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Volumn 45, Issue 39, 2006, Pages 11915-11933

Spectroscopic and computational studies of reduction of the metal versus the tetrapyrrole ring of coenzyme F430 from methyl-coenzyme M reductase

Author keywords

[No Author keywords available]

Indexed keywords

COMPUTATIONAL METHODS; DISCRETE FOURIER TRANSFORMS; METHANE; NICKEL COMPOUNDS; SODIUM COMPOUNDS; SPECTROMETERS;

EID: 33749323024     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0613269     Document Type: Article
Times cited : (11)

References (88)
  • 2
    • 0023658408 scopus 로고
    • On the role of N-7-mercaptoheptanoyl-O-phospho-L-threonine (component B) in the enzymatic reduction of methyl-coenzyme M to methane
    • Ellermann, J., Kobelt, A., Pfaltz, A., and Thauer, R. K. (1987) On the role of N-7-mercaptoheptanoyl-O-phospho-L-threonine (component B) in the enzymatic reduction of methyl-coenzyme M to methane, FEBS Lett. 220, 358-362.
    • (1987) FEBS Lett. , vol.220 , pp. 358-362
    • Ellermann, J.1    Kobelt, A.2    Pfaltz, A.3    Thauer, R.K.4
  • 5
    • 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
  • 6
    • 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
  • 7
    • 0019813985 scopus 로고
    • Nickel requirement and factor F430 content of methanogenic bacteria
    • Diekert, G., Konheiser, U., Piechulla, K., and Thauer, R. K. (1981) Nickel requirement and factor F430 content of methanogenic bacteria, J. Bacteriol. 148, 459-464.
    • (1981) J. Bacteriol. , vol.148 , pp. 459-464
    • Diekert, G.1    Konheiser, U.2    Piechulla, K.3    Thauer, R.K.4
  • 8
    • 0031018357 scopus 로고    scopus 로고
    • 430 is reduced to the nickel(I) oxidation state by titanium(III) citrate
    • 430 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
  • 9
    • 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
  • 10
    • 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
  • 12
    • 0842268682 scopus 로고
    • Coenzyme F430 from methanogenic bacteria: Reversible one-electron reduction of F430 pentamethyl ester to the nickel(I) form
    • Jaun, B., and Pfaltz, A. (1986) Coenzyme F430 from Methanogenic Bacteria: Reversible One-electron Reduction of F430 Pentamethyl Ester to the Nickel(I) Form, J. Chem. Soc., Chem. Commun., 1327-1329.
    • (1986) J. Chem. Soc., Chem. Commun. , pp. 1327-1329
    • Jaun, B.1    Pfaltz, A.2
  • 13
    • 0034639453 scopus 로고    scopus 로고
    • On the assignment of nickel oxidation states of the Ox1 and Ox2 forms of methyl-coenzyme M reductase
    • Telser, J., Horng, Y.-C., Becker, D., Hoffman, B., and Ragsdale, S. W. (2000) On the assignment of nickel oxidation states of the Ox1 and 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.3    Hoffman, B.4    Ragsdale, S.W.5
  • 14
    • 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
  • 15
    • 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. J., 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.J.4    Thauer, R.K.5
  • 16
    • 0031047161 scopus 로고    scopus 로고
    • Investigation by EPR and ENDOR spectroscopy of the nickel(I) form of cofactor F-430 of Methanobacterium thermoautotrophicum and of nickel(I) octaethylisobacteriochlorin
    • Telser, J., Fann, Y. C., Renner, M. W., Fajer, J., Wang, S. K., Zhang, H., Scott, R. A., and Hoffman, B. M. (1997) Investigation by EPR and ENDOR spectroscopy of the nickel(I) form of cofactor F-430 of Methanobacterium thermoautotrophicum and of nickel(I) octaethylisobacteriochlorin, J. Am. Chem. Soc. 119, 733-743.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 733-743
    • Telser, J.1    Fann, Y.C.2    Renner, M.W.3    Fajer, J.4    Wang, S.K.5    Zhang, H.6    Scott, R.A.7    Hoffman, B.M.8
  • 17
    • 0002247680 scopus 로고    scopus 로고
    • Nickel in F430
    • (Williams, R. J. P., Ed.), Springer-Verlag, Heidelberg, Germany
    • Telser, J. (1998) Nickel in F430, in Structure and Bonding (Williams, R. J. P., Ed.) pp 32-63, Springer-Verlag, Heidelberg, Germany.
