메뉴 건너뛰기




Volumn 15, Issue 2, 2011, Pages 276-283

A role for nickel-iron cofactors in biological carbon monoxide and carbon dioxide utilization

Author keywords

[No Author keywords available]

Indexed keywords

CARBON DIOXIDE; CARBON MONOXIDE; CARBON MONOXIDE DEHYDROGENASE; CYANIDE; NICKEL IRON COFACTOR; NICKEL IRON HYDROGENASE; UNCLASSIFIED DRUG;

EID: 79953316385     PISSN: 13675931     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpa.2010.11.005     Document Type: Review
Times cited : (86)

References (41)
  • 1
    • 35748930865 scopus 로고    scopus 로고
    • Structure/function relationships of [NiFe]- and [FeFe]-hydrogenases
    • Fontecilla-Camps J.C., Volbeda A., Cavazza C., Nicolet Y. Structure/function relationships of [NiFe]- and [FeFe]-hydrogenases. Chem Rev 2007, 107:4273-4303.
    • (2007) Chem Rev , vol.107 , pp. 4273-4303
    • Fontecilla-Camps, J.C.1    Volbeda, A.2    Cavazza, C.3    Nicolet, Y.4
  • 2
    • 35748974830 scopus 로고    scopus 로고
    • Occurrence, classification, and biological function of hydrogenases: an overview
    • Vignais P.M., Billoud B. Occurrence, classification, and biological function of hydrogenases: an overview. Chem Rev 2007, 107:4206-4272.
    • (2007) Chem Rev , vol.107 , pp. 4206-4272
    • Vignais, P.M.1    Billoud, B.2
  • 4
    • 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., Drennan C.L. A Ni-Fe-Cu center in a bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase. Science 2002, 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
  • 5
    • 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. Crystal structure of a carbon monoxide dehydrogenase reveals a [Ni-4Fe-5S] cluster. Science 2001, 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
  • 6
    • 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. Life on carbon monoxide: X-ray structure of Rhodospirillum rubrum Ni-Fe-S carbon monoxide dehydrogenase. Proc Natl Acad Sci U S A 2001, 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
  • 7
    • 1342293305 scopus 로고
    • Anaerobic growth of a Rhodopseudomonas species in the dark with carbon monoxide as sole carbon and energy substrate
    • Uffen R.L. Anaerobic growth of a Rhodopseudomonas species in the dark with carbon monoxide as sole carbon and energy substrate. Proc Natl Acad Sci U S A 1976, 73:3298-3302.
    • (1976) Proc Natl Acad Sci U S A , vol.73 , pp. 3298-3302
    • Uffen, R.L.1
  • 8
    • 0025894923 scopus 로고
    • Carboxydothermus hydrogenoformans gen. nov., sp. nov., a CO-utilizing thermophilic anaerobic bacterium from hydrothermal environments of Kunashir Island
    • Svetlichny V.A., Sokolova T.G., Gerhardt M., Ringpfeil M., Kostrikina N.A., Zavarzin G.A. Carboxydothermus hydrogenoformans gen. nov., sp. nov., a CO-utilizing thermophilic anaerobic bacterium from hydrothermal environments of Kunashir Island. Syst Appl Microbiol 1991, 14:254-260.
    • (1991) Syst Appl Microbiol , vol.14 , pp. 254-260
    • Svetlichny, V.A.1    Sokolova, T.G.2    Gerhardt, M.3    Ringpfeil, M.4    Kostrikina, N.A.5    Zavarzin, G.A.6
  • 9
    • 0018385285 scopus 로고
    • Microbial metabolism of carbon monoxide in culture and in soil
    • Bartholomew G.W., Alexander M. Microbial metabolism of carbon monoxide in culture and in soil. Appl Environ Microbiol 1979, 37:932-937.
    • (1979) Appl Environ Microbiol , vol.37 , pp. 932-937
    • Bartholomew, G.W.1    Alexander, M.2
  • 11
    • 0032864316 scopus 로고    scopus 로고
    • 2 reduction and acetyl-CoA synthesis in acetyl-CoA synthase from Clostridium thermoaceticum
    • 2 reduction and acetyl-CoA synthesis in acetyl-CoA synthase from Clostridium thermoaceticum. J Am Chem Soc 1999, 121:9221-9222.
