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Volumn 497, Issue 7447, 2013, Pages 132-136

The catalytic mechanism for aerobic formation of methane by bacteria

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSYLMETHIONINE LEVO METHIONINE; HYDROGEN; LYASE; METHANE; UNCLASSIFIED DRUG;

EID: 84877584386     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature12061     Document Type: Article
Times cited : (83)

References (22)
  • 1
    • 33847720244 scopus 로고    scopus 로고
    • Ocean methane biogeochemistry
    • Reeburgh, W. S. Ocean methane biogeochemistry. Chem. Rev. 107, 486-513 (2007).
    • (2007) Chem. Rev , vol.107 , pp. 486-513
    • Reeburgh, W.S.1
  • 2
    • 50149109783 scopus 로고    scopus 로고
    • Aerobic production of methane in the sea
    • Karl, D. M. et al. Aerobic production of methane in the sea. Nature Geosci. 1, 473-478 (2008).
    • (2008) Nature Geosci , vol.1 , pp. 473-478
    • Karl, D.M.1
  • 3
    • 84865535718 scopus 로고    scopus 로고
    • Synthesis of methylphosphonic acid by marine microbes: A source of methane in the aerobic ocean
    • Metcalf, W. W. et al. Synthesis of methylphosphonic acid by marine microbes: a source of methane in the aerobic ocean. Science 337, 1104-1107 (2012).
    • (2012) Science , vol.337 , pp. 1104-1107
    • Metcalf, W.W.1
  • 4
    • 0023101749 scopus 로고
    • Bacterial carbonphosphorus lyase: Production, ratesandregulationofphosphonicandphosphinic acid metabolism
    • Wackett, L. P., Shames, S. L., Venditti, C. P. & Walsh, C. T. Bacterial carbonphosphorus lyase: production, ratesandregulationofphosphonicandphosphinic acid metabolism. J. Bacteriol. 169, 710-717 (1987).
    • (1987) J. Bacteriol , vol.169 , pp. 710-717
    • Wackett, L.P.1    Shames, S.L.2    Venditti, C.P.3    Walsh, C.T.4
  • 5
    • 0023110479 scopus 로고
    • Radical-based dephosphorylation and organophosphonate biodegradation
    • Frost, J. W., Loo, S., Cordiero, M. & Li, D. Radical-based dephosphorylation and organophosphonate biodegradation. J. Am. Chem. Soc. 109, 2166-2171 (1987).
    • (1987) J. Am. Chem. Soc , vol.109 , pp. 2166-2171
    • Frost, J.W.1    Loo, S.2    Cordiero, M.3    Li, D.4
  • 6
    • 0023250677 scopus 로고
    • Involvement of the phosphate regulon and the psiD locus in the carbon-phosphorus lyase activity of Escherichia coli K-12
    • Wackett, L. P., Wanner, B. L., Venditti, C. P. & Walsh, C. T. Involvement of the phosphate regulon and the psiD locus in the carbon-phosphorus lyase activity of Escherichia coli K-12. J. Bacteriol. 169, 1753-1756 (1987).
    • (1987) J. Bacteriol , vol.169 , pp. 1753-1756
    • Wackett, L.P.1    Wanner, B.L.2    Venditti, C.P.3    Walsh, C.T.4
  • 7
    • 0027262172 scopus 로고
    • Mutational analysis of an Escherichia coli fourteengene operon for phosphonate degradation using TnphoA' elements
    • Metcalf, W. W. & Wanner, B. L. Mutational analysis of an Escherichia coli fourteengene operon for phosphonate degradation using TnphoA' elements. J. Bacteriol. 175, 3430-3442 (1993).
    • (1993) J. Bacteriol , vol.175 , pp. 3430-3442
    • Metcalf, W.W.1    Wanner, B.L.2
  • 8
    • 84355162021 scopus 로고    scopus 로고
    • Intermediates in the transformation of phosphonates to phosphate by bacteria
    • Kamat, S. S., Williams, H. J. & Raushel, F. M. Intermediates in the transformation of phosphonates to phosphate by bacteria. Nature 480, 570-573 (2011).
    • (2011) Nature , vol.480 , pp. 570-573
    • Kamat, S.S.1    Williams, H.J.2    Raushel, F.M.3
  • 9
    • 4644229658 scopus 로고    scopus 로고
    • Escherichia coli lipoyl synthase binds two distinct [4Fe-4S] clusters per polypeptide
    • Cicchillo, R. M. et al. Escherichia coli lipoyl synthase binds two distinct [4Fe-4S] clusters per polypeptide. Biochemistry 43, 11770-11781 (2004).
    • (2004) Biochemistry , vol.43 , pp. 11770-11781
    • Cicchillo, R.M.1
  • 10
    • 19744378992 scopus 로고    scopus 로고
    • Escherichia coli quinolinate synthetase does indeed harbor a [4Fe-4S] cluster
    • Cicchillo, R. M. et al. Escherichia coli quinolinate synthetase does indeed harbor a [4Fe-4S] cluster. J. Am. Chem. Soc. 127, 7310-7311 (2005).
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 7310-7311
    • Cicchillo, R.M.1
  • 11
    • 73649096195 scopus 로고    scopus 로고
    • Identification and characterization of a novel member of the radical AdoMet enzyme superfamily and implications for the biosynthesis of the Hmd hydrogenase active site cofactor