    • (1998) Structure and Bonding , pp. 32-63
    • Telser, J.1
  • 19
    • 0020144115 scopus 로고
    • Nickel-containing factor F430: Chromophore of the methylreductase of Methanobacterium
    • Ellefson, W. L., Whitman, W. B., and Wolfe, R. S. (1982) Nickel-containing factor F430: Chromophore of the methylreductase of Methanobacterium, Proc. Natl. Acad. Sci. U.S.A. 79, 3707-3710.
    • (1982) Proc. Natl. Acad. Sci. U.S.A. , vol.79 , pp. 3707-3710
    • Ellefson, W.L.1    Whitman, W.B.2    Wolfe, R.S.3
  • 20
    • 0024674470 scopus 로고
    • The magnetic properties of the nickel cofactor F430 in the enzyme methyl-coenzyme M reductase of Methanobacterium thermoautotrophicum
    • Cheesman, M. R., Ankel-Fuchs, D., Thauer, R. K., and Thompson, A. J. (1989) The magnetic properties of the nickel cofactor F430 in the enzyme methyl-coenzyme M reductase of Methanobacterium thermoautotrophicum, Biochem. J. 260, 613-616.
    • (1989) Biochem. J. , vol.260 , pp. 613-616
    • Cheesman, M.R.1    Ankel-Fuchs, D.2    Thauer, R.K.3    Thompson, A.J.4
  • 23
    • 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
  • 24
    • 0142214613 scopus 로고    scopus 로고
    • Direct determination of the number of electrons needed to reduce coenzyme F430 pentamethyl ester to the Ni(I) species exhibiting the electron paramagnetic resonance and ultraviolet-visible spectra characteristic for the MCR(red1) state of methyl-coenzyme M reductase
    • Piskorski, R., and Jaun, B. (2003) Direct determination of the number of electrons needed to reduce coenzyme F430 pentamethyl ester to the Ni(I) species exhibiting the electron paramagnetic resonance and ultraviolet-visible spectra characteristic for the MCR(red1) state of methyl-coenzyme M reductase, J. Am. Chem. Soc. 125, 13120-13125.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 13120-13125
    • Piskorski, R.1    Jaun, B.2
  • 25
    • 0842333899 scopus 로고    scopus 로고
    • Spectroscopic and computational characterization of the nickel-containing F(430) cofactor of methyl-coenzyme M reductase
    • Craft, J. L., Horng, Y. C., Ragsdale, S. W., and Brunold, T. C. (2004) Spectroscopic and computational characterization of the nickel-containing F(430) cofactor of methyl-coenzyme M reductase, J. Biol. Inorg. Chem. 9, 77-89.
    • (2004) J. Biol. Inorg. Chem. , vol.9 , pp. 77-89
    • Craft, J.L.1    Horng, Y.C.2    Ragsdale, S.W.3    Brunold, T.C.4
  • 26
    • 0018934161 scopus 로고
    • Nickel, cobalt, and molybdenum requirement for growth of Methanobacterium thermoautotrophicum
    • Schönheit, P., Moll, J., and Thauer, R. K. (1980) Nickel, cobalt, and molybdenum requirement for growth of Methanobacterium thermoautotrophicum, Arch. Microbiol. 127, 59-65.