    • (1999) J Am Chem Soc , vol.121 , pp. 9221-9222
    • Maynard, E.L.1    Lindahl, P.A.2
  • 12
    • 0034673091 scopus 로고    scopus 로고
    • Channeling of carbon monoxide during anaerobic carbon dioxide fixation
    • Seravalli J., Ragsdale S.W. Channeling of carbon monoxide during anaerobic carbon dioxide fixation. Biochemistry 2000, 39:1274-1277.
    • (2000) Biochemistry , vol.39 , pp. 1274-1277
    • Seravalli, J.1    Ragsdale, S.W.2
  • 14
    • 40949131858 scopus 로고    scopus 로고
    • Xenon in and at the end of the tunnel of bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase
    • Doukov T.I., Blasiak L.C., Seravalli J., Ragsdale S.W., Drennan C.L. Xenon in and at the end of the tunnel of bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase. Biochemistry 2008, 47:3474-3483.
    • (2008) Biochemistry , vol.47 , pp. 3474-3483
    • Doukov, T.I.1    Blasiak, L.C.2    Seravalli, J.3    Ragsdale, S.W.4    Drennan, C.L.5
  • 15
    • 0000311598 scopus 로고
    • Acetogenesis, acetogenic bacteria and the acetyl-CoA pathway: past and current perspectives
    • Chapman and Hall, H.L. Drake (Ed.)
    • Drake H.L., Daniel S.L., Matthies C., Küsel K. Acetogenesis, acetogenic bacteria and the acetyl-CoA pathway: past and current perspectives. Acetogenesis 1994, 3-60. Chapman and Hall. H.L. Drake (Ed.).
    • (1994) Acetogenesis , pp. 3-60
    • Drake, H.L.1    Daniel, S.L.2    Matthies, C.3    Küsel, K.4
  • 16
    • 0025787641 scopus 로고
    • Catalysis of acetyl-CoA cleavage and tetrahydrosarcinapterin methylation by a carbon monoxide dehydrogenase-corrinoid enzyme complex
    • Grahame D.A. Catalysis of acetyl-CoA cleavage and tetrahydrosarcinapterin methylation by a carbon monoxide dehydrogenase-corrinoid enzyme complex. J Biol Chem 1991, 266:22227-22233.
    • (1991) J Biol Chem , vol.266 , pp. 22227-22233
    • Grahame, D.A.1
  • 17
    • 0031685510 scopus 로고    scopus 로고
    • Biochemistry of methanogenesis: a tribute to Marjory Stephenson
    • Thauer R.K. Biochemistry of methanogenesis: a tribute to Marjory Stephenson. Microbiology 1998, 144:2377-2406.
    • (1998) Microbiology , vol.144 , pp. 2377-2406
    • Thauer, R.K.1
  • 18
    • 0001689934 scopus 로고    scopus 로고
    • Nickel-containing carbon monoxide dehydrogenase/acetyl-CoA synthase
    • Ragsdale S.W., Kumar M. Nickel-containing carbon monoxide dehydrogenase/acetyl-CoA synthase. Chem Rev 1996, 96:2515-2539.
    • (1996) Chem Rev , vol.96 , pp. 2515-2539
    • Ragsdale, S.W.1    Kumar, M.2
  • 20
    • 2342541642 scopus 로고    scopus 로고
    • Carbon monoxide induced decomposition of the active site [Ni-4Fe-5S] cluster of CO dehydrogenase
    • Dobbek H., Svetlitchnyi V., Liss J., Meyer O. Carbon monoxide induced decomposition of the active site [Ni-4Fe-5S] cluster of CO dehydrogenase. J Am Chem Soc 2004, 126:5382-5387.
    • (2004) J Am Chem Soc , vol.126 , pp. 5382-5387
    • Dobbek, H.1    Svetlitchnyi, V.2    Liss, J.3    Meyer, O.4
  • 21
    • 3242795754 scopus 로고    scopus 로고
    • Effect of sodium sulfide on Ni-containing carbon monoxide dehydrogenases
    • Feng J., Lindahl P.A. Effect of sodium sulfide on Ni-containing carbon monoxide dehydrogenases. J Am Chem Soc 2004, 126:9094-9100.
    • (2004) J Am Chem Soc , vol.126 , pp. 9094-9100
    • Feng, J.1    Lindahl, P.A.2
  • 22
    • 3142777049 scopus 로고    scopus 로고
    • CO-induced structural rearragement of the C cluster in Carboxydothermus hydrogenoformans CO dehydrogenase-evidence from Ni K-edge X-ray absorption spectroscopy
    • Gu W., Seravalli J., Ragsdale S.W., Cramer S.P. CO-induced structural rearragement of the C cluster in Carboxydothermus hydrogenoformans CO dehydrogenase-evidence from Ni K-edge X-ray absorption spectroscopy. Biochemistry 2004, 43:9029-9035.
