메뉴 건너뛰기




Volumn 49, Issue 35, 2010, Pages 7683-7693

Structural insight into methyl-coenzyme M reductase chemistry using coenzyme B analogues

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; CHEMICAL BONDS; CONFORMATIONS; HYDROPHOBICITY; METHANE; SUBSTRATES;

EID: 77956134458     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi100458d     Document Type: Article
Times cited : (43)

References (54)
  • 1
    • 0031685510 scopus 로고    scopus 로고
    • Biochemistry of methanogenesis: A tribute to Marjory Stephenson
    • Thauer, R. K. (1998) Biochemistry of methanogenesis: a tribute to Marjory Stephenson Microbiology 144, 2377-2406
    • (1998) Microbiology , vol.144 , pp. 2377-2406
    • Thauer, R.K.1
  • 2
    • 41349105149 scopus 로고    scopus 로고
    • Methane as fuel for anaerobic microorganisms
    • Thauer, R. K. and Shima, S. (2008) Methane as fuel for anaerobic microorganisms Ann. N.Y. Acad. Sci. 1125, 158-170
    • (2008) Ann. N.Y. Acad. Sci. , vol.1125 , pp. 158-170
    • Thauer, R.K.1    Shima, S.2
  • 3
    • 0024287227 scopus 로고
    • The final step in methane formation. Investigations with highly purified methyl-CoM reductase (component C) from Methanobacterium thermoautotrophicum (strain Marburg)
    • Ellermann, J., Hedderich, R., Bocher, R., and Thauer, R. K. (1988) The final step in methane formation. Investigations with highly purified methyl-CoM reductase (component C) from Methanobacterium thermoautotrophicum (strain Marburg) Eur. J. Biochem. 172, 669-677
    • (1988) Eur. J. Biochem. , vol.172 , pp. 669-677
    • Ellermann, J.1    Hedderich, R.2    Bocher, R.3    Thauer, R.K.4
  • 4
    • 0019515181 scopus 로고
    • Component C of the methylreductase system of Methanobacterium
    • Ellefson, W. L. and Wolfe, R. S. (1981) Component C of the methylreductase system of Methanobacterium J. Biol. Chem. 256, 4259-4262
    • (1981) J. Biol. Chem. , vol.256 , pp. 4259-4262
    • Ellefson, W.L.1    Wolfe, R.S.2
  • 5
    • 0030726657 scopus 로고    scopus 로고
    • Crystal structure of methyl-coenzyme M reductase: The key enzyme of biological methane formation
    • Ermler, U., Grabarse, W., Shima, S., Goubeaud, M., and Thauer, R. K. (1997) Crystal structure of methyl-coenzyme M reductase: the key enzyme of biological methane formation Science 278, 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
  • 6
    • 0019296298 scopus 로고
    • Incorporation of 8 succinate per mol nickel into factors F430 by Methanobacterium thermoautotrophicum
    • Diekert, G., Gilles, H. H., Jaenchen, R., and Thauer, R. K. (1980) Incorporation of 8 succinate per mol nickel into factors F430 by Methanobacterium thermoautotrophicum Arch. Microbiol. 128, 256-262
    • (1980) Arch. Microbiol. , vol.128 , pp. 256-262
    • Diekert, G.1    Gilles, H.H.2    Jaenchen, R.3    Thauer, R.K.4
  • 8
    • 0018873633 scopus 로고
    • Presence of nickel in factor F430 from Methanobacterium bryantii
    • Whitman, W. B. and Wolfe, R. S. (1980) Presence of nickel in factor F430 from Methanobacterium bryantii Biochem. Biophys. Res. Commun. 92, 1196-1201
    • (1980) Biochem. Biophys. Res. Commun. , vol.92 , pp. 1196-1201
    • Whitman, W.B.1    Wolfe, R.S.2
  • 9
  • 10
    • 35449004168 scopus 로고    scopus 로고
    • Characterization of alkyl-nickel adducts generated by reaction of methyl-coenzyme m reductase with brominated acids
    • Dey, M., Kunz, R. C., Lyons, D. M., and Ragsdale, S. W. (2007) Characterization of alkyl-nickel adducts generated by reaction of methyl-coenzyme m reductase with brominated acids Biochemistry 46, 11969-11978
    • (2007) Biochemistry , vol.46 , pp. 11969-11978
    • Dey, M.1    Kunz, R.C.2    Lyons, D.M.3    Ragsdale, S.W.4
  • 11
    • 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
    • Dey, M., Telser, J., Kunz, R. C., Lees, N. S., Ragsdale, S. W., and Hoffman, B. M. (2007) 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, 11030-11032