    • (1980) Arch. Microbiol. , vol.127 , pp. 59-65
    • Schönheit, P.1    Moll, J.2    Thauer, R.K.3
  • 27
    • 0343593731 scopus 로고    scopus 로고
    • Phylogenetic analysis of 18 thermophilic Methanobacterium isolates supports the proposals to create a new genus, Methanothermobacter gen. nov., and to reclassify several isolates in three species, Methanothermobacter thermautotrophicus comb, nov., Methanothermobacter wolfeii comb, nov., and Methanothermobacter marburgensis sp. nov
    • Wasserfallen, A., Nolling, J., Pfister, P., Reeve, J., and Conway de Macario, E. (2000) Phylogenetic analysis of 18 thermophilic Methanobacterium isolates supports the proposals to create a new genus, Methanothermobacter gen. nov., and to reclassify several isolates in three species, Methanothermobacter thermautotrophicus comb, nov., Methanothermobacter wolfeii comb, nov., and Methanothermobacter marburgensis sp. nov., Int. J. Syst. Evol. Microbiol. 50 (Part 1), 43-53.
    • (2000) Int. J. Syst. Evol. Microbiol. , vol.50 , Issue.PART 1 , pp. 43-53
    • Wasserfallen, A.1    Nolling, J.2    Pfister, P.3    Reeve, J.4    Conway De Macario, E.5
  • 28
    • 33749362261 scopus 로고    scopus 로고
    • Spectroscopic and kinetic studies of the reaction of bromopropane- sulfonate with methyl-coenzyme M reductase
    • in press
    • Kunz, R. C.; Horng, Y.-C., and Ragsdale, S. W. (2006) Spectroscopic and Kinetic Studies of the Reaction of Bromopropane-sulfonate with Methyl-Coenzyme M Reductase, J. Biol. Chem., in press.
    • (2006) J. Biol. Chem.
    • Kunz, R.C.1    Horng, Y.-C.2    Ragsdale, S.W.3
  • 29
    • 0040833854 scopus 로고
    • Nickel tetrapyrrole Cofactor F430: Comparison of the forms bound to Methyl-Coenzyme M Reductase and protein free in cells of Methanobacterium thermoautotrophicum ΔH
    • Hausinger, R. P., Orme-Johnson, W. H., and Walsh, C. (1984) Nickel tetrapyrrole Cofactor F430: Comparison of the forms bound to Methyl-Coenzyme M Reductase and protein free in cells of Methanobacterium thermoautotrophicum ΔH, Biochemistry 23, 801-804.
    • (1984) Biochemistry , vol.23 , pp. 801-804
    • Hausinger, R.P.1    Orme-Johnson, W.H.2    Walsh, C.3
  • 30
    • 33749350375 scopus 로고    scopus 로고
    • George, G. N., and Pickering, I. (2000) Stanford Linear Accelerator Center, Stanford, CA
    • George, G. N., and Pickering, I. (2000) Stanford Linear Accelerator Center, Stanford, CA.
  • 31
    • 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
  • 32
    • 84949116644 scopus 로고
    • Coenzyme F430 from methanogenic bacteria: Complete assignment of configuration based on an X-ray analysis of 12,13-diepi-F430 pentamethyl ester and on NMR spectroscopy
    • Färber, G., Keller, W., Kratky, C., Jaun, B., Pfaltz, A., Spinner, C., Kobelt, A., and Eschenmoser, A. (1991) Coenzyme F430 from methanogenic bacteria: Complete assignment of configuration based on an X-ray analysis of 12,13-diepi-F430 pentamethyl ester and on NMR spectroscopy, Helv. Chim. Acta 74, 697-716.
    • (1991) Helv. Chim. Acta , vol.74 , pp. 697-716
    • Färber, G.1    Keller, W.2    Kratky, C.3    Jaun, B.4    Pfaltz, A.5    Spinner, C.6    Kobelt, A.7    Eschenmoser, A.8
  • 33
    • 0038023343 scopus 로고
    • Self-consistent molecular Hartree-Fock-Slater calculations I. The computational procedure
    • Baerends, E. J., Ellis, D. E., and Ros, P. (1973) Self-consistent molecular Hartree-Fock-Slater calculations I. The computational procedure, Chem. Phys. 2, 41.
