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Volumn 105, Issue 28, 2008, Pages 9558-9563

Structure of the α2ε2 Ni-dependent CO dehydrogenase component of the Methanosarcina barkeri acetyl-CoA decarbonylase/synthase complex

Author keywords

Acetate; Carbon dioxide; Carbon monoxide; Methanogenesis; Oxidoreductase

Indexed keywords

ACETYL COENZYME A DECARBONYLASE; ACETYL COENZYME A SYNTHASE; CARBON MONOXIDE; CARBON MONOXIDE DEHYDROGENASE; ENZYME; FERROUS SULFATE; HYDROXIDE; IRON; METHANE; NICKEL; WATER; ALDEHYDE DEHYDROGENASE; IRON SULFUR PROTEIN; MULTIENZYME COMPLEX;

EID: 47749139329     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0800415105     Document Type: Article
Times cited : (102)

References (29)
  • 1
    • 0028860434 scopus 로고
    • CO dehydrogenase
    • Ferry JG (1995) CO dehydrogenase. Annu Rev Microbiol 49:305-333.
    • (1995) Annu Rev Microbiol , vol.49 , pp. 305-333
    • Ferry, J.G.1
  • 2
    • 0022860139 scopus 로고
    • Isolation of an enzyme complex with carbon monoxide dehydrogenase activity containing corrinoid and nickel from acetate-grown Methanosarcina thermophila
    • Terlesky KC, Nelson MJ, Ferry JG (1986) Isolation of an enzyme complex with carbon monoxide dehydrogenase activity containing corrinoid and nickel from acetate-grown Methanosarcina thermophila. J Bacteriol 168:1053-1058.
    • (1986) J Bacteriol , vol.168 , pp. 1053-1058
    • Terlesky, K.C.1    Nelson, M.J.2    Ferry, J.G.3
  • 3
    • 0025787641 scopus 로고
    • Catalysis of acetyl-CoA cleavage and tetrahydrosarcinapterin methylation by a carbon monoxide dehydrogenase-corrinoid enzyme complex
    • Grahame DA (1991) Catalysis of acetyl-CoA cleavage and tetrahydrosarcinapterin methylation by a carbon monoxide dehydrogenase-corrinoid enzyme complex. J Biol Chem 266:22227-22233.
    • (1991) J Biol Chem , vol.266 , pp. 22227-22233
    • Grahame, D.A.1
  • 4
    • 0029913246 scopus 로고    scopus 로고
    • Partial reactions catalyzed by protein components of the acetyl-CoA decarbonylase synthase enzyme complex from Methanosarcina barkeri
    • Grahame DA, DeMoll E (1996) Partial reactions catalyzed by protein components of the acetyl-CoA decarbonylase synthase enzyme complex from Methanosarcina barkeri. J Biol Chem 271:8352-8358.
    • (1996) J Biol Chem , vol.271 , pp. 8352-8358
    • Grahame, D.A.1    DeMoll, E.2
  • 5
    • 0023654301 scopus 로고
    • Carbon monoxide dehydrogenase from Methanosarcina barkeri. Disaggregation, purification, and physicochemical properties of the enzyme
    • Grahame DA, Stadtman TC (1987) Carbon monoxide dehydrogenase from Methanosarcina barkeri. Disaggregation, purification, and physicochemical properties of the enzyme. J Biol Chem 262:3706-3712.
    • (1987) J Biol Chem , vol.262 , pp. 3706-3712
    • Grahame, D.A.1    Stadtman, T.C.2
  • 7
    • 0021243323 scopus 로고
    • Characterization and purification of carbon monoxide dehydrogenase from Methanosarcina barkeri
    • Krzycki JA, Zeikus JG (1984) Characterization and purification of carbon monoxide dehydrogenase from Methanosarcina barkeri. J Bacteriol 158:231-237.
    • (1984) J Bacteriol , vol.158 , pp. 231-237
    • Krzycki, J.A.1    Zeikus, J.G.2
  • 8
    • 0035902973 scopus 로고    scopus 로고
    • Crystal structure of a carbon monoxide dehydrogenase reveals a [Ni-4Fe-5S] cluster
    • Dobbek H, et al. (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
  • 9
    • 0035834117 scopus 로고    scopus 로고
    • Life on carbon monoxide: X-ray structure of Rhodospirillum rubrum Ni-Fe-S carbon monoxide dehydrogenase
