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Volumn 28, Issue 3-4, 2007, Pages 123-171

Coordination and bioinorganic chemistry of aryl-appended tris(2-pyridylmethyl)amine ligands

Author keywords

Carboxylate shift; Cobalt; Copper; Iron; Manganese; Nickel; Nitrogen ligands; Oxygen activation; Zinc

Indexed keywords


EID: 34548495289     PISSN: 02603594     EISSN: 15489574     Source Type: Journal    
DOI: 10.1080/02603590701572940     Document Type: Article
Times cited : (14)

References (110)
  • 1
    • 11044220836 scopus 로고    scopus 로고
    • The coordination chemistry of tripodal tetraamine ligands
    • Blackman, A. G. 2005. The coordination chemistry of tripodal tetraamine ligands. Polyhedron, 24, 1-39.
    • (2005) Polyhedron , vol.24 , pp. 1-39
    • Blackman, A.G.1
  • 2
    • 31644439071 scopus 로고    scopus 로고
    • Bioinorganic chemistry of group 12 complexes supported by tetradentate tripodal ligands having internal hydrogen bond donors
    • Berreau, L. M. 2006. Bioinorganic chemistry of group 12 complexes supported by tetradentate tripodal ligands having internal hydrogen bond donors. Eur. J. Inorg. Chem., 273-283.
    • (2006) Eur. J. Inorg. Chem , pp. 273-283
    • Berreau, L.M.1
  • 4
    • 1642458294 scopus 로고    scopus 로고
    • Relative importance of hydrogen bonding and coordinating groups in modulating zinc-water acidity
    • Mareque-Rivas, J. C., R. Prabaharan, and R. T. M. de Rosales, 2004. Relative importance of hydrogen bonding and coordinating groups in modulating zinc-water acidity. Chem. Commun., 76-77.
    • (2004) Chem. Commun , pp. 76-77
    • Mareque-Rivas, J.C.1    Prabaharan, R.2    de Rosales, R.T.M.3
  • 5
    • 4744338220 scopus 로고    scopus 로고
    • Preparation and structural characterization of a novel dicoper(II) complex with a terminal hydroxide: A structural model of an active site in phosphohydrolases
    • Arii, H., Y. Funahashi, K. Jitsukawa, and H. Masuda, 2003. Preparation and structural characterization of a novel dicoper(II) complex with a terminal hydroxide: A structural model of an active site in phosphohydrolases. Dalton Trans., 2115-2116.
    • (2003) Dalton Trans , pp. 2115-2116
    • Arii, H.1    Funahashi, Y.2    Jitsukawa, K.3    Masuda, H.4
  • 6
    • 1642430579 scopus 로고    scopus 로고
    • Thermal stability and absorption spectroscopic behavior of (μ-peroxo)dicopper complexes regulated with intramolecular hydrogen bonding interactions
    • Yamaguchi, S., A. Wada, Y. Funahashi, S. Nagatomo, T. Kitagawa, K. Jitsukawa, and H. Masuda, 2003. Thermal stability and absorption spectroscopic behavior of (μ-peroxo)dicopper complexes regulated with intramolecular hydrogen bonding interactions. Eur. J. Inorg. Chem., 4378-4386.
    • (2003) Eur. J. Inorg. Chem , pp. 4378-4386
    • Yamaguchi, S.1    Wada, A.2    Funahashi, Y.3    Nagatomo, S.4    Kitagawa, T.5    Jitsukawa, K.6    Masuda, H.7
  • 8
    • 0038500742 scopus 로고    scopus 로고
    • Preparation and characterization of hydroxo-zinc(II) complex surrounded with hydrogen bonding and hydrophobic interaction groups. A structural/functional model of carbonic anhydrases
    • Yamaguchi, S., I. Tokairin, Y. Wakita, Y. Funahashi, K. Jitsukawa, and H. Masuda, 2003. Preparation and characterization of hydroxo-zinc(II) complex surrounded with hydrogen bonding and hydrophobic interaction groups. A structural/functional model of carbonic anhydrases. Chem. Lett., 32, 406-407.
    • (2003) Chem. Lett , vol.32 , pp. 406-407
    • Yamaguchi, S.1    Tokairin, I.2    Wakita, Y.3    Funahashi, Y.4    Jitsukawa, K.5    Masuda, H.6
  • 9
    • 0037152395 scopus 로고    scopus 로고
    • Structural and spectroscopic features of a cis (hydroxo)-Fe(III)-(carboxylato) configuration as an active site model for lipoxygenases
    • Ogo, S., R. Yamahara, M. Roach, T. Suenobu, M. Aki, T. Ogura, T. Kitagawa, H. Masuda, S. Fukuzumi, and Y. Watanabe, 2002. Structural and spectroscopic features of a cis (hydroxo)-Fe(III)-(carboxylato) configuration as an active site model for lipoxygenases. Inorg. Chem., 41, 5513-5520.