    • (1973) Chem. Phys. , vol.2 , pp. 41
    • Baerends, E.J.1    Ellis, D.E.2    Ros, P.3
  • 34
    • 36549093268 scopus 로고
    • The determination of molecular-structures by density functional theory: The evaluation of analytical energy gradients by numerical integration
    • Versluis, L., and Ziegler, T. (1988) The Determination of Molecular-Structures by Density Functional Theory: The Evaluation of Analytical Energy Gradients by Numerical Integration, J. Chem. Phys. 88, 322-328.
    • (1988) J. Chem. Phys. , vol.88 , pp. 322-328
    • Versluis, L.1    Ziegler, T.2
  • 35
    • 28144440701 scopus 로고
    • Numerical integration for polyatomic systems
    • Velde, G. T., and Baerends, E. J. (1992) Numerical Integration for Polyatomic Systems, J. Comput. Phys. 99, 84-98.
    • (1992) J. Comput. Phys. , vol.99 , pp. 84-98
    • Velde, G.T.1    Baerends, E.J.2
  • 37
    • 0000216001 scopus 로고
    • Accurate spin-dependent electron liquid correlation energies for local spin-density calculations: A critical analysis
    • Vosko, S. H., Wilk, L., and Nusair, M. (1980) Accurate Spin-Dependent Electron Liquid Correlation Energies for Local Spin-Density Calculations: A Critical Analysis, Can. J. Phys. 58, 1200-1211.
    • (1980) Can. J. Phys. , vol.58 , pp. 1200-1211
    • Vosko, S.H.1    Wilk, L.2    Nusair, M.3
  • 38
    • 0039892284 scopus 로고
    • Density functional calculations of molecular-bond energies
    • Becke, A. D. (1986) Density Functional Calculations of Molecular-Bond Energies, J. Chem. Phys. 84, 4524-4529.
    • (1986) J. Chem. Phys. , vol.84 , pp. 4524-4529
    • Becke, A.D.1
  • 39
    • 5944261746 scopus 로고
    • Density-functional approximation for the correlation-energy of the inhomogeneous electron-gas
    • Perdew, J. P. (1986) Density-Functional Approximation for the Correlation-Energy of the Inhomogeneous Electron-Gas, Phys. Rev. B 33, 8822-8824.
    • (1986) Phys. Rev. B , vol.33 , pp. 8822-8824
    • Perdew, J.P.1
  • 42
    • 0000189651 scopus 로고
    • Density-functional thermochemistry. 3. The Role of exact exchange
    • Becke, A. D. (1993) Density-Functional Thermochemistry. 3. The Role of Exact Exchange, J. Chem. Phys. 98, 5648-5652.
    • (1993) J. Chem. Phys. , vol.98 , pp. 5648-5652
    • Becke, A.D.1
  • 43
    • 34250817103 scopus 로고
    • A new mixing of hartree-fock and local density-functional theories
    • Becke, A. D. (1993) A New Mixing of Hartree-Fock and Local Density-Functional Theories, J. Chem. Phys. 98, 1372-1377.
    • (1993) J. Chem. Phys. , vol.98 , pp. 1372-1377
    • Becke, A.D.1
  • 44
    • 0345491105 scopus 로고
    • Development of the colle-salvetti correlation-energy formula into a functional of the electron-density
    • Lee, C. T., Yang, W. T., and Parr, R. G. (1988) Development of the Colle-Salvetti Correlation-Energy Formula into a Functional of the Electron-Density, Phys. Rev. B 37, 785-789.
    • (1988) Phys. Rev. B , vol.37 , pp. 785-789
    • Lee, C.T.1    Yang, W.T.2    Parr, R.G.3
  • 45
    • 26344435738 scopus 로고
    • Fully optimized contracted gaussian-basis sets for atoms Li to Kr
    • Schafer, A., Horn, H., and Ahlrichs, R. (1992) Fully Optimized Contracted Gaussian-Basis Sets for Atoms Li to Kr, J. Chem. Phys. 97, 2571-2577.