    • Drennan CL, et al. (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
  • 10
    • 0037131241 scopus 로고    scopus 로고
    • A Ni-Fe-Cu center in a bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase
    • Doukov TI, et al. (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
  • 11
    • 0037374820 scopus 로고    scopus 로고
    • 4] clusters in closed and open subunits of acetyl-CoA synthase/carbon monoxide dehydrogenase
    • 4] 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
  • 12
    • 0037133256 scopus 로고    scopus 로고
    • The Ni-containing carbon monoxide dehydrogenase family: Light at the end of the tunnel?
    • Lindahl PA (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
  • 14
    • 0033572254 scopus 로고    scopus 로고
    • Structure of the Ni/Fe-S protein subcomponent of the acetyl-CoA decarbonylase/synthase complex from Methanosarcina thermophila at 26-Å resolution
    • Kocsis E, Kessel M, DeMoll E, Grahame DA (1999) Structure of the Ni/Fe-S protein subcomponent of the acetyl-CoA decarbonylase/synthase complex from Methanosarcina thermophila at 26-Å resolution. J Struct Biol 128:165-174.
    • (1999) J Struct Biol , vol.128 , pp. 165-174
    • Kocsis, E.1    Kessel, M.2    DeMoll, E.3    Grahame, D.A.4
  • 15
    • 0037458613 scopus 로고    scopus 로고
    • Nickel in subunit beta of the acetyl-CoA decarbonylase/synthase multienzyme complex in methanogens. Catalytic properties and evidence for a binuclear Ni-Ni site
    • Gencic S, Grahame DA (2003) Nickel in subunit beta of the acetyl-CoA decarbonylase/synthase multienzyme complex in methanogens. Catalytic properties and evidence for a binuclear Ni-Ni site. J Biol Chem 278:6101-6110.
    • (2003) J Biol Chem , vol.278 , pp. 6101-6110
    • Gencic, S.1    Grahame, D.A.2
  • 16
    • 33746093231 scopus 로고    scopus 로고
    • Support for nickel as the labile metal in the A-center of the M. barkeri acetyl-CoA decarbonylase/synthase complex
    • Arndt JW, et al. (2004) Support for nickel as the labile metal in the A-center of the M. barkeri acetyl-CoA decarbonylase/synthase complex. J Chin Chem Soc 51:1253-1258.
    • (2004) J Chin Chem Soc , vol.51 , pp. 1253-1258
    • Arndt, J.W.1
  • 17
    • 0026317878 scopus 로고
    • Resolution of component proteins in an enzyme complex from Methanosarcina thermophila catalyzing the synthesis or cleavage of acetyl-CoA
    • Abbanat DR, Ferry JG (1991) Resolution of component proteins in an enzyme complex from Methanosarcina thermophila catalyzing the synthesis or cleavage of acetyl-CoA. Proc Natl Acad Sci USA 88:3272-3276.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 3272-3276
    • Abbanat, D.R.1    Ferry, J.G.2
  • 18
    • 33749267810 scopus 로고    scopus 로고
    • Structural insights into methyltransfer reactions of a corrinoid iron-sulfur protein involved in acetyl-CoA synthesis
    • Svetlitchnaia T, Svetlitchnyi V, Meyer O, Dobbek H (2006) Structural insights into methyltransfer reactions of a corrinoid iron-sulfur protein involved in acetyl-CoA synthesis. Proc Natl Acad Sci USA 103:14331-14336.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 14331-14336
    • Svetlitchnaia, T.1    Svetlitchnyi, V.2    Meyer, O.3    Dobbek, H.4
  • 19
    • 0034832032 scopus 로고    scopus 로고
    • The evolution of acetyl-CoA synthase
    • Lindahl PA, Chang B (2001) The evolution of acetyl-CoA synthase. Orig Life Evol Biosph 31:403-434.
    • (2001) Orig Life Evol Biosph , vol.31 , pp. 403-434
    • Lindahl, P.A.1    Chang, B.2