    • (2002) Inorg. Chem , vol.41 , pp. 5513-5520
    • Ogo, S.1    Yamahara, R.2    Roach, M.3    Suenobu, T.4    Aki, M.5    Ogura, T.6    Kitagawa, T.7    Masuda, H.8    Fukuzumi, S.9    Watanabe, Y.10
  • 10
    • 0001069677 scopus 로고    scopus 로고
    • Synthesis and characterization of novel alkylperoxo mononuclear iron(III) complexes with a tripodal pyridylamine ligand: A model for peroxo intermediates in reactions catalyzed by non-heme iron enzymes
    • Wada, A., S. Ogo, Y. Watanabe, M. Mukai, T. Kitagawa, K. Jitsukawa, H. Masuda, and H. Einaga, 1999. Synthesis and characterization of novel alkylperoxo mononuclear iron(III) complexes with a tripodal pyridylamine ligand: A model for peroxo intermediates in reactions catalyzed by non-heme iron enzymes. Inorg. Chem., 38, 3592-3593.
    • (1999) Inorg. Chem , vol.38 , pp. 3592-3593
    • Wada, A.1    Ogo, S.2    Watanabe, Y.3    Mukai, M.4    Kitagawa, T.5    Jitsukawa, K.6    Masuda, H.7    Einaga, H.8
  • 12
    • 0035851674 scopus 로고    scopus 로고
    • SOD activities of the copper complexes with tripodal polypyridylamine ligands having a hydrogen bonding site
    • Jitsukawa, K., M. Harata, H. Arii, H. Sakurai, and H. Masuda, 2001. SOD activities of the copper complexes with tripodal polypyridylamine ligands having a hydrogen bonding site. Inorg. Chim. Acta., 324, 108-116.
    • (2001) Inorg. Chim. Acta , vol.324 , pp. 108-116
    • Jitsukawa, K.1    Harata, M.2    Arii, H.3    Sakurai, H.4    Masuda, H.5
  • 14
    • 0031900123 scopus 로고    scopus 로고
    • Structural and spectroscopic characterization of a mononuclear hydroperoxo-copper(II) complex with tripodal pyridylamine ligands
    • Wada, A., M. Harata, K. Hasegawa, K. Jitsukawa, H. Masuda, M. Mukai, T. Kitagawa, and H. Einaga, 1998. Structural and spectroscopic characterization of a mononuclear hydroperoxo-copper(II) complex with tripodal pyridylamine ligands. Angew. Chem. Int. Ed. Engl., 37, 798-799.
    • (1998) Angew. Chem. Int. Ed. Engl , vol.37 , pp. 798-799
    • Wada, A.1    Harata, M.2    Hasegawa, K.3    Jitsukawa, K.4    Masuda, H.5    Mukai, M.6    Kitagawa, T.7    Einaga, H.8
  • 15
    • 0001581146 scopus 로고    scopus 로고
    • Preparations, structures, and properties of copper(II) complexes with a new tripodal tetradentate ligand, N-(2-pyridylmethyl)bis(6-pivaloylamido-2- pyridylmethyl)amine, and reactivities of the Cu(I) complex with dioxygen
    • Harata, M., K. Hasegawa, K. Jitsukawa, H. Masuda, and H. Einaga, 1998. Preparations, structures, and properties of copper(II) complexes with a new tripodal tetradentate ligand, N-(2-pyridylmethyl)bis(6-pivaloylamido-2- pyridylmethyl)amine, and reactivities of the Cu(I) complex with dioxygen. Bull. Chem. Soc. Jpn., 71, 1031-1038.
    • (1998) Bull. Chem. Soc. Jpn , vol.71 , pp. 1031-1038
    • Harata, M.1    Hasegawa, K.2    Jitsukawa, K.3    Masuda, H.4    Einaga, H.5
  • 16
    • 0001574204 scopus 로고    scopus 로고
    • Preparations, structures, and properties of Cu(II) complexes with tripodal tetradentate ligand, tris(6-pivaloylamino-2-pyridylmethyl)amine (htppa), and reaction of its Cu(I) complex with dioxygen
    • Harata, M., K. Jitsukawa, H. Masuda, and H. Einaga, 1998. Preparations, structures, and properties of Cu(II) complexes with tripodal tetradentate ligand, tris(6-pivaloylamino-2-pyridylmethyl)amine (htppa), and reaction of its Cu(I) complex with dioxygen. Bull. Chem. Soc. Jpn., 71, 637-645.
    • (1998) Bull. Chem. Soc. Jpn , vol.71 , pp. 637-645
    • Harata, M.1    Jitsukawa, K.2    Masuda, H.3    Einaga, H.4
  • 17
    • 0000969116 scopus 로고    scopus 로고
    • Independent synthesis and structural characterization of a mononuclear copper-hydroxide complex previously assigned as a copper-superoxide species
    • Berreau, L. M., S. Mahapatra, J. A. Halfen, V. G. Young, Jr., and W. B. Tolman, 1996. Independent synthesis and structural characterization of a mononuclear copper-hydroxide complex previously assigned as a copper-superoxide species. Inorg. Chem., 35, 6339-6342.
    • (1996) Inorg. Chem , vol.35 , pp. 6339-6342
    • Berreau, L.M.1    Mahapatra, S.2    Halfen, J.A.3    Young Jr., V.G.4    Tolman, W.B.5
  • 18
    • 0027536105 scopus 로고
    • Reduction potentials and their pH dependence in site-directed-mutant forms of azurin from Pseudomonas aeruginosa
    • Pascher, T., B. G. Karlsson, M. Nordling, B. G. Malmstrom, and T. Vanngard, 1993. Reduction potentials and their pH dependence in site-directed-mutant forms of azurin from Pseudomonas aeruginosa. Eur. J. Biochem., 212, 289-296.