    • (1992) J. Chem. Phys. , vol.97 , pp. 2571-2577
    • Schafer, A.1    Horn, H.2    Ahlrichs, R.3
  • 46
    • 0031285839 scopus 로고    scopus 로고
    • RI-MP2: First derivatives and global consistency
    • Weigend, F., and Haser, M. (1997) RI-MP2: First derivatives and global consistency, Theor. Chem. Acc. 97, 331-340.
    • (1997) Theor. Chem. Acc. , vol.97 , pp. 331-340
    • Weigend, F.1    Haser, M.2
  • 47
    • 0039209924 scopus 로고
    • Fully optimized contracted gaussian-basis sets of triple zeta valence quality for atoms Li to Kr
    • Schafer, A., Huber, C., and Ahlrichs, R. (1994) Fully Optimized Contracted Gaussian-Basis Sets of Triple Zeta Valence Quality for Atoms Li to Kr, J. Chem. Phys. 100, 5829-5835.
    • (1994) J. Chem. Phys. , vol.100 , pp. 5829-5835
    • Schafer, A.1    Huber, C.2    Ahlrichs, R.3
  • 48
    • 84961980743 scopus 로고
    • Cosmo: A new approach to dielectric screening in solvents with explicit expressions for the screening energy and its gradient
    • Klamt, A., and Schuurmann, G. (1993) Cosmo: A New Approach to Dielectric Screening in Solvents with Explicit Expressions for the Screening Energy and Its Gradient, J. Chem. Soc., Perkin Trans., 799-805.
    • (1993) J. Chem. Soc., Perkin Trans. , pp. 799-805
    • Klamt, A.1    Schuurmann, G.2
  • 49
    • 0026590397 scopus 로고
    • A graphics program for the analysis and display of molecular dynamics trajectories
    • Laaksonen, L. (1992) A graphics program for the analysis and display of molecular dynamics trajectories, J. Mol. Graphics 10, 33-34.
    • (1992) J. Mol. Graphics , vol.10 , pp. 33-34
    • Laaksonen, L.1
  • 50
    • 0023945677 scopus 로고
    • Structural heterogeneity and purification of protein-free F430 from the cytoplasm of Methanobacterium thermoautotrophicum
    • Shiemke, A. K., Hamilton, C. L., and Scott, R. A. (1988) Structural heterogeneity and purification of protein-free F430 from the cytoplasm of Methanobacterium thermoautotrophicum, J. Biol. Chem. 263, 5611-5616.
    • (1988) J. Biol. Chem. , vol.263 , pp. 5611-5616
    • Shiemke, A.K.1    Hamilton, C.L.2    Scott, R.A.3
  • 51
    • 77956868541 scopus 로고
    • A roll tube method for cultivation of strict anaerobes
    • (Norris, J. R., and Ribbons, D. W., Eds.), Chapter IV, Academic Press, New York
    • Hungate, R. E. (1969) A roll tube method for cultivation of strict anaerobes, in Methods in Microbiology (Norris, J. R., and Ribbons, D. W., Eds.) Chapter IV, pp 117, Academic Press, New York.
    • (1969) Methods in Microbiology , pp. 117
    • Hungate, R.E.1
  • 52
    • 0037026798 scopus 로고    scopus 로고
    • Magnetic circular dichroism of octaethylcorrphycene and its doubly protonated and deprotonated forms
    • Gorski, A., Vogel, E., Sessler, J. L., and Waluk, J. (2002) Magnetic Circular Dichroism of Octaethylcorrphycene and Its Doubly Protonated and Deprotonated Forms, J. Phys. Chem. A 106, 8139-8145.
    • (2002) J. Phys. Chem. A , vol.106 , pp. 8139-8145
    • Gorski, A.1    Vogel, E.2    Sessler, J.L.3    Waluk, J.4
  • 54
    • 0025233379 scopus 로고
    • Two-dimensional NMR studies of native coenzyme F430
    • Won, H., Summers, M. F., Olson, K., and Wolfe, R. S. (1990) Two-Dimensional NMR Studies of Native Coenzyme F430, J. Am. Chem. Soc. 112, 2178-2184.