    • (2007) J. Am. Chem. Soc. , vol.129 , 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
  • 12
    • 0037257818 scopus 로고    scopus 로고
    • Coordination and geometry of the nickel atom in active methyl-coenzyme M reductase from Methanothermobacter marburgensis as detected by X-ray absorption spectroscopy
    • Duin, E. C., Cosper, N. J., Mahlert, F., Thauer, R. K., and Scott, R. A. (2003) Coordination and geometry of the nickel atom in active methyl-coenzyme M reductase from Methanothermobacter marburgensis as detected by X-ray absorption spectroscopy J. Biol. Inorg. Chem. 8, 141-148
    • (2003) J. Biol. Inorg. Chem. , vol.8 , pp. 141-148
    • Duin, E.C.1    Cosper, N.J.2    Mahlert, F.3    Thauer, R.K.4    Scott, R.A.5
  • 13
    • 3943085693 scopus 로고    scopus 로고
    • Spectroscopic investigation of the nickel-containing porphinoid cofactor F(430). Comparison of the free cofactor in the (+)1, (+)2 and (+)3 oxidation states with the cofactor bound to methyl-coenzyme M reductase in the silent, red and ox forms
    • Duin, E. C., Signor, L., Piskorski, R., Mahlert, F., Clay, M. D., Goenrich, M., Thauer, R. K., Jaun, B., and Johnson, M. K. (2004) Spectroscopic investigation of the nickel-containing porphinoid cofactor F(430). Comparison of the free cofactor in the (+)1, (+)2 and (+)3 oxidation states with the cofactor bound to methyl-coenzyme M reductase in the silent, red and ox forms J. Biol. Inorg. Chem. 9, 563-576
    • (2004) J. Biol. Inorg. Chem. , vol.9 , pp. 563-576
    • Duin, E.C.1    Signor, L.2    Piskorski, R.3    Mahlert, F.4    Clay, M.D.5    Goenrich, M.6    Thauer, R.K.7    Jaun, B.8    Johnson, M.K.9
  • 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
    • Goubeaud, M., Schreiner, G., and Thauer, R. K. (1997) 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, 110-114
    • (1997) Eur. J. Biochem. , vol.243 , pp. 110-114
    • Goubeaud, M.1    Schreiner, G.2    Thauer, R.K.3
  • 20
    • 33749362261 scopus 로고    scopus 로고
    • Spectroscopic and kinetic studies of the reaction of bromopropanesulfonate with methyl-coenzyme M reductase
    • Kunz, R. C., Horng, Y. C., and Ragsdale, S. W. (2006) Spectroscopic and kinetic studies of the reaction of bromopropanesulfonate with methyl-coenzyme M reductase J. Biol. Chem. 281, 34663-34676
    • (2006) J. Biol. Chem. , vol.281 , pp. 34663-34676
    • Kunz, R.C.1    Horng, Y.C.2    Ragsdale, S.W.3
  • 21
    • 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
    • Mahlert, F., Bauer, C., Jaun, B., Thauer, R. K., and Duin, E. C. (2002) 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, 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
  • 22
    • 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
    • Mahlert, F., Grabarse, W., Kahnt, J., Thauer, R. K., and Duin, E. C. (2002) 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, 101-112
    • (2002) J. Biol. Inorg. Chem. , vol.7 , pp. 101-112
    • Mahlert, F.1    Grabarse, W.2    Kahnt, J.3    Thauer, R.K.4    Duin, E.C.5
  • 23
    • 0026441226 scopus 로고
    • Substrate-analogue-induced changes in the nickel-EPR spectrum of active methyl-coenzyme-M reductase from Methanobacterium thermoautotrophicum
    • Rospert, S., Voges, M., Berkessel, A., Albracht, S. P., and Thauer, R. K. (1992) Substrate-analogue-induced changes in the nickel-EPR spectrum of active methyl-coenzyme-M reductase from Methanobacterium thermoautotrophicum Eur. J. Biochem. 210, 101-107
    • (1992) Eur. J. Biochem. , vol.210 , pp. 101-107
    • Rospert, S.1    Voges, M.2    Berkessel, A.3    Albracht, S.P.4    Thauer, R.K.5
  • 24
    • 65249183133 scopus 로고    scopus 로고
    • Geometric and electronic structures of the Ni(I) and methyl-Ni(III) intermediates of methyl-coenzyme M reductase
    • Sarangi, R., Dey, M., and Ragsdale, S. W. (2009) Geometric and electronic structures of the Ni(I) and methyl-Ni(III) intermediates of methyl-coenzyme M reductase Biochemistry 48, 3146-3156