    • (1993) Eur. J. Biochem , vol.212 , pp. 289-296
    • Pascher, T.1    Karlsson, B.G.2    Nordling, M.3    Malmstrom, B.G.4    Vanngard, T.5
  • 19
    • 0000116867 scopus 로고
    • Three-dimensional macrocyclic encapsulation reactions. II. Synthesis and properties of nonoctahedral clathro chelates derived from tris(2-aldoximo-6-pyridyl)phosphine and boron trifluoride or tetrafluoroborate
    • Parks, J. E., B. E. Wagner, and R. H. Holm, 1971. Three-dimensional macrocyclic encapsulation reactions. II. Synthesis and properties of nonoctahedral clathro chelates derived from tris(2-aldoximo-6-pyridyl)phosphine and boron trifluoride or tetrafluoroborate. Inorg. Chem., 10, 2472-2478.
    • (1971) Inorg. Chem , vol.10 , pp. 2472-2478
    • Parks, J.E.1    Wagner, B.E.2    Holm, R.H.3
  • 20
    • 0035959023 scopus 로고    scopus 로고
    • 3 complex. Inorg. Chem., 40, 4803-4806.
    • 3 complex. Inorg. Chem., 40, 4803-4806.
  • 21
    • 0000774001 scopus 로고
    • Synthesis, cyclic voltammetry, and X-ray crystal structures of copper(I) and copper(II) complexes of tris((6-phenyl-2-pyridyl)methyl)amine (TPPA)
    • Chuang, C., K. Lim, Q. Chen, J. Zubieta, and J. W. Canary, 1995. Synthesis, cyclic voltammetry, and X-ray crystal structures of copper(I) and copper(II) complexes of tris((6-phenyl-2-pyridyl)methyl)amine (TPPA). Inorg. Chem., 34, 2562-2568.
    • (1995) Inorg. Chem , vol.34 , pp. 2562-2568
    • Chuang, C.1    Lim, K.2    Chen, Q.3    Zubieta, J.4    Canary, J.W.5
  • 22
    • 0242609386 scopus 로고    scopus 로고
    • First row divalent transition metal complexes of aryl-appended tris((pyridyl)methyl)amine ligands: Syntheses, structures, electrochemistry, and hydroxamate binding properties
    • Makowska-Grzyska, M. M., E. Szajna, C. Shipley, A. M. Arif, M. H. Mitchell, J. A. Halfen, and L. M. Berreau, 2003. First row divalent transition metal complexes of aryl-appended tris((pyridyl)methyl)amine ligands: Syntheses, structures, electrochemistry, and hydroxamate binding properties. Inorg. Chem., 42, 7472-7488.
    • (2003) Inorg. Chem , vol.42 , pp. 7472-7488
    • Makowska-Grzyska, M.M.1    Szajna, E.2    Shipley, C.3    Arif, A.M.4    Mitchell, M.H.5    Halfen, J.A.6    Berreau, L.M.7
  • 23
    • 0037467108 scopus 로고    scopus 로고
    • Jensen, M. P., S. J. Lange, M. P. Mehn, E. L. Que, and L. Que, Jr., 2003. Biomimetic aryl hydroxylation derived from alkyl hydroperoxide at a nonheme iron center. Evidence for an Fe(IV)=O oxidant. J. Am. Chem. Soc., 125, 2113-2128.
    • Jensen, M. P., S. J. Lange, M. P. Mehn, E. L. Que, and L. Que, Jr., 2003. Biomimetic aryl hydroxylation derived from alkyl hydroperoxide at a nonheme iron center. Evidence for an Fe(IV)=O oxidant. J. Am. Chem. Soc., 125, 2113-2128.
  • 24
    • 33748574614 scopus 로고    scopus 로고
    • 2 to bis[2-(2,3-dihydroxyphenyl)-6-pyridylmethyl](2-pyridylmethyl)amine: Access to a diiron(III) compound with an unusual petagonal-bipyramidal/square pyramidal environment
    • 2 to bis[2-(2,3-dihydroxyphenyl)-6-pyridylmethyl](2-pyridylmethyl)amine: Access to a diiron(III) compound with an unusual petagonal-bipyramidal/square pyramidal environment. Chem. Eur. J., 12, 6660-6668.
    • (2006) Chem. Eur. J , vol.12 , pp. 6660-6668
    • Machkour, A.1    Thallaj, N.K.2    Benhamou, L.3    Lachkar, M.4    Mandon, D.5
  • 26
    • 0000351748 scopus 로고    scopus 로고
    • Solid state and solution characterization of chiral, conformationally mobile tripodal ligands
    • Canary, J. W., C. S. Allen, J. M. Castagnetto, Y.-H. Chiu, P. J. Toscano, and Y. Wang, 1998. Solid state and solution characterization of chiral, conformationally mobile tripodal ligands. Inorg. Chem., 37, 6255-6262.
