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Volumn 8, Issue 6, 2005, Pages 643-648

Methyl-coenzyme M reductase and the anaerobic oxidation of methane in methanotrophic Archaea

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; METHANE; METHYL COENZYME M REDUCTASE; UNCLASSIFIED DRUG;

EID: 27844544240     PISSN: 13695274     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mib.2005.10.002     Document Type: Review
Times cited : (130)

References (51)
  • 1
    • 0034548842 scopus 로고    scopus 로고
    • New perspectives on anaerobic methane oxidation
    • D.L. Valentine, and W.S. Reeburgh New perspectives on anaerobic methane oxidation Environ Microbiol 2 2000 477 484
    • (2000) Environ Microbiol , vol.2 , pp. 477-484
    • Valentine, D.L.1    Reeburgh, W.S.2
  • 2
    • 9244252034 scopus 로고    scopus 로고
    • Anaerobic oxidation of methane and ammonium
    • M. Strous, and Jetten MSM Anaerobic oxidation of methane and ammonium Annu Rev Microbiol 58 2004 99 117
    • (2004) Annu Rev Microbiol , vol.58 , pp. 99-117
    • Strous, M.1    Msm, J.2
  • 3
    • 0036417909 scopus 로고    scopus 로고
    • Biogeochemistry and microbial ecology of methane oxidation in anoxic environments: A review
    • D.L. Valentine Biogeochemistry and microbial ecology of methane oxidation in anoxic environments: a review Antonie Van Leeuwenhoek 81 2002 271 282
    • (2002) Antonie Van Leeuwenhoek , vol.81 , pp. 271-282
    • Valentine, D.L.1
  • 4
    • 2142766873 scopus 로고    scopus 로고
    • Hydrate Ridge: A natural laboratory for the study of microbial life fueled by methane from near-surface gas hydrates
    • A. Boetius, and E. Suess Hydrate Ridge: a natural laboratory for the study of microbial life fueled by methane from near-surface gas hydrates Chem Geol 205 2004 291 310
    • (2004) Chem Geol , vol.205 , pp. 291-310
    • Boetius, A.1    Suess, E.2
  • 5
    • 0141815960 scopus 로고    scopus 로고
    • Growth and methane oxidation rates of anaerobic methanotrophic archaea in a continuous-flow bioreactor
    • P.R. Girguis, V.J. Orphan, S.J. Hallam, and E.F. DeLong Growth and methane oxidation rates of anaerobic methanotrophic archaea in a continuous-flow bioreactor Appl Environ Microbiol 69 2003 5472 5482
    • (2003) Appl Environ Microbiol , vol.69 , pp. 5472-5482
    • Girguis, P.R.1    Orphan, V.J.2    Hallam, S.J.3    Delong, E.F.4
  • 8
    • 0035919654 scopus 로고    scopus 로고
    • Methane-consuming archaea revealed by directly coupled isotopic and phylogenetic analysis
    • V.J. Orphan, C.H. House, K.U. Hinrichs, K.D. McKeegan, and E.F. DeLong Methane-consuming archaea revealed by directly coupled isotopic and phylogenetic analysis Science 293 2001 484 487
    • (2001) Science , vol.293 , pp. 484-487
    • Orphan, V.J.1    House, C.H.2    Hinrichs, K.U.3    McKeegan, K.D.4    Delong, E.F.5
  • 13
    • 0141447278 scopus 로고    scopus 로고
    • Characterization of specific membrane fatty acids as chemotaxonomic markers for sulfate-reducing bacteria involved in anaerobic oxidation of methane
    • M. Elvert, A. Boetius, K. Knittel, and B.B. Jørgensen Characterization of specific membrane fatty acids as chemotaxonomic markers for sulfate-reducing bacteria involved in anaerobic oxidation of methane Geomicrobiol J 20 2003 403 419
    • (2003) Geomicrobiol J , vol.20 , pp. 403-419
    • Elvert, M.1    Boetius, A.2    Knittel, K.3    Jørgensen, B.B.4
  • 14
    • 0141447287 scopus 로고    scopus 로고
    • Activity, distribution, and diversity of sulfate reducers and other bacteria in sediments above gas hydrate (Cascadia margin, Oregon)