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 2178-2184
    • Won, H.1    Summers, M.F.2    Olson, K.3    Wolfe, R.S.4
  • 55
    • 0842264385 scopus 로고    scopus 로고
    • Chemical transformation of abietic acid to new chiral derivatives
    • dos Santos, C., Zukerman-Schpector, J., and Imamura, P. M. (2003) Chemical Transformation of Abietic Acid to New Chiral Derivatives, J. Braz. Chem. Soc. 14, 998-1004.
    • (2003) J. Braz. Chem. Soc. , vol.14 , pp. 998-1004
    • Dos Santos, C.1    Zukerman-Schpector, J.2    Imamura, P.M.3
  • 58
    • 0038295926 scopus 로고    scopus 로고
    • 3+-corrinoids: Spectral and electronic properties of the B12 cofactors and biologically relevant precursors
    • 3+-corrinoids: Spectral and electronic properties of the B12 cofactors and biologically relevant precursors, J. Am. Chem. Soc. 125, 5897-5914.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 5897-5914
    • Stich, T.A.1    Brooks, A.J.2    Buan, N.R.3    Brunold, T.C.4
  • 60
    • 20944441368 scopus 로고    scopus 로고
    • Spectroscopic and computational studies of the ATP: Corrinoid adenosyltransferase (CobA) from Salmonella enterica: Insights into the mechanism of adenosylcobalamin biosynthesis
    • Stich, T. A., Buan, N. R., Escalante-Semerena, J. C., and Brunold, T. C. (2005) Spectroscopic and computational studies of the ATP: corrinoid adenosyltransferase (CobA) from Salmonella enterica: Insights into the mechanism of adenosylcobalamin biosynthesis, J. Am. Chem. Soc. 127, 8710-8719.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 8710-8719
    • Stich, T.A.1    Buan, N.R.2    Escalante-Semerena, J.C.3    Brunold, T.C.4
  • 62
    • 0000287603 scopus 로고    scopus 로고
    • Molecular excitation energies to high-lying bound states from time-dependent density-functional response theory: Characterization and correction of the time-dependent local density approximation ionization threshold
    • Casida, M. E., Jamorski, C., Casida, K. C., and Salahub, D. R. (1998) Molecular excitation energies to high-lying bound states from time-dependent density-functional response theory: Characterization and correction of the time-dependent local density approximation ionization threshold, J. Chem. Phys. 108, 4439-4449.
    • (1998) J. Chem. Phys. , vol.108 , pp. 4439-4449
    • Casida, M.E.1    Jamorski, C.2    Casida, K.C.3    Salahub, D.R.4
  • 63
    • 0037072217 scopus 로고    scopus 로고
    • Efficient use of the resolution of the identity approximation in time-dependent density functional calculations with hybrid functionals
    • Neese, F., and Olbrich, G. (2002) Efficient use of the Resolution of the Identity Approximation in Time-Dependent Density Functional Calculations with Hybrid Functionals, Chem. Phys. Lett. 362, 170-178.
    • (2002) Chem. Phys. Lett. , vol.362 , pp. 170-178
    • Neese, F.1    Olbrich, G.2
  • 64
    • 0035935302 scopus 로고    scopus 로고
    • Theoretical analysis of electronic absorption spectra of vitamin B12 models
    • Andruniów, T., Kozlowski, P. M., and Zgierski, M. Z. (2001) Theoretical analysis of electronic absorption spectra of vitamin B12 models, J. Chem. Phys. 115, 7522-7533.
    • (2001) J. Chem. Phys. , vol.115 , pp. 7522-7533
    • Andruniów, T.1    Kozlowski, P.M.2    Zgierski, M.Z.3
  • 66
    • 0039246584 scopus 로고
    • X-ray spectroscopic studies of nickel complexes, with application to the structure of nickel sites in hydrogenases
    • Colpas, G. J., Maroney, M. J., Bagyinka, C., Kumar, M., Willis, W. S., Suib, S. L., Mascharak, P. K., and Baidya, N. (1991) X-ray spectroscopic studies of nickel complexes, with application to the structure of nickel sites in hydrogenases, Inorg. Chem. 30, 920-928.
