. USA 96, 8884-8889.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 8884-8889
    • Dobbek, H.1    Gremer, L.2    Meyer, O.3    Huber, R.4
  • 4
    • 0028925554 scopus 로고
    • Carbon monoxide-dependent growth of Rhodospirillum rubrum
    • Kerby, R.L., Ludden, P.W. & Roberts, G.P. (1995) Carbon monoxide-dependent growth of Rhodospirillum rubrum. J. Bacteriol. 177, 2241-2244.
    • (1995) J. Bacteriol. , vol.177 , pp. 2241-2244
    • Kerby, R.L.1    Ludden, P.W.2    Roberts, G.P.3
  • 5
    • 1342293305 scopus 로고
    • Anaerobic growth of a Rhodopseudomonas species in the dark with carbon monoxide as sole carbon and energy substrate
    • Uffen, R.L. (1976) Anaerobic growth of a Rhodopseudomonas species in the dark with carbon monoxide as sole carbon and energy substrate. Proc. Natl Acad. Sci. USA 73, 3298-3302.
    • (1976) Proc. Natl Acad. Sci. USA , vol.73 , pp. 3298-3302
    • Uffen, R.L.1
  • 6
    • 0020509698 scopus 로고
    • Metabolism of carbon monoxide by Rhodopseudomonas gelatinosa: Cell growth and properties of the oxidation system
    • Uffen, R.L. (1983) Metabolism of carbon monoxide by Rhodopseudomonas gelatinosa: cell growth and properties of the oxidation system. J. Bacteriol. 155, 956-965.
    • (1983) J. Bacteriol. , vol.155 , pp. 956-965
    • Uffen, R.L.1
  • 7
    • 0025894923 scopus 로고
    • Carboxydothermus hydrogenoformans General nov., sp. nov., a CO-utilizing thermophilic anaerobic bacterium from hypothermal environments of Kunashir island
    • Svetlichnyi, V.A., Sokolova, T.G., Gerhardt, M., Ringpfeil, M., Kostrikina, N.A. & Zavarzin, G.A. (1991) Carboxydothermus hydrogenoformans General nov., sp. nov., a CO-utilizing thermophilic anaerobic bacterium from hypothermal environments of Kunashir island. System. Appl. Microbiol. 14, 254-260.
    • (1991) System. Appl. Microbiol. , vol.14 , pp. 254-260
    • Svetlichnyi, V.A.1    Sokolova, T.G.2    Gerhardt, M.3    Ringpfeil, M.4    Kostrikina, N.A.5    Zavarzin, G.A.6
  • 9
    • 0030856066 scopus 로고    scopus 로고
    • CooA, a CO-sensing transcription factor from Rhodospirillum rubrum, is a CO-binding heme protein
    • Shelver, D., Kerby, R.L., He, Y. & Roberts, G.P. (1997) CooA, a CO-sensing transcription factor from Rhodospirillum rubrum, is a CO-binding heme protein. Proc. Natl Acad. Sci. USA 94, 11216-11220.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 11216-11220
    • Shelver, D.1    Kerby, R.L.2    He, Y.3    Roberts, G.P.4
  • 10
    • 0026649571 scopus 로고
    • Genetic and physiological characterization of the Rhodospirillum rubrum carbon monoxide dehydrogenase system
    • Kerby, R.L., Hong, S.S., Ensign, S.A., Coppoc, L.J., Ludden, P.W. & Roberts, G.P. (1992) Genetic and physiological characterization of the Rhodospirillum rubrum carbon monoxide dehydrogenase system. J. Bacteriol. 174, 5284-5294.
    • (1992) J. Bacteriol. , vol.174 , pp. 5284-5294
    • Kerby, R.L.1    Hong, S.S.2    Ensign, S.A.3    Coppoc, L.J.4    Ludden, P.W.5    Roberts, G.P.6
  • 11
    • 0030944159 scopus 로고    scopus 로고
    • In vivo nickel insertion into the carbon monoxide dehydrogenase of Rhodospirillum rubrum: Molecular and physiological characterization of CooCTJ
    • Kerby, R.L., Ludden, P.W. & Roberts, G.P. (1997) In vivo nickel insertion into the carbon monoxide dehydrogenase of Rhodospirillum rubrum: Molecular and physiological characterization of CooCTJ. J. Bacteriol. 179, 2259-2266.
    • (1997) J. Bacteriol. , vol.179 , pp. 2259-2266
    • Kerby, R.L.1    Ludden, P.W.2    Roberts, G.P.3
  • 12
    • 0023644648 scopus 로고
    • Purification and characterization of carbon monoxide dehydrogenase, a nickel, zinc, iron-sulfur protein, from Rhodospirillum rubrum
    • Bonam, D. & Ludden, P.W. (1987) Purification and characterization of carbon monoxide dehydrogenase, a nickel, zinc, iron-sulfur protein, from Rhodospirillum rubrum. J. Biol. Chem. 262, 2980-2987.