    • K. Knittel, A. Boetius, A. Lemke, H. Eilers, K. Lochte, O. Pfannkuche, P. Linke, and R. Amann Activity, distribution, and diversity of sulfate reducers and other bacteria in sediments above gas hydrate (Cascadia margin, Oregon) Geomicrobiol J 20 2003 269 294
    • (2003) Geomicrobiol J , vol.20 , pp. 269-294
    • Knittel, K.1    Boetius, A.2    Lemke, A.3    Eilers, H.4    Lochte, K.5    Pfannkuche, O.6    Linke, P.7    Amann, R.8
  • 15
    • 0036045379 scopus 로고    scopus 로고
    • In vitro demonstration of anaerobic oxidation of methane coupled to sulphate reduction in sediment from a marine gas hydrate area
    • K. Nauhaus, A. Boetius, M. Krüger, and F. Widdel In vitro demonstration of anaerobic oxidation of methane coupled to sulphate reduction in sediment from a marine gas hydrate area Environ Microbiol 4 2002 296 305
    • (2002) Environ Microbiol , vol.4 , pp. 296-305
    • Nauhaus, K.1    Boetius, A.2    Krüger, M.3    Widdel, F.4
  • 16
    • 0035675972 scopus 로고    scopus 로고
    • Apparent minimum free energy requirements for methanogenic Archaea and sulfate-reducing bacteria in an anoxic marine sediment
    • T.M. Hoehler, M.J. Alperin, D.B. Albert, and C.S. Martens Apparent minimum free energy requirements for methanogenic Archaea and sulfate-reducing bacteria in an anoxic marine sediment FEMS Microbiol Ecol 38 2001 33 41
    • (2001) FEMS Microbiol Ecol , vol.38 , pp. 33-41
    • Hoehler, T.M.1    Alperin, M.J.2    Albert, D.B.3    Martens, C.S.4
  • 18
    • 0141592799 scopus 로고    scopus 로고
    • Identification of methyl coenzyme M reductase a (mcrA) genes associated with methane-oxidizing archaea
    • S.J. Hallam, P.R. Girguis, C.M. Preston, P.M. Richardson, and E.F. DeLong Identification of methyl coenzyme M reductase A (mcrA) genes associated with methane-oxidizing archaea Appl Environ Microbiol 69 2003 5483 5491
    • (2003) Appl Environ Microbiol , vol.69 , pp. 5483-5491
    • Hallam, S.J.1    Girguis, P.R.2    Preston, C.M.3    Richardson, P.M.4    Delong, E.F.5
  • 20
    • 10444248885 scopus 로고    scopus 로고
    • Characterization of C1-metabolizing prokaryotic communities in methane seep habitats at the Kuroshima Knoll, southern Ryukyu Arc, by analyzing pmoA, mmoX, mxaF, mcrA, and 16S rRNA genes
    • F. Inagaki, U. Tsunogai, M. Suzuki, A. Kosaka, H. Machiyama, K. Takai, T. Nunoura, K.H. Nealson, and K. Horikoshi Characterization of C1-metabolizing prokaryotic communities in methane seep habitats at the Kuroshima Knoll, southern Ryukyu Arc, by analyzing pmoA, mmoX, mxaF, mcrA, and 16S rRNA genes Appl Environ Microbiol 70 2004 7445 7455
    • (2004) Appl Environ Microbiol , vol.70 , pp. 7445-7455
    • Inagaki, F.1    Tsunogai, U.2    Suzuki, M.3    Kosaka, A.4    MacHiyama, H.5    Takai, K.6    Nunoura, T.7    Nealson, K.H.8    Horikoshi, K.9
  • 21
    • 14844340576 scopus 로고    scopus 로고
    • A genomic view of methane oxidation by aerobic bacteria and anaerobic archaea
    • L. Chistoserdova, J.A. Vorholt, and M.E. Lidstrom A genomic view of methane oxidation by aerobic bacteria and anaerobic archaea Genome Biol 6 2005 208.1 208.6
    • (2005) Genome Biol , vol.6 , pp. 2081-2086
    • Chistoserdova, L.1    Vorholt, J.A.2    Lidstrom, M.E.3
  • 22
    • 4644265740 scopus 로고    scopus 로고
    • Probing the reactivity of Ni in the active site of methyl-coenzyme M reductase with substrate analogues
    • M. Goenrich, F. Mahlert, E.C. Duin, C. Bauer, B. Jaun, and R.K. Thauer Probing the reactivity of Ni in the active site of methyl-coenzyme M reductase with substrate analogues J Biol Inorg Chem 9 2004 691 705 In this study, the inactivation of methyl-coenzyme M reductase by bromoethane sulfonate and other substrate analogues is described.