  • 20
    • 0031865006 scopus 로고    scopus 로고
    • Touring protein fold space with Dali/FSSP
    • Holm L, Sander C (1998) Touring protein fold space with Dali/FSSP. Nucleic Acids Res 26:316-319.
    • (1998) Nucleic Acids Res , vol.26 , pp. 316-319
    • Holm, L.1    Sander, C.2
  • 21
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: A new generation of protein database search programs
    • Altschul SF, et al. (1997) Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res 25:3389-3402.
    • (1997) Nucleic Acids Res , vol.25 , pp. 3389-3402
    • Altschul, S.F.1
  • 22
    • 0347717810 scopus 로고    scopus 로고
    • The crystal structures of Klebsiella pneumoniae acetolactate synthase with enzyme-bound cofactor and with an unusual intermediate
    • Pang SS, Duggleby RG, Schowen RL, Guddat LW (2004) The crystal structures of Klebsiella pneumoniae acetolactate synthase with enzyme-bound cofactor and with an unusual intermediate. J Biol Chem 279:2242-2253.
    • (2004) J Biol Chem , vol.279 , pp. 2242-2253
    • Pang, S.S.1    Duggleby, R.G.2    Schowen, R.L.3    Guddat, L.W.4
  • 23
    • 0028296918 scopus 로고
    • The refined structures of a stabilized mutant and of wild-type pyruvate oxidase from Lactobacillus plantarum
    • Muller YA, Schumacher G, Rudolph R, Schulz GE (1994) The refined structures of a stabilized mutant and of wild-type pyruvate oxidase from Lactobacillus plantarum. J Mol Biol 237:315-335.
    • (1994) J Mol Biol , vol.237 , pp. 315-335
    • Muller, Y.A.1    Schumacher, G.2    Rudolph, R.3    Schulz, G.E.4
  • 24
    • 0027479683 scopus 로고
    • Structure of the thiamine- and flavin-dependent enzyme pyruvate oxidase
    • Muller YA, Schulz GE (1993) Structure of the thiamine- and flavin-dependent enzyme pyruvate oxidase. Science 259:965-967.
    • (1993) Science , vol.259 , pp. 965-967
    • Muller, Y.A.1    Schulz, G.E.2
  • 25
    • 3242795754 scopus 로고    scopus 로고
    • Effect of sodium sulfide on Ni-containing carbon monoxide dehydrogenases
    • Feng J, Lindahl PA (2004) Effect of sodium sulfide on Ni-containing carbon monoxide dehydrogenases. J Am Chem Soc 126:9094-9100.
    • (2004) J Am Chem Soc , vol.126 , pp. 9094-9100
    • Feng, J.1    Lindahl, P.A.2
  • 26
    • 36749053439 scopus 로고    scopus 로고
    • Carbon dioxide activation at the Ni,Fe-cluster of anaerobic carbon monoxide dehydrogenase
    • Jeoung JH, 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
  • 27
    • 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 EJ, Feng J, Bramlett MR, Lindahl PA (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
  • 28
    • 0034666137 scopus 로고    scopus 로고
    • The role of pyruvate ferredoxin oxidoreductase in pyruvate synthesis during autotrophic growth by the Wood-Ljungdahl pathway
    • Furdui C, Ragsdale SW (2000) The role of pyruvate ferredoxin oxidoreductase in pyruvate synthesis during autotrophic growth by the Wood-Ljungdahl pathway. J Biol Chem 275:28494-28499.
    • (2000) J Biol Chem , vol.275 , pp. 28494-28499
    • Furdui, C.1    Ragsdale, S.W.2
  • 29
    • 0024961972 scopus 로고
    • Paramagnetic centers of carbon monoxide dehydrogenase from aceticlastic Methanosarcina barkeri
    • Krzycki JA, Mortenson LE, Prince RC (1989) Paramagnetic centers of carbon monoxide dehydrogenase from aceticlastic Methanosarcina barkeri. J Biol Chem 264:7217-7221.
    • (1989) J Biol Chem , vol.264 , pp. 7217-7221
    • Krzycki, J.A.1    Mortenson, L.E.2    Prince, R.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.