    • (1998) Inorg. Chem , vol.37 , pp. 6255-6262
    • Canary, J.W.1    Allen, C.S.2    Castagnetto, J.M.3    Chiu, Y.-H.4    Toscano, P.J.5    Wang, Y.6
  • 27
    • 84972865128 scopus 로고
    • The influence of phenyl substituents on the redox potentials of sterically hindered tripodal ligand/copper complexes
    • Chuang, C.-L., K. Lim, and J. W. Canary, 1995. The influence of phenyl substituents on the redox potentials of sterically hindered tripodal ligand/copper complexes. Supramolecular Chemistry., 5, 39-43.
    • (1995) Supramolecular Chemistry , vol.5 , pp. 39-43
    • Chuang, C.-L.1    Lim, K.2    Canary, J.W.3
  • 28
    • 0036027056 scopus 로고    scopus 로고
    • Structures and properties of 6-aryl substituted tris(2-pyridylmethyl)amine transition metal complexes
    • He, Z., D. C. Craig, and S. B. Colbran, 2002. Structures and properties of 6-aryl substituted tris(2-pyridylmethyl)amine transition metal complexes. J. Chem. Soc., Dalton Trans., 4224-4235.
    • (2002) J. Chem. Soc., Dalton Trans , pp. 4224-4235
    • He, Z.1    Craig, D.C.2    Colbran, S.B.3
  • 29
    • 0001580017 scopus 로고    scopus 로고
    • Synthesis and cyclic voltammetry studies of copper complexes of bromo- and alkoxyphenyl-substituted derivatives of tris(2-pyridylmethyl)amine: Influence of cation-alkoxy interactions on copper redox potentials
    • Chuang, C.-L., O. dos Santos, X. Xu, and J. W. Canary, 1997. Synthesis and cyclic voltammetry studies of copper complexes of bromo- and alkoxyphenyl-substituted derivatives of tris(2-pyridylmethyl)amine: Influence of cation-alkoxy interactions on copper redox potentials. Inorg. Chem., 36, 1967-1972.
    • (1997) Inorg. Chem , vol.36 , pp. 1967-1972
    • Chuang, C.-L.1    dos Santos, O.2    Xu, X.3    Canary, J.W.4
  • 30
    • 13244279450 scopus 로고    scopus 로고
    • Neutral acetohydroxamic acid coordination to a mononuclear Ni(II) center stabilized by an intramolecular hydrogen-bonding interaction
    • Rudzka, K., M. M. Makowska-Grzyska, E. Szajna, A. M. Arif, and L. M. Berreau, 2005. Neutral acetohydroxamic acid coordination to a mononuclear Ni(II) center stabilized by an intramolecular hydrogen-bonding interaction. Chem. Commun., 489-491.
    • (2005) Chem. Commun , pp. 489-491
    • Rudzka, K.1    Makowska-Grzyska, M.M.2    Szajna, E.3    Arif, A.M.4    Berreau, L.M.5
  • 31
    • 26944452063 scopus 로고    scopus 로고
    • Chemistry of a Ni(II) acetohydroxamic acid complex: Formation, reactivity with water, and attempted preparation of zinc and cobalt analogues
    • Rudzka, K., A. M. Arif, and L. M. Berreau, 2005. Chemistry of a Ni(II) acetohydroxamic acid complex: Formation, reactivity with water, and attempted preparation of zinc and cobalt analogues. Inorg. Chem., 44, 7234-7242.
    • (2005) Inorg. Chem , vol.44 , pp. 7234-7242
    • Rudzka, K.1    Arif, A.M.2    Berreau, L.M.3
  • 32
    • 0345017212 scopus 로고    scopus 로고
    • Geometry-dependent phosphodiester hydrolysis catalyzed by binuclear copper complexes
    • Zhu, L., O. dos Santos, C. W. Koo, M. Rybstein, L. Pape, and J. W. Canary, 2003. Geometry-dependent phosphodiester hydrolysis catalyzed by binuclear copper complexes. Inorg. Chem., 42, 7912-7920.
    • (2003) Inorg. Chem , vol.42 , pp. 7912-7920
    • Zhu, L.1    dos Santos, O.2    Koo, C.W.3    Rybstein, M.4    Pape, L.5    Canary, J.W.6
  • 33
    • 19944411487 scopus 로고    scopus 로고
    • Zinc complex chemistry of N,N,O ligands providing a hydrophobic cavity
    • Gross, F. and H. Vahrenkamp, 2005. Zinc complex chemistry of N,N,O ligands providing a hydrophobic cavity. Inorg. Chem., 44, 3321-3329.
    • (2005) Inorg. Chem , vol.44 , pp. 3321-3329
    • Gross, F.1    Vahrenkamp, H.2
  • 34
    • 0037152382 scopus 로고    scopus 로고
    • 2 complexes with tris(2-pyridylmethyl)amine derivatives bis-α-substituted with bulky groups. Structures and spectroscopic comparative studies
    • 2 complexes with tris(2-pyridylmethyl)amine derivatives bis-α-substituted with bulky groups. Structures and spectroscopic comparative studies. Inorg. Chem., 41, 5364-5372.
    • (2002) Inorg. Chem , vol.41 , pp. 5364-5372
    • Mandon, D.1    Machkour, A.2    Goetz, S.3    Welter, R.4
  • 35
    • 0033532840 scopus 로고    scopus 로고
    • Lange, S. J., H. Miyake, and L. Que, Jr., 1999. Evidence for a nonheme Fe(IV)=O species in the intramolecular hydroxylation of a phenyl moiety. J. Am. Chem., 121, 6330-6331.