    • (2004) J Biol Inorg Chem , vol.9 , pp. 691-705
    • Goenrich, M.1    Mahlert, F.2    Duin, E.C.3    Bauer, C.4    Jaun, B.5    Thauer, R.K.6
  • 25
    • 0031685510 scopus 로고    scopus 로고
    • Biochemistry of methanogenesis: A tribute to Marjory Stephenson
    • R.K. Thauer Biochemistry of methanogenesis: a tribute to Marjory Stephenson Microbiology 144 1998 2377 2406
    • (1998) Microbiology , vol.144 , pp. 2377-2406
    • Thauer, R.K.1
  • 26
    • 0030726657 scopus 로고    scopus 로고
    • Crystal structure of methyl-coenzyme M reductase: The key enzyme of biological methane formation
    • U. Ermler, W. Grabarse, S. Shima, M. Goubeaud, and R.K. Thauer Crystal structure of methyl-coenzyme M reductase: the key enzyme of biological methane formation Science 278 1997 1457 1462
    • (1997) Science , vol.278 , pp. 1457-1462
    • Ermler, U.1    Grabarse, W.2    Shima, S.3    Goubeaud, M.4    Thauer, R.K.5
  • 27
    • 0034692923 scopus 로고    scopus 로고
    • Comparison of three methyl-coenzyme M reductases from phylogenetically distant organisms: Unusual amino acid modification, conservation and adaptation
    • W. Grabarse, F. Mahlert, S. Shima, R.K. Thauer, and U. Ermler Comparison of three methyl-coenzyme M reductases from phylogenetically distant organisms: unusual amino acid modification, conservation and adaptation J Mol Biol 303 2000 329 344
    • (2000) J Mol Biol , vol.303 , pp. 329-344
    • Grabarse, W.1    Mahlert, F.2    Shima, S.3    Thauer, R.K.4    Ermler, U.5
  • 28
    • 0035946914 scopus 로고    scopus 로고
    • On the mechanism of biological methane formation: Structural evidence for conformational changes in methyl-coenzyme M reductase upon substrate binding
    • W. Grabarse, F. Mahlert, E.C. Duin, M. Goubeaud, S. Shima, R.K. Thauer, V. Lamzin, and U. Ermler On the mechanism of biological methane formation: structural evidence for conformational changes in methyl-coenzyme M reductase upon substrate binding J Mol Biol 309 2001 315 330
    • (2001) J Mol Biol , vol.309 , pp. 315-330
    • Grabarse, W.1    Mahlert, F.2    Duin, E.C.3    Goubeaud, M.4    Shima, S.5    Thauer, R.K.6    Lamzin, V.7    Ermler, U.8
  • 30
    • 0034635543 scopus 로고    scopus 로고
    • The biosynthesis of methylated amino acids in the active site region of methyl-coenzyme M reductase
    • T. Selmer, J. Kahnt, M. Goubeaud, S. Shima, W. Grabarse, U. Ermler, and R.K. Thauer The biosynthesis of methylated amino acids in the active site region of methyl-coenzyme M reductase J Biol Chem 275 2000 3755 3760
    • (2000) J Biol Chem , vol.275 , pp. 3755-3760
    • Selmer, T.1    Kahnt, J.2    Goubeaud, M.3    Shima, S.4    Grabarse, W.5    Ermler, U.6    Thauer, R.K.7
  • 31
    • 21644433865 scopus 로고    scopus 로고
    • Temperature dependence of methyl-coenzyme M reductase activity and of the formation of the methyl-coenzyme M reductase red2 state induced by coenzyme B
    • M. Goenrich, E.C. Duin, F. Mahlert, and R.K. Thauer Temperature dependence of methyl-coenzyme M reductase activity and of the formation of the methyl-coenzyme M reductase red2 state induced by coenzyme B J Biol Inorg Chem 10 2005 333 342 Evidence is presented that the two active sites of MCR are structurally and functionally interlinked and that the enzyme could have a dual-stroke engine like mechanism.