    • (1987) J. Biol. Chem. , vol.262 , pp. 2980-2987
    • Bonam, D.1    Ludden, P.W.2
  • 13
    • 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. & Ludden, P.W. (2001) Life on carbon monoxide: X-ray structure of Rhodospirillum rubrum Ni-Fe-S carbon monoxide dehydrogenase. Proc. Natl Acad. Sci. USA 98, 11973-11978.
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 11973-11978
    • Drennan, C.L.1    Heo, J.2    Sintchak, M.D.3    Schreiter, E.4    Ludden, P.W.5
  • 14
    • 0025954526 scopus 로고
    • 2 evolution system of Rhodospirillum rubrum. Role of a 22-kDa iron-sulfur protein in mediating electron transfer between carbon monoxide dehydrogenase and hydrogenase
    • 2 evolution system of Rhodospirillum rubrum. Role of a 22-kDa iron-sulfur protein in mediating electron transfer between carbon monoxide dehydrogenase and hydrogenase. J. Biol. Chem. 266, 18395-18403.
    • (1991) J. Biol. Chem. , vol.266 , pp. 18395-18403
    • Ensign, S.A.1    Ludden, P.W.2
  • 15
    • 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
    • Fox, J.D., Kerby, R.L., Roberts, G.P. & Ludden, P.W. (1996a) 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
  • 16
    • 10344238576 scopus 로고    scopus 로고
    • Characterization of the region encoding the CO-induced hydrogenase of Rhodospirillum rubrum
    • Fox, J.D., He, Y., Shelver, D., Roberts, G.P. & Ludden, P.W. (1996b) 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
    • 0032521598 scopus 로고    scopus 로고
    • An Escherichia coli hydrogenase-3-type hydrogenase in methanogenic archaea
    • 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
  • 18
    • 0033214609 scopus 로고    scopus 로고
    • Purification and catalytic properties of Ech hydrogenase from Methanosarcina barkeri
    • Meuer, J., Bartoschek, S., Koch, J., Künkel, A. & Hedderich, R. (1999) Purification and catalytic properties of Ech hydrogenase from Methanosarcina barkeri. Eur. J. Biochem. 265, 325-335.
    • (1999) Eur. J. Biochem. , vol.265 , pp. 325-335
    • Meuer, J.1    Bartoschek, S.2    Koch, J.3    Künkel, A.4    Hedderich, R.5
  • 19
    • 0025157053 scopus 로고
    • Nucleotide sequence and expression of an operon in Escherichia coli coding for formate hydrogenlyase components
    • 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
  • 20
    • 0026725149 scopus 로고
    • Mutational analysis of the operon (hyc) determining hydrogenase 3 formation in Escherichia coli
    • 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
  • 21
    • 0034637432 scopus 로고    scopus 로고
    • The respiratory complex I of bacteria, archaea and eukarya and its module common with membrane-bound multisubunit hydrogenases
    • Friedrich, T. & Scheide, D. (2000) The respiratory complex I of bacteria, archaea and eukarya and its module common with membrane-bound multisubunit hydrogenases. FEBS Lett. 479, 1-5.
    • (2000) FEBS Lett. , vol.479 , pp. 1-5
    • Friedrich, T.1    Scheide, D.2
  • 22
    • 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
    • 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. 264, 930-943.
    • (1999) Eur. J. Biochem. , vol.264 , pp. 930-943
    • Tersteegen, A.1    Hedderich, R.2
  • 24
    • 0037117505 scopus 로고    scopus 로고
    • Genetic analysis of the archaeon Methanosarcina barkeri Fusaro reveals a central role for Ech hydrogenase and ferredoxin in methanogenesis and carbon fixation
    • Meuer, J., Kuettner, H.C., Zhang, J.K., Hedderich, R. & Metcalf, W.W. (2002) Genetic analysis of the archaeon Methanosarcina barkeri Fusaro reveals a central role for Ech hydrogenase and ferredoxin in methanogenesis and carbon fixation. Proc. Natl Acad. Sci. USA 99, 5632-5637.
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 5632-5637
    • Meuer, J.1    Kuettner, H.C.2    Zhang, J.K.3    Hedderich, R.4    Metcalf, W.W.5
  • 25
    • 0034879722 scopus 로고    scopus 로고
    • Two membrane-associated NiFeS-carbon monoxide dehy-drogenases from the anaerobic carbon-monoxide-utilizing eubacterium Carboxydothermus hydrogenoformans
    • Svetlitchnyi, V., Peschel, C., Acker, G. & Meyer, O. (2001) Two membrane-associated NiFeS-carbon monoxide dehy-drogenases from the anaerobic carbon-monoxide-utilizing eubacterium Carboxydothermus hydrogenoformans. J. Bacteriol. 183, 5134-5144.