    • (2004) Biochemistry , vol.43 , pp. 9029-9035
    • Gu, W.1    Seravalli, J.2    Ragsdale, S.W.3    Cramer, S.P.4
  • 23
    • 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., Lindahl P.A. Evidence for a proton transfer network and a required persulfide-bond-forming cysteine residue in Ni-containing carbon monoxide dehydrogenases. Biochemistry 2004, 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
  • 24
    • 0021111688 scopus 로고
    • Properties of purified carbon monoxide dehydrogenase from Clostridium thermoaceticum, a nickel, iron-sulfur protein
    • Ragsdale S.W., Clark J.E., Ljungdahl L.G., Lundie L.L., Drake H.L. Properties of purified carbon monoxide dehydrogenase from Clostridium thermoaceticum, a nickel, iron-sulfur protein. J Biol Chem 1983, 258:2364-2369.
    • (1983) J Biol Chem , vol.258 , pp. 2364-2369
    • Ragsdale, S.W.1    Clark, J.E.2    Ljungdahl, L.G.3    Lundie, L.L.4    Drake, H.L.5
  • 25
    • 0029731356 scopus 로고    scopus 로고
    • Unleashing hydrogenase activity in carbon monoxide dehydrogenase/acetyl-CoA synthase and pyruvate:ferredoxin oxidoreductase
    • Menon S., Ragsdale S.W. Unleashing hydrogenase activity in carbon monoxide dehydrogenase/acetyl-CoA synthase and pyruvate:ferredoxin oxidoreductase. Biochemistry 1996, 35:15814-15821.
    • (1996) Biochemistry , vol.35 , pp. 15814-15821
    • Menon, S.1    Ragsdale, S.W.2
  • 26
    • 46049094831 scopus 로고    scopus 로고
    • 2 catalyzed by carbon monoxide dehydrogenase
    • 2 catalyzed by carbon monoxide dehydrogenase. Biochemistry 2008, 47:6770-6781.
    • (2008) Biochemistry , vol.47 , pp. 6770-6781
    • Seravalli, J.1    Ragsdale, S.W.2
  • 27
    • 0027143443 scopus 로고
    • Identification of a cyanide binding site in CO dehydrogenase from Clostridium thermoaceticum using EPR and ENDOR spectroscopies
    • Anderson M.E., DeRose V.J., Hoffman B.M., Lindahl P.A. Identification of a cyanide binding site in CO dehydrogenase from Clostridium thermoaceticum using EPR and ENDOR spectroscopies. J Am Chem Soc 1993, 115:12204-12205.
    • (1993) J Am Chem Soc , vol.115 , pp. 12204-12205
    • Anderson, M.E.1    DeRose, V.J.2    Hoffman, B.M.3    Lindahl, P.A.4
  • 28
    • 0034879722 scopus 로고    scopus 로고
    • Two membrane-associated NiFeS-carbon monoxide dehydrogenases from the anaerobic carbon-monoxide-utilizing eubacterium Carboxydothermus hydrogenoformans
    • Svetlitchnyi V., Peschel C., Acker G., Meyer O. Two membrane-associated NiFeS-carbon monoxide dehydrogenases from the anaerobic carbon-monoxide-utilizing eubacterium Carboxydothermus hydrogenoformans. J Bacteriol 2001, 183:5134-5144.
    • (2001) J Bacteriol , vol.183 , pp. 5134-5144
    • Svetlitchnyi, V.1    Peschel, C.2    Acker, G.3    Meyer, O.4
  • 29
    • 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 1996, 35:8371-8390.
    • (1996) Biochemistry , vol.35 , pp. 8371-8390
    • Anderson, M.E.1    Lindahl, P.A.2
  • 30
    • 0030885194 scopus 로고    scopus 로고
    • 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., Ragsdale S.W. Mechanism of carbon monoxide oxidation by the carbon monoxide dehydrogenase/acetyl-CoA synthase from Clostridium thermoaceticum: kinetic characterization of the intermediates. Biochemistry 1997, 36:11241-11251.
    • (1997) Biochemistry , vol.36 , pp. 11241-11251
    • Seravalli, J.1    Kumar, M.2    Lu, W.-P.3    Ragsdale, S.W.4
  • 32
    • 36749053439 scopus 로고    scopus 로고
    • Carbon dioxide activation at the Ni,Fe-cluster of anaerobic carbon monoxide dehydrogenase
    • Jeoung J.-H., Dobbek H. Carbon dioxide activation at the Ni,Fe-cluster of anaerobic carbon monoxide dehydrogenase. Science 2007, 318:1461-1464.