    • (2005) J Biol Inorg Chem , vol.10 , pp. 333-342
    • Goenrich, M.1    Duin, E.C.2    Mahlert, F.3    Thauer, R.K.4
  • 32
    • 0037032248 scopus 로고    scopus 로고
    • X-ray absorption and resonance Raman studies of methyl-coenzyme M reductase indicating that ligand exchange and macrocycle reduction accompany reductive activation
    • Q. Tang, P.E. Carrington, Y.C. Horng, M.J. Maroney, S.W. Ragsdale, and D.F. Bocian X-ray absorption and resonance Raman studies of methyl-coenzyme M reductase indicating that ligand exchange and macrocycle reduction accompany reductive activation J Am Chem Soc 124 2002 13242 13256
    • (2002) J Am Chem Soc , vol.124 , pp. 13242-13256
    • Tang, Q.1    Carrington, P.E.2    Horng, Y.C.3    Maroney, M.J.4    Ragsdale, S.W.5    Bocian, D.F.6
  • 33
    • 0142214613 scopus 로고    scopus 로고
    • red1 state of methyl-coenzyme M reductase
    • red1 state of methyl-coenzyme M reductase J Am Chem Soc 125 2003 13120 13125
    • (2003) J Am Chem Soc , vol.125 , pp. 13120-13125
    • Piskorski, R.1    Jaun, B.2
  • 35
    • 0036943599 scopus 로고    scopus 로고
    • The nickel enzyme methyl-coenzyme M reductase from methanogenic archaea: In vitro induction of the nickel-based MCR-ox EPR signals from MCR-red2
    • F. Mahlert, C. Bauer, B. Jaun, R.K. Thauer, and E.C. Duin The nickel enzyme methyl-coenzyme M reductase from methanogenic archaea: in vitro induction of the nickel-based MCR-ox EPR signals from MCR-red2 J Biol Inorg Chem 7 2002 500 513
    • (2002) J Biol Inorg Chem , vol.7 , pp. 500-513
    • Mahlert, F.1    Bauer, C.2    Jaun, B.3    Thauer, R.K.4    Duin, E.C.5
  • 36
    • 0034639453 scopus 로고    scopus 로고
    • On the assignment of nickel oxidation states of the Ox1, Ox2 forms of methyl-coenzyme M reductase
    • J. Telser, Y.C. Horng, D.F. Becker, B.M. Hoffman, and S.W. Ragsdale On the assignment of nickel oxidation states of the Ox1, Ox2 forms of methyl-coenzyme M reductase J Am Chem Soc 122 2000 182 183
    • (2000) J Am Chem Soc , vol.122 , pp. 182-183
    • Telser, J.1    Horng, Y.C.2    Becker, D.F.3    Hoffman, B.M.4    Ragsdale, S.W.5
  • 41
    • 0037123266 scopus 로고    scopus 로고
    • A mechanism from quantum chemical studies for methane formation in methanogenesis
    • V. Pelmenschikov, M.R. Blomberg, P.E. Siegbahn, and R.H. Crabtree A mechanism from quantum chemical studies for methane formation in methanogenesis J Am Chem Soc 124 2002 4039 4049
    • (2002) J Am Chem Soc , vol.124 , pp. 4039-4049
    • Pelmenschikov, V.1    Blomberg, M.R.2    Siegbahn, P.E.3    Crabtree, R.H.4
  • 42
    • 0042155695 scopus 로고    scopus 로고
    • Catalysis by methyl-coenzyme M reductase: A theoretical study for heterodisulfide product formation
    • V. Pelmenschikov, and P.E. Siegbahn Catalysis by methyl-coenzyme M reductase: a theoretical study for heterodisulfide product formation J Biol Inorg Chem 8 2003 653 662
    • (2003) J Biol Inorg Chem , vol.8 , pp. 653-662
    • Pelmenschikov, V.1    Siegbahn, P.E.2
  • 43
    • 0001159545 scopus 로고
    • 430
    • Edited by Sigel H, Sigel A. Marcel Dekker; Properties of Metal Alkyl Derivatives.