    • (2009) Biochemistry , vol.48 , pp. 3146-3156
    • Sarangi, R.1    Dey, M.2    Ragsdale, S.W.3
  • 25
    • 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
    • Tang, Q., Carrington, P. E., Horng, Y. C., Maroney, M. J., Ragsdale, S. W., and Bocian, D. F. (2002) 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, 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
  • 26
    • 0034819997 scopus 로고    scopus 로고
    • Cryoreduction of methyl-coenzyme M reductase: EPR characterization of forms, MCR(ox1) and MCR (red1)
    • Telser, J., Davydov, R., Horng, Y. C., Ragsdale, S. W., and Hoffman, B. M. (2001) Cryoreduction of methyl-coenzyme M reductase: EPR characterization of forms, MCR(ox1) and MCR (red1) J. Am. Chem. Soc. 123, 5853-5860
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 5853-5860
    • Telser, J.1    Davydov, R.2    Horng, Y.C.3    Ragsdale, S.W.4    Hoffman, B.M.5
  • 27
    • 34548748159 scopus 로고    scopus 로고
    • Formation of a nickel-methyl species in methyl-coenzyme M reductase, an enzyme catalyzing methane formation
    • Yang, N., Reiher, M., Wang, M., Harmer, J., and Duin, E. C. (2007) Formation of a nickel-methyl species in methyl-coenzyme M reductase, an enzyme catalyzing methane formation J. Am. Chem. Soc. 129, 11028-11029
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 11028-11029
    • Yang, N.1    Reiher, M.2    Wang, M.3    Harmer, J.4    Duin, E.C.5
  • 29
    • 0034639453 scopus 로고    scopus 로고
    • On the assignment of nickel oxidation states of the Ox1, Ox2 forms of methyl-coenzyme M reductase
    • Telser, J., Horng, Y. C., Becker, D. F., Hoffman, B. M., and Ragsdale, S. W. (2000) On the assignment of nickel oxidation states of the Ox1, Ox2 forms of methyl-coenzyme M reductase J. Am. Chem. Soc. 122, 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
  • 31
    • 35348897220 scopus 로고    scopus 로고
    • Two sub-states of the red2 state of methyl-coenzyme M reductase revealed by high-field EPR spectroscopy
    • Kern, D. I., Goenrich, M., Jaun, B., Thauer, R. K., Harmer, J., and Hinderberger, D. (2007) Two sub-states of the red2 state of methyl-coenzyme M reductase revealed by high-field EPR spectroscopy J. Biol. Inorg. Chem. 12, 1097-1105
    • (2007) J. Biol. Inorg. Chem. , vol.12 , pp. 1097-1105
    • Kern, D.I.1    Goenrich, M.2    Jaun, B.3    Thauer, R.K.4    Harmer, J.5    Hinderberger, D.6
  • 32
    • 0032562134 scopus 로고    scopus 로고
    • Activation of methyl-SCoM reductase to high specific activity after treatment of whole cells with sodium sulfide
    • Becker, D. F. and Ragsdale, S. W. (1998) Activation of methyl-SCoM reductase to high specific activity after treatment of whole cells with sodium sulfide Biochemistry 37, 2639-2647
    • (1998) Biochemistry , vol.37 , pp. 2639-2647
    • Becker, D.F.1    Ragsdale, S.W.2
  • 33
    • 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
    • Grabarse, W., Mahlert, F., Duin, E. C., Goubeaud, M., Shima, S., Thauer, R. K., Lamzin, V., and Ermler, U. (2001) On the mechanism of biological methane formation: structural evidence for conformational changes in methyl-coenzyme M reductase upon substrate binding J. Mol. Biol. 309, 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
  • 34
    • 0034692923 scopus 로고    scopus 로고
    • Comparison of three methyl-coenzyme M reductases from phylogenetically distant organisms: Unusual amino acid modification, conservation and adaptation
    • Grabarse, W., Mahlert, F., Shima, S., Thauer, R. K., and Ermler, U. (2000) Comparison of three methyl-coenzyme M reductases from phylogenetically distant organisms: unusual amino acid modification, conservation and adaptation J. Mol. Biol. 303, 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
  • 35
    • 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