    • Lange, S. J., H. Miyake, and L. Que, Jr., 1999. Evidence for a nonheme Fe(IV)=O species in the intramolecular hydroxylation of a phenyl moiety. J. Am. Chem., 121, 6330-6331.
  • 36
    • 2942754171 scopus 로고    scopus 로고
    • NMR studies of mononuclear octahedral Ni(II) complexes supported by tris((2-pyridyl)methyl)amine-type ligands
    • Szajna, E., P. Dobrowolski, A. L. Fuller, A. M. Arif, and L. M. Berreau, 2004. NMR studies of mononuclear octahedral Ni(II) complexes supported by tris((2-pyridyl)methyl)amine-type ligands. Inorg. Chem., 43, 3988-3997.
    • (2004) Inorg. Chem , vol.43 , pp. 3988-3997
    • Szajna, E.1    Dobrowolski, P.2    Fuller, A.L.3    Arif, A.M.4    Berreau, L.M.5
  • 38
    • 0037415107 scopus 로고    scopus 로고
    • Could redox-switched binding of a redox-active ligand to a copper(II) centre drive a conformational proton pump gate? A synthetic model study
    • He, Z., S. B. Colbran, and D. C. Craig, 2003. Could redox-switched binding of a redox-active ligand to a copper(II) centre drive a conformational proton pump gate? A synthetic model study. Chem. Eur. J., 9, 116-129.
    • (2003) Chem. Eur. J , vol.9 , pp. 116-129
    • He, Z.1    Colbran, S.B.2    Craig, D.C.3
  • 39
    • 0346666964 scopus 로고    scopus 로고
    • Crystal-driven distortion of ligands in copper coordination complexes: Conformational pseudo-enantiomers
    • Xu, X., K. J. Maresca, D. Das, S. Zahn, J. Zubieta, and J. W. Canary, 2002. Crystal-driven distortion of ligands in copper coordination complexes: Conformational pseudo-enantiomers. Chem. Eur. J., 8, 5679-5683.
    • (2002) Chem. Eur. J , vol.8 , pp. 5679-5683
    • Xu, X.1    Maresca, K.J.2    Das, D.3    Zahn, S.4    Zubieta, J.5    Canary, J.W.6
  • 40
    • 0029117927 scopus 로고
    • The CH/π interaction: Significance in molecular recognition
    • Nishio, M., Y. Umezawa, M. Hirota, and Y. Takeuchi, 1995. The CH/π interaction: Significance in molecular recognition. Tetrahedron., 51, 8665-8701.
    • (1995) Tetrahedron , vol.51 , pp. 8665-8701
    • Nishio, M.1    Umezawa, Y.2    Hirota, M.3    Takeuchi, Y.4
  • 43
    • 37049096497 scopus 로고
    • Synthesis, structure, and spectroscopic properties of copper(II) compounds containing nitrogen-sulfur donor ligands; the crystal and molecular structure of aqua[1,7-bis(N-methylbenzimidazol-2′-yl)-2,6-dithiaheptane]copper(II) Perchlorate
    • Addison, A. W., T. N. Rao, J. Reedijk, J. van Rijn, and G. C. Verschoor, 1984. Synthesis, structure, and spectroscopic properties of copper(II) compounds containing nitrogen-sulfur donor ligands; the crystal and molecular structure of aqua[1,7-bis(N-methylbenzimidazol-2′-yl)-2,6-dithiaheptane]copper(II) Perchlorate. J. Chem. Soc., Dalton Trans., 1349-1356.
    • (1984) J. Chem. Soc., Dalton Trans , pp. 1349-1356
    • Addison, A.W.1    Rao, T.N.2    Reedijk, J.3    van Rijn, J.4    Verschoor, G.C.5
  • 44
    • 0000458506 scopus 로고    scopus 로고
    • Iron(II) polyamine chemistry: Variation of spin state and coordination number in solid state and solution with iron(II) tris(2-pyridylmethyl)amine complexes
    • Diebold, A. and K. S. Hagen, 1998. Iron(II) polyamine chemistry: Variation of spin state and coordination number in solid state and solution with iron(II) tris(2-pyridylmethyl)amine complexes. Inorg. Chem., 37, 215-223.
    • (1998) Inorg. Chem , vol.37 , pp. 215-223
    • Diebold, A.1    Hagen, K.S.2
  • 45
    • 0002825114 scopus 로고
    • Spin crossover in iron complexes
    • Gütlich, P. 1981. Spin crossover in iron complexes. Struct. Bonding., 44, 83.
    • (1981) Struct. Bonding , vol.44 , pp. 83
    • Gütlich, P.1
  • 46
    • 0034363907 scopus 로고    scopus 로고
    • Spin crossover phenomena in Fe(II) complexes
    • Gütlich, P., Y. Garcia, and H. A. Goodwin, 2000. Spin crossover phenomena in Fe(II) complexes. Chem. Soc. Rev., 29, 419-427.