    • (1991) Inorg. Chem. , vol.30 , pp. 920-928
    • Colpas, G.J.1    Maroney, M.J.2    Bagyinka, C.3    Kumar, M.4    Willis, W.S.5    Suib, S.L.6    Mascharak, P.K.7    Baidya, N.8
  • 67
    • 33845273466 scopus 로고
    • Polarized X-ray absorption edge spectroscopy of single-crystal copper(II) complexes
    • Smith, T. A., Penner-Hahn, J. E., Berding, M. A., Doniach, S., and Hodgson, K. O. (1985) Polarized X-ray absorption edge spectroscopy of single-crystal copper(II) complexes, J. Am. Chem. Soc. 107, 5945-5955.
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 5945-5955
    • Smith, T.A.1    Penner-Hahn, J.E.2    Berding, M.A.3    Doniach, S.4    Hodgson, K.O.5
  • 69
    • 0024557106 scopus 로고
    • Structural and spectroscopic characterization of exogenous ligand binding to isolated factor F430 and its configurational isomers
    • Shiemke, A. K., Kaplan, W. A., Hamilton, C. L., Shelnutt, J. A., and Scott, R. A. (1989) Structural and spectroscopic characterization of exogenous ligand binding to isolated factor F430 and its configurational isomers, J. Biol. Chem. 264, 7276-7284.
    • (1989) J. Biol. Chem. , vol.264 , pp. 7276-7284
    • Shiemke, A.K.1    Kaplan, W.A.2    Hamilton, C.L.3    Shelnutt, J.A.4    Scott, R.A.5
  • 70
    • 0024962185 scopus 로고
    • 430. Axial ligation equilibrium between square-planar and bis-aquo species in aqueous solution
    • 430. Axial ligation equilibrium between square-planar and bis-aquo species in aqueous solution, J. Biol. Chem. 264, 11236-11245.
    • (1989) J. Biol. Chem. , vol.264 , pp. 11236-11245
    • Shiemke, A.K.1    Shelnutt, J.A.2    Scott, R.A.3
  • 71
    • 0004142029 scopus 로고
    • University of Georgia, Athens, GA
    • Li, M. (1993) in Chemistry, University of Georgia, Athens, GA.
    • (1993) Chemistry
    • Li, M.1
  • 72
    • 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
  • 78
    • 1842390409 scopus 로고
    • Structural modeling of small molecules by NMR: Solution-state structure of 12,13-diepimeric coenzyme F430 and comparison with the X-ray structure of the pentamethyl ester derivative
    • Won, H., Olson, K. D., Hare, D. R., Wolfe, R. S., Kratky, C., and Summers, M. F. (1992) Structural modeling of small molecules by NMR: Solution-state structure of 12,13-diepimeric coenzyme F430 and comparison with the X-ray structure of the pentamethyl ester derivative, J. Am. Chem. Soc. 114, 6880-6892.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 6880-6892
    • Won, H.1    Olson, K.D.2    Hare, D.R.3    Wolfe, R.S.4    Kratky, C.5    Summers, M.F.6
  • 80
    • 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. G., 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.G.1    Mahlert, F.2    Duin, E.C.3    Goubeaud, M.4    Shima, S.5    Thauer, R.K.6    Lamzin, V.7    Ermler, U.8
  • 81
    • 84940935551 scopus 로고    scopus 로고
    • 430
    • (Kadish, K. M., Smith, K. M., and Guilard, R., Eds.), Academic Press, New York
    • 430, in The Porphyrin Handbook (Kadish, K. M., Smith, K. M., and Guilard, R., Eds.) pp 205-228, Academic Press, New York.