    • Horng, Y. C., Becker, D. F., and Ragsdale, S. W. (2001) 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, 12875-12885
    • (2001) Biochemistry , vol.40 , pp. 12875-12885
    • Horng, Y.C.1    Becker, D.F.2    Ragsdale, S.W.3
  • 36
    • 0026022064 scopus 로고
    • Methyl-coenzyme-M reductase-Model studies on pentadentate nickel-complexes and a hypothetical mechanism
    • Berkessel, A. (1991) Methyl-coenzyme-M reductase-Model studies on pentadentate nickel-complexes and a hypothetical mechanism Bioorg. Chem. 19, 101-115
    • (1991) Bioorg. Chem. , vol.19 , pp. 101-115
    • Berkessel, A.1
  • 37
    • 0025601888 scopus 로고
    • Coenzyme-F430 from methanogenic bacteria-Oxidation of F430 pentamethyl ester to the Ni(III) form
    • Jaun, B. (1990) Coenzyme-F430 from methanogenic bacteria-Oxidation of F430 pentamethyl ester to the Ni(III) form Helv. Chim. Acta 73, 2209-2217
    • (1990) Helv. Chim. Acta , vol.73 , pp. 2209-2217
    • Jaun, B.1
  • 38
    • 0034596913 scopus 로고    scopus 로고
    • Methane formation by reaction of a methyl thioether with a photo-excited nickel thiolate-A process mimicking methanogenesis in archaea
    • Signor, L., Knuppe, C., Hug, R., Schweizer, B., Pfaltz, A., and Jaun, B. (2000) Methane formation by reaction of a methyl thioether with a photo-excited nickel thiolate-A process mimicking methanogenesis in archaea Chem.-Eur. J. 6, 3508-3516
    • (2000) Chem.-Eur. J. , vol.6 , pp. 3508-3516
    • Signor, L.1    Knuppe, C.2    Hug, R.3    Schweizer, B.4    Pfaltz, A.5    Jaun, B.6
  • 39
    • 67651235342 scopus 로고    scopus 로고
    • Is there a Ni-methyl intermediate in the mechanism of methyl-coenzyme M reductase?
    • Chen, S. L., Pelmenschikov, V., Blomberg, M. R., and Siegbahn, P. E. (2009) Is there a Ni-methyl intermediate in the mechanism of methyl-coenzyme M reductase? J. Am. Chem. Soc. 131, 9912-9913
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 9912-9913
    • Chen, S.L.1    Pelmenschikov, V.2    Blomberg, M.R.3    Siegbahn, P.E.4
  • 40
    • 0037123266 scopus 로고    scopus 로고
    • A mechanism from quantum chemical studies for methane formation in methanogenesis
    • Pelmenschikov, V., Blomberg, M. R. A., Siegbahn, P. E. M., and Crabtree, R. H. (2002) A mechanism from quantum chemical studies for methane formation in methanogenesis J. Am. Chem. Soc. 124, 4039-4049
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 4039-4049
    • Pelmenschikov, V.1    Blomberg, M.R.A.2    Siegbahn, P.E.M.3    Crabtree, R.H.4
  • 41
    • 0042155695 scopus 로고    scopus 로고
    • Catalysis by methyl-coenzyme M reductase: A theoretical study for heterodisulfide product formation
    • Pelmenschikov, V. and Siegbahn, P. E. (2003) Catalysis by methyl-coenzyme M reductase: a theoretical study for heterodisulfide product formation J. Biol. Inorg. Chem. 8, 653-662
    • (2003) J. Biol. Inorg. Chem. , vol.8 , pp. 653-662
    • Pelmenschikov, V.1    Siegbahn, P.E.2
  • 42
    • 40549127470 scopus 로고    scopus 로고
    • A new mechanism for methane production from methyl-coenzyme M reductase as derived from density functional calculations
    • Duin, E. C. and McKee, M. L. (2008) A new mechanism for methane production from methyl-coenzyme M reductase as derived from density functional calculations J. Phys. Chem. B 112, 2466-2482
    • (2008) J. Phys. Chem. B , vol.112 , pp. 2466-2482
    • Duin, E.C.1    McKee, M.L.2
  • 43
    • 0023777023 scopus 로고
    • Physiological importance of the heterodisulfide of coenzyme M and 7-mercaptoheptanoylthreonine phosphate in the reduction of carbon dioxide to methane in Methanobacterium
    • Bobik, T. A. and Wolfe, R. S. (1988) Physiological importance of the heterodisulfide of coenzyme M and 7-mercaptoheptanoylthreonine phosphate in the reduction of carbon dioxide to methane in Methanobacterium Proc. Natl. Acad. Sci. U.S.A. 85, 60-63
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 60-63
    • Bobik, T.A.1    Wolfe, R.S.2
  • 44