    • (2000) Chem. Soc. Rev , vol.29 , pp. 419-427
    • Gütlich, P.1    Garcia, Y.2    Goodwin, H.A.3
  • 47
    • 0542449228 scopus 로고
    • Spin equilibria in iron(II) complexes
    • Toftlund, H. 1989. Spin equilibria in iron(II) complexes. Coord. Chem. Rev., 94, 67-108.
    • (1989) Coord. Chem. Rev , vol.94 , pp. 67-108
    • Toftlund, H.1
  • 50
    • 0042206037 scopus 로고
    • The determination of the paramagnetic susceptibility of substances in solution by nuclear magnetic resonance
    • Evans, D. F. 1959. The determination of the paramagnetic susceptibility of substances in solution by nuclear magnetic resonance. J. Chem. Soc., 2003-2005.
    • (1959) J. Chem. Soc , pp. 2003-2005
    • Evans, D.F.1
  • 51
  • 52
    • 34547228269 scopus 로고    scopus 로고
    • Acireductone dioxygenase (ARD)-type reactivity of a Ni(II) Complex having monoanionic coordination of a model substrate: Product identification and comparisons to unreactive analogues
    • Szajna-Fuller, E., K. Rudzka, A. M. Arif, and L. M. Berreau, 2007. Acireductone dioxygenase (ARD)-type reactivity of a Ni(II) Complex having monoanionic coordination of a model substrate: Product identification and comparisons to unreactive analogues. Inorg. Chem., 46, 5499-5507.
    • (2007) Inorg. Chem , vol.46 , pp. 5499-5507
    • Szajna-Fuller, E.1    Rudzka, K.2    Arif, A.M.3    Berreau, L.M.4
  • 53
    • 34547189743 scopus 로고    scopus 로고
    • Carboxylate coordination chemistry of a mononuclear Ni(II) center in a hydrophobic or hydrogen bond donor secondary environment: Relevance to acireductone dioxygenases
    • Szajna-Fuller, E., B. M. Chambers, A. M. Arif, and L. M. Berreau, 2007. Carboxylate coordination chemistry of a mononuclear Ni(II) center in a hydrophobic or hydrogen bond donor secondary environment: Relevance to acireductone dioxygenases. Inorg. Chem., 46, 5486-5498.
    • (2007) Inorg. Chem , vol.46 , pp. 5486-5498
    • Szajna-Fuller, E.1    Chambers, B.M.2    Arif, A.M.3    Berreau, L.M.4
  • 54
    • 33845960757 scopus 로고    scopus 로고
    • Glyoxalase I-type hemithioacetal isomerization reactivity of a mononuclear Ni(II) deprotonated amide complex
    • Rudzka, K., A. M. Arif, and L. M. Berreau, 2006. Glyoxalase I-type hemithioacetal isomerization reactivity of a mononuclear Ni(II) deprotonated amide complex. J. Am. Chem. Soc., 128, 17018-17023.
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 17018-17023
    • Rudzka, K.1    Arif, A.M.2    Berreau, L.M.3
  • 55
    • 33748496877 scopus 로고    scopus 로고
    • Insights into the catalytic mechanisms of phenylalanine and tryptophan hydroxylase from kinetic isotope effects on aromatic hydroxylation
    • Pavon, J. A. and P. F. Fitzpatrick, 2006. Insights into the catalytic mechanisms of phenylalanine and tryptophan hydroxylase from kinetic isotope effects on aromatic hydroxylation. Biochemistry, 45, 11030-11037.
    • (2006) Biochemistry , vol.45 , pp. 11030-11037
    • Pavon, J.A.1    Fitzpatrick, P.F.2
  • 56
    • 0345492036 scopus 로고    scopus 로고
    • Mechanism of aromatic amino acid hydroxylation
    • Fitzpatrick, P. F. 2003. Mechanism of aromatic amino acid hydroxylation. Biochemistry, 42, 14083-14091.
    • (2003) Biochemistry , vol.42 , pp. 14083-14091
    • Fitzpatrick, P.F.1
  • 59
    • 0032852842 scopus 로고    scopus 로고
    • Tetrahydropterin-dependent amino acid hydroxylases
    • Fitzpatrick, P. F. 1999. Tetrahydropterin-dependent amino acid hydroxylases. Annu. Rev. Biochem., 68, 355-381.
    • (1999) Annu. Rev. Biochem , vol.68 , pp. 355-381
    • Fitzpatrick, P.F.1
  • 60
    • 0031010420 scopus 로고    scopus 로고
    • Crystal structure of tyrosine hydroxylase at 2.3 Å and its implications for inherited neurodegenerative diseases
    • Goodwill, K. E., C. Sabatier, C. Marks, R. Raag, P. F. Fitzpatrick, and R. C Stevens, 1997. Crystal structure of tyrosine hydroxylase at 2.3 Å and its implications for inherited neurodegenerative diseases. Nat. Struct. Biol., 4, 578-585.
    • (1997) Nat. Struct. Biol , vol.4 , pp. 578-585
    • Goodwill, K.E.1    Sabatier, C.2    Marks, C.3    Raag, R.4    Fitzpatrick, P.F.5    Stevens, R.C.6
  • 61
    • 0001749787 scopus 로고    scopus 로고
    • Structural insight into the aromatic amino acid hydroxylases and their disease-related mutant forms
    • Flatmark, T. and R. C. Stevens, 1999. Structural insight into the aromatic amino acid hydroxylases and their disease-related mutant forms. Chem. Rev., 99, 2137-2160.