    • (2003) The Porphyrin Handbook , pp. 205-228
    • Ragsdale, S.W.1
  • 82
    • 0001549105 scopus 로고
    • Zur kenntnis des faktors F430 aus methanogenen bakterien: Uber die natur der isolierungsartefakte von F430, ein beitrag zur chemie von F430 und zur konformationellen stereochemie der ligandperipherie von hydroporphinoiden nickel(II)-komplexen
    • Pfaltz, A., Livingston, D. A., Jaun, B., Diekert, G., Thauer, R. K., and Eschenmoser, A. (1985) Zur Kenntnis des Faktors F430 aus methanogenen Bakterien: Uber die Natur der Isolierungsartefakte von F430, ein Beitrag zur Chemie von F430 und zur konformationellen Stereochemie der Ligandperipherie von hydroporphinoiden Nickel(II)-Komplexen, Helv. Chim. Acta 68, 1338-1358.
    • (1985) Helv. Chim. Acta , vol.68 , pp. 1338-1358
    • Pfaltz, A.1    Livingston, D.A.2    Jaun, B.3    Diekert, G.4    Thauer, R.K.5    Eschenmoser, A.6
  • 83
    • 0001613220 scopus 로고
    • Studies on the terminal reaction in the biosynthesis of methionine
    • Weissbach, H., Peterkofsky, A., Redfield, B. G., and Dickerman, H. (1963) Studies on the Terminal Reaction in the Biosynthesis of Methionine, J. Biol. Chem. 238, 3318-3324.
    • (1963) J. Biol. Chem. , vol.238 , pp. 3318-3324
    • Weissbach, H.1    Peterkofsky, A.2    Redfield, B.G.3    Dickerman, H.4
  • 84
    • 0032482056 scopus 로고    scopus 로고
    • Amine additives greatly expand the scope of asymmetric hydrosilylation of imines
    • Verdaguer, X., Lange, U. E. W., and Buchwald, S. L. (1998) Amine Additives Greatly Expand the Scope of Asymmetric Hydrosilylation of Imines, Angew. Chem., Int. Ed., 1103-1107.
    • (1998) Angew. Chem., Int. Ed. , pp. 1103-1107
    • Verdaguer, X.1    Lange, U.E.W.2    Buchwald, S.L.3
  • 85
    • 0001012323 scopus 로고
    • Selective reductions. XIII. Reaction of 2-cyclopentenones with representative complex hydrides. Aluminum hydride as a selective reagent for the reduction of the carbonyl group in 2-cyclopentenones
    • Brown, H. C., and Hess, H. M. (1969) Selective reductions. XIII. Reaction of 2-cyclopentenones with representative complex hydrides. Aluminum hydride as a selective reagent for the reduction of the carbonyl group in 2-cyclopentenones, J. Org. Chem. 34, 2206-2209.
    • (1969) J. Org. Chem. , vol.34 , pp. 2206-2209
    • Brown, H.C.1    Hess, H.M.2
  • 86
    • 0000643775 scopus 로고
    • Sodium borohydride reduction of conjugated aldehydes and ketones
    • Johnson, M. R., and Rickborn, B. (1970) Sodium borohydride reduction of conjugated aldehydes and ketones, J. Org. Chem. 35, 1041-1045.
    • (1970) J. Org. Chem. , vol.35 , pp. 1041-1045
    • Johnson, M.R.1    Rickborn, B.2
  • 87
    • 0342697384 scopus 로고
    • Asymmetric boron-catalyzed reactions
    • Deloux, L., and Srebnik, M. (1993) Asymmetric boron-catalyzed reactions, Chem. Rev. 93, 763-784.
    • (1993) Chem. Rev. , vol.93 , pp. 763-784
    • Deloux, L.1    Srebnik, M.2
  • 88
    • 0023871069 scopus 로고
    • Biosynthesis of coenzyme F430 in methanogenic bacteria. Identification of 15,17(3)-seco-F430-17(3)-acid as an intermediate
    • Pfaltz, A., Kobelt, A., Huster, R., and Thauer, R. K. (1987) Biosynthesis of coenzyme F430 in methanogenic bacteria. Identification of 15,17(3)-seco-F430-17(3)-acid as an intermediate, Eur. J. Biochem. 170, 459-467.
    • (1987) Eur. J. Biochem. , vol.170 , pp. 459-467
    • Pfaltz, A.1    Kobelt, A.2    Huster, R.3    Thauer, R.K.4


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