    • 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
    • Goenrich, M., Duin, E. C., Mahlert, F., and Thauer, R. K. (2005) 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, 333-342
    • (2005) J. Biol. Inorg. Chem. , vol.10 , pp. 333-342
    • Goenrich, M.1    Duin, E.C.2    Mahlert, F.3    Thauer, R.K.4
  • 45
    • 39749085836 scopus 로고    scopus 로고
    • Characterization of the thioether product formed from the thiolytic cleavage of the alkyl-nickel bond in methyl-coenzyme M reductase
    • Kunz, R. C., Dey, M., and Ragsdale, S. W. (2008) Characterization of the thioether product formed from the thiolytic cleavage of the alkyl-nickel bond in methyl-coenzyme M reductase Biochemistry 47, 2661-2667
    • (2008) Biochemistry , vol.47 , pp. 2661-2667
    • Kunz, R.C.1    Dey, M.2    Ragsdale, S.W.3
  • 46
    • 0023123041 scopus 로고
    • Synthesis of 7-mercaptoheptanoylthreonine phosphate and its activity in the methylcoenzyme M methylreductase system
    • Noll, K. M., Donnelly, M. I., and Wolfe, R. S. (1987) Synthesis of 7-mercaptoheptanoylthreonine phosphate and its activity in the methylcoenzyme M methylreductase system J. Biol. Chem. 262, 513-515
    • (1987) J. Biol. Chem. , vol.262 , pp. 513-515
    • Noll, K.M.1    Donnelly, M.I.2    Wolfe, R.S.3
  • 47
    • 0025762554 scopus 로고
    • Photoactivation of the 2-(methylthio)ethanesulfonic acid reductase from Methanobacterium
    • Olson, K. D., McMahon, C. W., and Wolfe, R. S. (1991) Photoactivation of the 2-(methylthio)ethanesulfonic acid reductase from Methanobacterium Proc. Natl. Acad. Sci. U.S.A. 88, 4099-4103
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 4099-4103
    • Olson, K.D.1    McMahon, C.W.2    Wolfe, R.S.3
  • 48
    • 0017036833 scopus 로고
    • Titanium(III) citrate as a nontoxic oxidation-reduction buffering system for the culture of obligate anaerobes
    • Zehnder, A. J. and Wuhrmann, K. (1976) Titanium(III) citrate as a nontoxic oxidation-reduction buffering system for the culture of obligate anaerobes Science 194, 1165-1166
    • (1976) Science , vol.194 , pp. 1165-1166
    • Zehnder, A.J.1    Wuhrmann, K.2
  • 49
    • 0017886342 scopus 로고
    • Preparation of coenzyme M analogues and their activity in the methyl coenzyme M reductase system of Methanobacterium thermoautotrophicum
    • Gunsalus, R. P., Romesser, J. A., and Wolfe, R. S. (1978) Preparation of coenzyme M analogues and their activity in the methyl coenzyme M reductase system of Methanobacterium thermoautotrophicum Biochemistry 17, 2374-2377
    • (1978) Biochemistry , vol.17 , pp. 2374-2377
    • Gunsalus, R.P.1    Romesser, J.A.2    Wolfe, R.S.3
  • 51
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • (1994) The CCP4 suite: programs for protein crystallography, Acta Crystallogr., Sect. D: Biol. Crystallogr. 50, 760-763.
    • (1994) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.50 , pp. 760-763
  • 53
    • 74949109377 scopus 로고    scopus 로고
    • Binding of coenzyme B induces a major conformational change in the active site of methyl-coenzyme M reductase
    • Ebner, S., Jaun, B., Goenrich, M., Thauer, R. K., and Harmer, J. (2010) Binding of coenzyme B induces a major conformational change in the active site of methyl-coenzyme M reductase J. Am. Chem. Soc. 132, 567-575
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 567-575
    • Ebner, S.1    Jaun, B.2    Goenrich, M.3    Thauer, R.K.4    Harmer, J.5
  • 54
    • 4644265740 scopus 로고    scopus 로고
    • Probing the reactivity of Ni in the active site of methyl-coenzyme M reductase with substrate analogues
    • Goenrich, M., Mahlert, F., Duin, E. C., Bauer, C., Jaun, B., and Thauer, R. K. (2004) Probing the reactivity of Ni in the active site of methyl-coenzyme M reductase with substrate analogues J. Biol. Inorg. Chem. 9, 691-705
    • (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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.