메뉴 건너뛰기




Volumn 494, Issue , 2011, Pages 159-187

Methyl-coenzyme M reductase from Methanothermobacter marburgensis

Author keywords

[No Author keywords available]

Indexed keywords

METHANE; METHYL COENZYME M REDUCTASE; OXIDOREDUCTASE; UNCLASSIFIED DRUG;

EID: 79952602650     PISSN: 00766879     EISSN: None     Source Type: Book Series    
DOI: 10.1016/B978-0-12-385112-3.00009-3     Document Type: Chapter
Times cited : (10)

References (36)
  • 3
    • 0032562134 scopus 로고    scopus 로고
    • Activation of methyl-SCoM reductase to high specific activity after treatment of whole cells with sodium sulfide
    • DOI 10.1021/bi972145x
    • D.F. Becker, and S.W. Ragsdale Activation of methyl-SCoM reductase to high specific activity after treatment of whole cells with sodium sulfide Biochemistry 37 1998 2639 2647 (Pubitemid 28119341)
    • (1998) Biochemistry , vol.37 , Issue.8 , pp. 2639-2647
    • Becker, D.F.1    Ragsdale, S.W.2
  • 4
    • 0018169292 scopus 로고
    • EPR spectroscopy of components of the mitochondrial electron-transfer system
    • H. Beinert EPR spectroscopy of components of the mitochondrial electron-transfer system Methods Enzymol. 54 1978 133 150
    • (1978) Methods Enzymol. , vol.54 , pp. 133-150
    • Beinert, H.1
  • 5
    • 0018109331 scopus 로고
    • Special techniques for the preparation of samples for low-temperature EPR spectroscopy
    • H. Beinert, W.H. Orme-Johnson, and G. Palmer Special techniques for the preparation of samples for low-temperature EPR spectroscopy Methods Enzymol. 54 1978 111 132
    • (1978) Methods Enzymol. , vol.54 , pp. 111-132
    • Beinert, H.1    Orme-Johnson, W.H.2    Palmer, G.3
  • 7
    • 0017184389 scopus 로고
    • Rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford Rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72 1976 248 254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 8
    • 34548727458 scopus 로고    scopus 로고
    • Biochemical and spectroscopic studies of the electronic structure and reactivity of a methyl-Ni species formed on methyl-coenzyme M reductase
    • DOI 10.1021/ja074556z
    • M. Dey, J. Telser, R.C. Kunz, N.S. Lees, S.W. Ragsdale, and B.M. Hoffman Biochemical and spectroscopic studies of the electronic structure and reactivity of a methyl-ni species formed on methyl-coenzyme M reductase J. Am. Chem. Soc. 129 2007 11030 11032 (Pubitemid 47435702)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.36 , pp. 11030-11032
    • Dey, M.1    Telser, J.2    Kunz, R.C.3    Lees, N.S.4    Ragsdale, S.W.5    Hoffman, B.M.6
  • 10
    • 40549127470 scopus 로고    scopus 로고
    • A new mechanism for methane production from methyl-coenzyme M reductase as derived from density functional calculations
    • DOI 10.1021/jp709860c
    • E.C. Duin, and M.L. Mckee A new mechanism for methane production from methyl-coenzyme M reductase as derived from density functional calculations J. Phys. Chem. B 112 2008 2466 2482 (Pubitemid 351362371)
    • (2008) Journal of Physical Chemistry B , vol.112 , Issue.8 , pp. 2466-2482
    • Duin, E.C.1    McKee, M.L.2
  • 12
    • 0019515181 scopus 로고
    • Component C of the methylreductase system of Methanobacterium
    • W.L. Ellefson, and R.S. Wolfe Component C of the methylreductase system of Methanobacterium J. Biol. Chem. 256 1981 4259 4262 (Pubitemid 11089693)
    • (1981) Journal of Biological Chemistry , vol.256 , Issue.9 , pp. 4259-4262
    • Ellefson, W.L.1    Wolfe, R.S.2
  • 13
    • 0017908773 scopus 로고
    • Transition metal electron paramagnetic resonance related to proteins
    • J.A. Fee Transition metal electron paramagnetic resonance related to proteins Methods Enzymol. 49 1978 512 528
    • (1978) Methods Enzymol. , vol.49 , pp. 512-528
    • Fee, J.A.1
  • 15
    • 4644265740 scopus 로고    scopus 로고
    • Probing the reactivity of Ni in the active site of methyl-coenzyme M reductase with substrate analogues
    • DOI 10.1007/s00775-004-0552-1
    • 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 (Pubitemid 39279248)