    • 430. In Metal Ions in Biological Systems. Edited by Sigel H, Sigel A. Marcel Dekker; 1993:287-337. vol 29, Properties of Metal Alkyl Derivatives.
    • (1993) Metal Ions in Biological Systems , vol.29 , pp. 287-337
    • Jaun, B.1
  • 44
    • 0012233552 scopus 로고    scopus 로고
    • Activation of CH bonds by metal complexes
    • A.E. Shilov, and G.B. Shul'pin Activation of CH bonds by metal complexes Chem Rev 97 2005 2879 2932
    • (2005) Chem Rev , vol.97 , pp. 2879-2932
    • Shilov, A.E.1    Shul'Pin, G.B.2
  • 45
    • 20144385037 scopus 로고    scopus 로고
    • Trace methane oxidation studied in several Euryarchaeota under diverse conditions
    • J.J. Moran, C.H. House, K.H. Freeman, and J.G. Ferry Trace methane oxidation studied in several Euryarchaeota under diverse conditions Archaea 1 2005 303 309
    • (2005) Archaea , vol.1 , pp. 303-309
    • Moran, J.J.1    House, C.H.2    Freeman, K.H.3    Ferry, J.G.4
  • 46
  • 47
    • 0037419007 scopus 로고    scopus 로고
    • Redox potentials of methanophenazine and CoB-S-S-CoM, factors involved in electron transport in Methanogenic archaea
    • M. Tietze, A. Beuchle, I. Lamla, N. Orth, M. Dehler, G. Greiner, and U. Beifuss Redox potentials of methanophenazine and CoB-S-S-CoM, factors involved in electron transport in Methanogenic archaea ChemBioChem 4 2003 333 335
    • (2003) ChemBioChem , vol.4 , pp. 333-335
    • Tietze, M.1    Beuchle, A.2    Lamla, I.3    Orth, N.4    Dehler, M.5    Greiner, G.6    Beifuss, U.7
  • 48
    • 1642523198 scopus 로고    scopus 로고
    • Anaerobic oxidation of methane above gas hydrates at hydrate ridge, NE Pacific Ocean
    • T. Treude, A. Boetius, K. Knittel, K. Wallmann, and B.B. Jørgensen Anaerobic oxidation of methane above gas hydrates at hydrate ridge, NE Pacific Ocean Mar Ecol Prog Ser 264 2003 1 14
    • (2003) Mar Ecol Prog Ser , vol.264 , pp. 1-14
    • Treude, T.1    Boetius, A.2    Knittel, K.3    Wallmann, K.4    Jørgensen, B.B.5
  • 50
    • 2142705248 scopus 로고    scopus 로고
    • Life at the edge of methane ice: Microbial cycling of carbon and sulfur in Gulf of Mexico gas hydrates
    • B.N. Orcutt, A. Boetius, S.K. Lugo, I.R. MacDonal, V.A. Samarkin, and S.B. Joye Life at the edge of methane ice: microbial cycling of carbon and sulfur in Gulf of Mexico gas hydrates Chem Geol 205 2004 239 251
    • (2004) Chem Geol , vol.205 , pp. 239-251
    • Orcutt, B.N.1    Boetius, A.2    Lugo, S.K.3    MacDonal, I.R.4    Samarkin, V.A.5    Joye, S.B.6


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