    • McGlynn, S. E. et al. Identification and characterization of a novel member of the radical AdoMet enzyme superfamily and implications for the biosynthesis of the Hmd hydrogenase active site cofactor. J. Bacteriol. 192, 595-598 (2010).
    • (2010) J. Bacteriol , vol.192 , pp. 595-598
    • McGlynn, S.E.1
  • 12
    • 77953723343 scopus 로고    scopus 로고
    • Diphthamide biosynthesis requires an organic radical generated by an iron-sulphur enzyme
    • Zhang, Y. et al. Diphthamide biosynthesis requires an organic radical generated by an iron-sulphur enzyme. Nature 465, 891-896 (2010).
    • (2010) Nature , vol.465 , pp. 891-896
    • Zhang, Y.1
  • 13
    • 0035282866 scopus 로고    scopus 로고
    • Radical SAM, a novel superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: Functional characterization using new analysis and information visual methods
    • Sofia, H. J.,Chen, G.,Hetzler, B. G., Reyes-Spindola, J. F.&Miller, N. E.RadicalSAM, a novel superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: functional characterization using new analysis and information visual methods. Nucleic Acids Res. 29, 1097-1106 (2001).
    • (2001) Nucleic Acids Res , vol.29 , pp. 1097-1106
    • Sofia, H.J.1    Chen, G.2    Hetzler, B.G.3    Reyes-Spindola, J.F.4    Miller, N.E.5
  • 15
    • 77955076779 scopus 로고    scopus 로고
    • Mechanistic and functional versatility of radical SAM enzymes
    • Booker, S. J. & Grove, T. L. Mechanistic and functional versatility of radical SAM enzymes. F1000 Biol. Rep. 2, 52 (2010).
    • (2010) F1000 Biol. Rep , vol.2 , pp. 52
    • Booker, S.J.1    Grove, T.L.2
  • 16
    • 0033571352 scopus 로고    scopus 로고
    • Glycyl radical enzymes: A conservative structural basis for radicals
    • Eklund, H. & Fontecave, M. Glycyl radical enzymes: a conservative structural basis for radicals. Structure 7, R257-R262 (1999).
    • (1999) Structure , vol.7
    • Eklund, H.1    Fontecave, M.2
  • 17
    • 0033525599 scopus 로고    scopus 로고
    • A glycyl radical site in the crystal structure of a class III ribonucleotide reductase
    • Logan, D. T., Andersson, J., Sjoberg, B. M. & Nordlund, P. A glycyl radical site in the crystal structure of a class III ribonucleotide reductase. Science 283, 1499-1504 (1999).
    • (1999) Science , vol.283 , pp. 1499-1504
    • Logan, D.T.1    Andersson, J.2    Sjoberg, B.M.3    Nordlund, P.4
  • 18
    • 0032851377 scopus 로고    scopus 로고
    • Structure and mechanism of the glycyl radical enzyme pyruvate formate-lyase
    • Becker, A. et al. Structure and mechanism of the glycyl radical enzyme pyruvate formate-lyase. Nature Struct. Biol. 6, 969-975 (1999).
    • (1999) Nature Struct. Biol , vol.6 , pp. 969-975
    • Becker, A.1
  • 19
    • 55849139092 scopus 로고    scopus 로고
    • Structural basis for glycyl radical formation by pyruvate formatelyase activating enzyme
    • Vey, J. L. et al. Structural basis for glycyl radical formation by pyruvate formatelyase activating enzyme. Proc. Natl Acad. Sci. USA 105, 16137-16141 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 16137-16141
    • Vey, J.L.1
  • 20
    • 34547742504 scopus 로고    scopus 로고
    • Characterization of a phosphodiesterase capable of hydrolyzing EA 2192, the most toxic degradation product of the nerve agent VX
    • Ghanem, E., Li, Y., Xu, C. & Raushel, F. M. Characterization of a phosphodiesterase capable of hydrolyzing EA 2192, the most toxic degradation product of the nerve agent VX. Biochemistry 46, 9032-9040 (2007).
    • (2007) Biochemistry , vol.46 , pp. 9032-9040
    • Ghanem, E.1    Li, Y.2    Xu, C.3    Raushel, F.M.4
  • 21
    • 0028275314 scopus 로고
    • Adenosyl methionine-dependent synthesis of the glycyl radical in pyruvate formate-lyase by abstraction of the glycine C-2 pro-S hydrogen atom
    • Frey, M., Rothe, M., Wagner, A. F. V. & Knappe, J. Adenosyl methionine-dependent synthesis of the glycyl radical in pyruvate formate-lyase by abstraction of the glycine C-2 pro-S hydrogen atom. J. Biol. Chem. 269, 12432-12437 (1994).
    • (1994) J. Biol. Chem , vol.269 , pp. 12432-12437
    • Frey, M.1    Rothe, M.2    Wagner, A.F.V.3    Knappe, J.4
  • 22
    • 0030028971 scopus 로고    scopus 로고
    • Thiyl radicals in ribonucleotide reductases
    • Licht, S., Garfen, G. J. & Stubbe, J. Thiyl radicals in ribonucleotide reductases. Science 271, 477-481 (1996).
    • (1996) Science , vol.271 , pp. 477-481
    • Licht, S.1    Garfen, G.J.2    Stubbe, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.