    • (2007) Science , vol.318 , pp. 1461-1464
    • Jeoung, J.-H.1    Dobbek, H.2
  • 33
    • 68249098941 scopus 로고    scopus 로고
    • Crystallographic snapshots of cyanide- and water-bound C-clusters from bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase
    • Kung Y., Doukov T.I., Seravalli J., Ragsdale S.W., Drennan C.L. Crystallographic snapshots of cyanide- and water-bound C-clusters from bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase. Biochemistry 2009, 48:7432-7440.
    • (2009) Biochemistry , vol.48 , pp. 7432-7440
    • Kung, Y.1    Doukov, T.I.2    Seravalli, J.3    Ragsdale, S.W.4    Drennan, C.L.5
  • 35
    • 0346995022 scopus 로고    scopus 로고
    • Infrared studies of carbon monoxide binding to carbon monoxide dehydrogenase/acetyl-CoA synthase from Moorella thermoacetica
    • Chen J., Huang S., Seravalli J., Gutzma H., Swartz D.J., Ragsdale S.W., Bagley K.A. Infrared studies of carbon monoxide binding to carbon monoxide dehydrogenase/acetyl-CoA synthase from Moorella thermoacetica. Biochemistry 2003, 42:14822-14830.
    • (2003) Biochemistry , vol.42 , pp. 14822-14830
    • Chen, J.1    Huang, S.2    Seravalli, J.3    Gutzma, H.4    Swartz, D.J.5    Ragsdale, S.W.6    Bagley, K.A.7
  • 36
    • 0023654301 scopus 로고
    • Carbon monoxide dehydrogenase from Methanosarcina barkeri: disaggregation, purification, and physicochemical properties of the enzyme
    • Grahame D.A., Stadtman T.C. Carbon monoxide dehydrogenase from Methanosarcina barkeri: disaggregation, purification, and physicochemical properties of the enzyme. J Biol Chem 1987, 262:3706-3712.
    • (1987) J Biol Chem , vol.262 , pp. 3706-3712
    • Grahame, D.A.1    Stadtman, T.C.2
  • 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., Ludden P.W. 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 1989, 28:4968-4973.
    • (1989) Biochemistry , vol.28 , pp. 4968-4973
    • Ensign, S.A.1    Bonam, D.2    Ludden, P.W.3
  • 38
    • 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. Nickel-specific, slow-binding inhibition of carbon monoxide dehydrogenase from Rhodospirillum rubrum by cyanide. Biochemistry 1989, 28:4973-4979.
    • (1989) Biochemistry , vol.28 , pp. 4973-4979
    • Ensign, S.A.1    Hyman, M.R.2    Ludden, P.W.3
  • 39
    • 0028110887 scopus 로고
    • Organization of clusters and internal electron pathways in CO dehydrogenase from Clostridium thermoaceticum: relevance to the mechanism of catalysis and cyanide inhibition
    • Anderson M.E., Lindahl P.A. Organization of clusters and internal electron pathways in CO dehydrogenase from Clostridium thermoaceticum: relevance to the mechanism of catalysis and cyanide inhibition. Biochemistry 1994, 33:8702-8711.
    • (1994) Biochemistry , vol.33 , pp. 8702-8711
    • Anderson, M.E.1    Lindahl, P.A.2
  • 40
    • 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.-W., Korbas K., Klepsch M., Meyer-Klaucke W., Meyer O., Svetlitchnyi V. Interaction of potassium cyanide with the [Ni-4Fe-5S] active site cluster of CO dehydrogenase from Carboxydothermus hydrogenoformans. J Biol Chem 2007, 282:10639-10646.
    • (2007) J Biol Chem , vol.282 , pp. 10639-10646
    • Ha, S.-W.1    Korbas, K.2    Klepsch, M.3    Meyer-Klaucke, W.4    Meyer, O.5    Svetlitchnyi, V.6
  • 41
    • 67651228949 scopus 로고    scopus 로고
    • Structural basis of cyanide inhibition of Ni, Fe-containing carbon monoxide dehydrogenase
    • Jeoung J.-H., Dobbek H. Structural basis of cyanide inhibition of Ni, Fe-containing carbon monoxide dehydrogenase. J Am Chem Soc 2009, 131:9922-9923.
    • (2009) J Am Chem Soc , vol.131 , pp. 9922-9923
    • Jeoung, J.-H.1    Dobbek, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.