    • (1999) Chem. Rev , vol.99 , pp. 2137-2160
    • Flatmark, T.1    Stevens, R.C.2
  • 62
    • 3643061399 scopus 로고    scopus 로고
    • A mechanism for hydroxylation by tyrosine hydroxylase based on partitioning of substituted phenylalanines
    • Hillas, P. J. and P. F. Fitzpatrick, 1996. A mechanism for hydroxylation by tyrosine hydroxylase based on partitioning of substituted phenylalanines. Biochemistry, 35, 6969-6975.
    • (1996) Biochemistry , vol.35 , pp. 6969-6975
    • Hillas, P.J.1    Fitzpatrick, P.F.2
  • 63
    • 0000783838 scopus 로고    scopus 로고
    • Pterin-dependent amino acid hydroxylases
    • Kappock, T. J. and J. P. Caradonna, 1996. Pterin-dependent amino acid hydroxylases. Chem. Rev., 96, 2659-2756.
    • (1996) Chem. Rev , vol.96 , pp. 2659-2756
    • Kappock, T.J.1    Caradonna, J.P.2
  • 64
    • 0037165727 scopus 로고    scopus 로고
    • Intrinsic deuterium isotope effects on benzylic hydroxylation by tyrosine hydroxylase
    • Frantom, P. A., R. Pongdee, G. A. Sulikowksi, and P. F. Fitzpatrick, 2002. Intrinsic deuterium isotope effects on benzylic hydroxylation by tyrosine hydroxylase. J. Am. Chem. Soc., 124, 4202-4203.
    • (2002) J. Am. Chem. Soc , vol.124 , pp. 4202-4203
    • Frantom, P.A.1    Pongdee, R.2    Sulikowksi, G.A.3    Fitzpatrick, P.F.4
  • 65
    • 0141645556 scopus 로고    scopus 로고
    • Jensen, M. P., M. P. Mehn, and L. Que, Jr., 2003. Intramolecular aromatic amination through iron-mediated nitrene transfer. Angew. Chem. Int. Ed., 42, 4357-4360.
    • Jensen, M. P., M. P. Mehn, and L. Que, Jr., 2003. Intramolecular aromatic amination through iron-mediated nitrene transfer. Angew. Chem. Int. Ed., 42, 4357-4360.
  • 66
  • 67
    • 33645548612 scopus 로고    scopus 로고
    • Using synthetic chemistry to understand copper protein active sites: A personal perspective
    • Tolman, W. B. 2006. Using synthetic chemistry to understand copper protein active sites: A personal perspective. J. Biol. Inorg. Chem., 11, 261-271.
    • (2006) J. Biol. Inorg. Chem , vol.11 , pp. 261-271
    • Tolman, W.B.1
  • 70
    • 1542288709 scopus 로고    scopus 로고
    • Reactivity of dioxygen-copper systems
    • Lewis, E. A. and W. B. Tolman, 2004. Reactivity of dioxygen-copper systems. Chem. Rev., 104, 1047-1076.
    • (2004) Chem. Rev , vol.104 , pp. 1047-1076
    • Lewis, E.A.1    Tolman, W.B.2
  • 71
    • 29844438770 scopus 로고    scopus 로고
    • Hydroxylation of phenolic compounds by a peroxodicopper(II) complex: Further insight into the mechanism of tyrosinase
    • Palavicini, S., A. Granata, E. Monzani, and L. Casella, 2005. Hydroxylation of phenolic compounds by a peroxodicopper(II) complex: Further insight into the mechanism of tyrosinase. J. Am. Chem. Soc., 127, 18031-18036.
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 18031-18036
    • Palavicini, S.1    Granata, A.2    Monzani, E.3    Casella, L.4
  • 72
    • 84902417564 scopus 로고    scopus 로고
    • McCleverty, J. A. and T. J. Meyer eds, Elsevier, Amsterdam
    • Itoh, S. 2004. In Comprehensive Coordination Chemistry II, McCleverty, J. A. and T. J. Meyer (eds.), vol. 8, pp. 369-393, Elsevier, Amsterdam.
    • (2004) Comprehensive Coordination Chemistry II , vol.8 , pp. 369-393
    • Itoh, S.1
  • 75
    • 0032511358 scopus 로고    scopus 로고
    • Investigation of the reactive oxygen intermediate in an arene hydroxylation reaction performed by xylyl-bridged binuclear copper complexes
    • Pidcock, E., H. V. Obias, C. X. Zhang, K. D. Karlin, and E. I. Solomon, 1998. Investigation of the reactive oxygen intermediate in an arene hydroxylation reaction performed by xylyl-bridged binuclear copper complexes. J. Am. Chem. Soc., 120, 7841-7847.
    • (1998) J. Am. Chem. Soc , vol.120 , pp. 7841-7847
    • Pidcock, E.1    Obias, H.V.2    Zhang, C.X.3    Karlin, K.D.4    Solomon, E.I.5
  • 76
    • 0033583463 scopus 로고    scopus 로고
    • Is the bis(μ-oxo)dicopper core capable of hydroxylating an arene?