    • (2004) Journal of Biological Inorganic Chemistry , vol.9 , Issue.6 , pp. 691-705
    • Goenrich, M.1    Mahlert, F.2    Duin, E.C.3    Bauer, C.4    Jaun, B.5    Thauer, R.K.6
  • 16
    • 0031018357 scopus 로고    scopus 로고
    • Purified methyl-coenzyme-M reductase is activated when the enzyme-bound coenzyme F430 is reduced to the nickel(I) oxidation state by titanium(III) citrate
    • M. Goubeaud, G. Schreiner, and R.K. Thauer Purified methyl-coenzyme-M reductase is activated when the enzyme-bound coenzyme F430 is reduced to the nickel(I) oxidation state by titanium(III) citrate Eur. J. Biochem. 243 1997 110 114 (Pubitemid 27060391)
    • (1997) European Journal of Biochemistry , vol.243 , Issue.1-2 , pp. 110-114
    • Goubeaud, M.1    Schreiner, G.2    Thauer, R.K.3
  • 17
    • 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
    • DOI 10.1006/jmbi.2001.4647
    • 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 (Pubitemid 32553526)
    • (2001) Journal of Molecular Biology , vol.309 , Issue.1 , 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
  • 19
    • 0035980250 scopus 로고    scopus 로고
    • Mechanistic studies of methane biogenesis by methyl-coenzyme M reductase: Evidence that coenzyme B participates in cleaving the C - S bond of methyl-coenzyme M
    • DOI 10.1021/bi011196y
    • Y.-C. Horng, D.F. Becker, and S.W. Ragsdale Mechanistic studies of methane biogenesis by methyl-coenzyme M reductase: Evidence that coenzyme B participates in cleaving the C-S bond of methyl-coenzyme M Biochemistry 40 2001 12875 12885 (Pubitemid 33026634)
    • (2001) Biochemistry , vol.40 , Issue.43 , pp. 12875-12885
    • Horng, Y.-C.1    Becker, D.F.2    Ragsdale, S.W.3
  • 20
  • 21
    • 0027300206 scopus 로고
    • Component A2 of methylcoenzyme M reductase system from Methanobacterium thermoautotrophicum ΔH: Nucleotide sequence and functional expression by Escherichia coli
    • C.H. Kuhner, B.D. Lindenbach, and R.S. Wolfe Component A2 of methylcoenzyme M reductase system from Methanobacterium thermoautotrophicum ΔH: Nucleotide sequence and functional expression by Escherichia coli J. Bacteriol. 175 1993 3195 3203 (Pubitemid 23148759)
    • (1993) Journal of Bacteriology , vol.175 , Issue.10 , pp. 3195-3203
    • Kuhner, C.H.1    Lindenbach, B.D.2    Wolfe, R.S.3
  • 22
    • 33749362261 scopus 로고    scopus 로고
    • Spectroscopic and kinetic studies of the reaction of bromopropanesulfonate with methyl-coenzyme M reductase
    • DOI 10.1074/jbc.M606715200
    • R.C. Kunz, Y.C. Horng, and S.W. Ragsdale Spectroscopic and kinetic studies of the reaction of bromopropanesulfonate with methyl-coenzyme M reductase J. Biol. Chem. 281 2006 34663 34676 (Pubitemid 46036672)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.45 , pp. 34663-34676
    • Kunz, R.C.1    Horng, Y.-C.2    Ragsdale, S.W.3
  • 23
    • 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
    • DOI 10.1007/s00775-001-0325-z
    • 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 (Pubitemid 36061701)
    • (2002) Journal of Biological Inorganic Chemistry , vol.7 , Issue.4-5 , pp. 500-513
    • Mahlert, F.1    Bauer, C.2    Jaun, B.3    Thauer, R.K.4    Duin, E.C.5
  • 24
    • 0036359359 scopus 로고    scopus 로고
    • The nickel enzyme methyl-coenzyme M reductase from methanogenic archaea: In vitro interconversions among the EPR detectable MCR-red1 and MCR-red2 states
    • DOI 10.1007/s007750100270
    • F. Mahlert, W. Grabarse, J. Kahnt, R.K. Thauer, and E.C. Duin The nickel enzyme methyl-coenzyme M reductase from methanogenic archaea: In vitro interconversions among the EPR detectable MCR-red1 and MCR-red2 states J. Biol. Inorg. Chem. 7 2002 101 112 (Pubitemid 41490223)
    • (2002) Journal of Biological Inorganic Chemistry , vol.7 , Issue.1-2 , pp. 101-112
    • Mahlert, F.1    Grabarse, W.2    Kahnt, J.3    Thauer, R.K.4    Duin, E.C.5
  • 25
    • 0013654408 scopus 로고
    • Electron paramagnetic resonance