    • (2001) J. Bacteriol. , vol.183 , pp. 5134-5144
    • Svetlitchnyi, V.1    Peschel, C.2    Acker, G.3    Meyer, O.4
  • 26
    • 0035902973 scopus 로고    scopus 로고
    • Crystal structure of a carbon monoxide dehydrogenase reveals a [Ni-4Fe-5S] cluster
    • Dobbek, H., Svetlitchnyi, V., Gremer, L., Huber, R. & Meyer, O. (2001) Crystal structure of a carbon monoxide dehydrogenase reveals a [Ni-4Fe-5S] cluster. Science. 293, 1281-1285.
    • (2001) Science , vol.293 , pp. 1281-1285
    • Dobbek, H.1    Svetlitchnyi, V.2    Gremer, L.3    Huber, R.4    Meyer, O.5
  • 27
    • 0023899855 scopus 로고
    • Rapid colorimetric micromethod for the quantitation of complexed iron in biological samples
    • Riordan, J.F. & Vallee, B.L., eds. Academic Press Inc, New York
    • Fish, W.W. (1988) Rapid colorimetric micromethod for the quantitation of complexed iron in biological samples. Methods in Enzymology (Riordan, J.F. & Vallee, B.L., eds), pp. 357-364. Academic Press Inc, New York.
    • (1988) Methods in Enzymology , pp. 357-364
    • Fish, W.W.1
  • 28
    • 84944816274 scopus 로고
    • Spectrophotometric determination of hydrogen sulfide in natural waters
    • 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
  • 29
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • 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
  • 30
    • 0033773868 scopus 로고    scopus 로고
    • Organic solvent extraction as a versatile procedure to identify hydrophobic chloroplast membrane proteins
    • Ferro, M., Seigneurin-Berny, D., Rolland, N., Chapel, A., Salvi, D., Garin, J. & Joyard, J. (2000) Organic solvent extraction as a versatile procedure to identify hydrophobic chloroplast membrane proteins. Electrophoresis. 21, 3517-3526.
    • (2000) Electrophoresis , vol.21 , pp. 3517-3526
    • Ferro, M.1    Seigneurin-Berny, D.2    Rolland, N.3    Chapel, A.4    Salvi, D.5    Garin, J.6    Joyard, J.7
  • 31
    • 0036127937 scopus 로고    scopus 로고
    • Improved in-gel approaches to generate peptide maps of integral membrane proteins with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
    • van Montfort, B.A., Canas, B., Duurkens, R., Godovac-Zimmermann, J. & Robillard, G.T. (2002) Improved in-gel approaches to generate peptide maps of integral membrane proteins with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. J. Mass Spectrom. 37, 322-330.
    • (2002) J. Mass Spectrom , vol.37 , pp. 322-330
    • Van Montfort, B.A.1    Canas, B.2    Duurkens, R.3    Godovac-Zimmermann, J.4    Robillard, G.T.5
  • 32
    • 85173396213 scopus 로고
    • Denaturing electrophoretic techniques
    • G.V.J. H. & S., eds. Academic Press, San Diego
    • Schägger, H. (1994) Denaturing electrophoretic techniques. A Practical Guide to Membrane Protein Purification (G.V.J. H. & S., eds), pp. 59-79. Academic Press, San Diego.
    • (1994) A Practical Guide to Membrane Protein Purification , pp. 59-79
    • Schägger, H.1
  • 33
    • 0036304751 scopus 로고    scopus 로고
    • Network of hydrogenase maturation in Escherichia coli: Role of accessory proteins HypA and HybF
    • Hube, M. Blokesch, M. & Böck, A. (2002) Network of hydro-genase maturation in Escherichia coli: role of accessory proteins HypA and HybF. J. Bacteriol. 184, 3879-3885.
    • (2002) J. Bacteriol. , vol.184 , pp. 3879-3885
    • Hube, M.1    Blokesch, M.2    Böck, A.3
  • 34
    • 0034933868 scopus 로고    scopus 로고
    • Redox-dependent activation of CO dehydrogenase from Rhodospirillum rubrum
    • Heo, J. Halbleib, C.M. & Ludden, P.W. (2001) Redox-dependent activation of CO dehydrogenase from Rhodospirillum rubrum. Proc. Natl Acad. Sci. USA 98, 7690-7693.
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 7690-7693
    • Heo, J.1    Halbleib, C.M.2    Ludden, P.W.3
  • 35
    • 0031018357 scopus 로고    scopus 로고
    • 430 is reduced to the nickel (I) oxidation state by titanium (III) citrate
    • 430 is reduced to the nickel (I) oxidation state by titanium (III) citrate. Eur. J. Biochem. 243, 110-114.
    • (1997) Eur. J. Biochem. , vol.243 , pp. 110-114
    • Goubeaud, M.1    Schreiner, G.2    Thauer, R.K.3
  • 36
    • 0024968417 scopus 로고
    • Nickel-specific, slow-binding inhibition of carbon monoxide dehydrogenase from Rhodospirillum rubrum by cyanide
    • Ensign, S.A. Hyman, M.R. & 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
  • 38
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.