    • G. Palmer Electron paramagnetic resonance Methods Enzymol. 10 1967 594 595
    • (1967) Methods Enzymol. , vol.10 , pp. 594-595
    • Palmer, G.1
  • 26
    • 0042155695 scopus 로고    scopus 로고
    • Catalysis by methyl-coenzyme M reductase: A theoretical study for heterodisulfide product formation
    • DOI 10.1007/s00775-003-0461-8
    • V. Pelmenschikov, and P.E.M. Siegbahn Catalysis by methyl-coenzyme M reductase: A theoretical study for heterodisulfide product formation J. Biol. Inorg. Chem. 8 2003 653 662 (Pubitemid 36960813)
    • (2003) Journal of Biological Inorganic Chemistry , vol.8 , Issue.6 , pp. 653-662
    • Pelmenschikov, V.1    Siegbahn, P.E.M.2
  • 28
    • 84940935551 scopus 로고    scopus 로고
    • 430
    • 430 K.M. Kadish, K.M. Smith, R. Guilard, Porphyrin Handbook 2003 Elsevier Science San Diego 205 228
    • (2003) Porphyrin Handbook , pp. 205-228
    • Ragsdale, S.W.1
  • 30
    • 0026441226 scopus 로고
    • Substrate-analoque-induced changes in the nickel-EPR spectrum of active methyl-coenzyme-M reductase from Methanobacterium thermoautotrophicum
    • S. Rospert, M. Vogus, A. Berkessel, S.P.J. Albracht, and R.K. Thauer Substrate-analoque-induced changes in the nickel-EPR spectrum of active methyl-coenzyme-M reductase from Methanobacterium thermoautotrophicum Eur. J. Biochem. 210 1992 101 107
    • (1992) Eur. J. Biochem. , vol.210 , pp. 101-107
    • Rospert, S.1    Vogus, M.2    Berkessel, A.3    Albracht, S.P.J.4    Thauer, R.K.5
  • 31
    • 0024731034 scopus 로고
    • Component A3 of the methylcoenzyme M methylreductase system of Methanobacterium thermoautotrophicum Δh: Resolution into two components
    • P.E. Rouvire, and R.S. Wolfe Component A3 of the methylcoenzyme M methylreductase system of Methanobacterium thermoautotrophicum ΔH: Resolution into two components J. Bacteriol. 171 1989 4556 4562
    • (1989) J. Bacteriol. , vol.171 , pp. 4556-4562
    • Rouvire, P.E.1    Wolfe, R.S.2
  • 32
    • 65249183133 scopus 로고    scopus 로고
    • Geometric and electronic structures of the Ni-I and methyl-Ni-III intermediates of methyl-coenzyme M reductase
    • R. Sarangi, M. Dey, and S.W. Ragsdale Geometric and electronic structures of the Ni-I and methyl-Ni-III intermediates of methyl-coenzyme M reductase Biochemistry 48 2009 3146 3156
    • (2009) Biochemistry , vol.48 , pp. 3146-3156
    • Sarangi, R.1    Dey, M.2    Ragsdale, S.W.3
  • 33
    • 77953222884 scopus 로고    scopus 로고
    • The key nickel enzyme of methanogenesis catalyses the anaerobic oxidation of methane
    • S. Scheller, M. Goenrich, R. Boecher, R.K. Thauer, and B. Jaun The key nickel enzyme of methanogenesis catalyses the anaerobic oxidation of methane Nature 465 2010 606 609
    • (2010) Nature , vol.465 , pp. 606-609
    • Scheller, S.1    Goenrich, M.2    Boecher, R.3    Thauer, R.K.4    Jaun, B.5
  • 34
    • 27844544240 scopus 로고    scopus 로고
    • Methyl-coenzyme M reductase and the anaerobic oxidation of methane in methanotrophic Archaea
    • DOI 10.1016/j.mib.2005.10.002, PII S136952740500158X, Growth Development
    • S. Shima, and R.K. Thauer Methyl-coenzyme M reductase and the anaerobic oxidation of methane in methanotrophic Archaea Curr. Opin. Microbiol. 8 2005 643 648 (Pubitemid 41643032)
    • (2005) Current Opinion in Microbiology , vol.8 , Issue.6 , pp. 643-648
    • Shima, S.1    Thauer, R.K.2
  • 35
    • 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
  • 36
    • 34548748159 scopus 로고    scopus 로고
    • Formation of a nickel-methyl species in methyl-coenzyme M reductase, an enzyme catalyzing methane formation
    • DOI 10.1021/ja0734501
    • N. Yang, M. Reiher, M. Wang, J. Harmer, and E.C. Duin Formation of a nickel-methyl species in methyl-coenzyme M reductase, an enzyme catalyzing methane formation J. Am. Chem. Soc. 129 2007 11028 11029 (Pubitemid 47435701)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.36 , pp. 11028-11029
    • Yang, N.1    Reiher, M.2    Wang, M.3    Harmer, J.4    Duin, E.C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.