    • Holland, P. L., K. R. Rogers, and W. B. Tolman, 1999. Is the bis(μ-oxo)dicopper core capable of hydroxylating an arene? Angew. Chem. Int. Ed., 38, 1139-1142.
    • (1999) Angew. Chem. Int. Ed , vol.38 , pp. 1139-1142
    • Holland, P.L.1    Rogers, K.R.2    Tolman, W.B.3
  • 77
    • 0027378886 scopus 로고
    • A bacterial enzyme that catalyzes the formation of carbon monoxide
    • Wray, J. W. and R. H. Abeles, 1993. A bacterial enzyme that catalyzes the formation of carbon monoxide. J. Biol. Chem., 268, 21466-21469.
    • (1993) J. Biol. Chem , vol.268 , pp. 21466-21469
    • Wray, J.W.1    Abeles, R.H.2
  • 78
    • 0027367423 scopus 로고
    • Purification and characterization of an enzyme involved in oxidative carbon-carbon bond cleavage reactions in the methionine salvage pathway of Klebsiella pneumoniae
    • Myers, R. W., J. W. Wray, S. Fish, and R. H. Abeles, 1993. Purification and characterization of an enzyme involved in oxidative carbon-carbon bond cleavage reactions in the methionine salvage pathway of Klebsiella pneumoniae. J. Biol. Chem., 268, 24785-24791.
    • (1993) J. Biol. Chem , vol.268 , pp. 24785-24791
    • Myers, R.W.1    Wray, J.W.2    Fish, S.3    Abeles, R.H.4
  • 79
    • 0028850881 scopus 로고
    • The methionine salvage pathway in Klebsiella pneumoniae and rat liver. Identification and characterization of two novel dioxygenases
    • Wray, J. W. and R. H. Abeles, 1995. The methionine salvage pathway in Klebsiella pneumoniae and rat liver. Identification and characterization of two novel dioxygenases. J. Biol. Chem., 270, 3147-3153.
    • (1995) J. Biol. Chem , vol.270 , pp. 3147-3153
    • Wray, J.W.1    Abeles, R.H.2
  • 81
    • 0035967509 scopus 로고    scopus 로고
    • Mechanistic studies of two dioxygenases in the methionine salvage pathway of Klebsiella pneumoniae
    • Dai, Y., T. C. Pochapsky, and R. H. Abeles, 2001. Mechanistic studies of two dioxygenases in the methionine salvage pathway of Klebsiella pneumoniae. Biochemistry, 40, 6379-6387.
    • (2001) Biochemistry , vol.40 , pp. 6379-6387
    • Dai, Y.1    Pochapsky, T.C.2    Abeles, R.H.3
  • 82
    • 0037188378 scopus 로고    scopus 로고
    • XAS investigation of the structure and function of Ni in acireductone dioxygenase
    • Al-Mjeni, F., T. Ju, T. C. Pochapsky, and M. J. Maroney, 2002. XAS investigation of the structure and function of Ni in acireductone dioxygenase. Biochemistry, 41, 6761-6769.
    • (2002) Biochemistry , vol.41 , pp. 6761-6769
    • Al-Mjeni, F.1    Ju, T.2    Pochapsky, T.C.3    Maroney, M.J.4
  • 83
    • 0036895878 scopus 로고    scopus 로고
    • Modeling and experiment yields the structure of acireductone dioxygenase from Klebsiella pneumoniae
    • Pochapsky, T. C., S. S. Pochapsky, T. Ju, H. Mo, F. Al-Mjeni, and M. J. Maroney, 2002. Modeling and experiment yields the structure of acireductone dioxygenase from Klebsiella pneumoniae. Nat. Struct. Biol., 9, 966-972.
    • (2002) Nat. Struct. Biol , vol.9 , pp. 966-972
    • Pochapsky, T.C.1    Pochapsky, S.S.2    Ju, T.3    Mo, H.4    Al-Mjeni, F.5    Maroney, M.J.6
  • 84
    • 33645466012 scopus 로고    scopus 로고
    • A refined model for the structure of acireductone dioxygenase from Klebsiella ATCC 8724 incorporating residual dipolar couplings
    • Pochapsky, T. C., S. S. Pochapsky, T. Ju, C. Hoefler, and J. Liang, 2006. A refined model for the structure of acireductone dioxygenase from Klebsiella ATCC 8724 incorporating residual dipolar couplings. J. Biomol. NMR., 34, 117-127.
    • (2006) J. Biomol. NMR , vol.34 , pp. 117-127
    • Pochapsky, T.C.1    Pochapsky, S.S.2    Ju, T.3    Hoefler, C.4    Liang, J.5
  • 85
    • 33749545777 scopus 로고    scopus 로고
    • One protein, two enzymes revisited: A structural entropy switch interconverts the two isoforms of acireductone dioxygenase
    • Ju, T., R. B. Goldsmith, S. C. Chai, M. J. Maroney, S. S. Pochapsky, and T. C Pochapsky, 2006. One protein, two enzymes revisited: A structural entropy switch interconverts the two isoforms of acireductone dioxygenase. J. Mol. Biol., 363, 823-834.
    • (2006) J. Mol. Biol , vol.363 , pp. 823-834
    • Ju, T.1    Goldsmith, R.B.2    Chai, S.C.3    Maroney, M.J.4    Pochapsky, S.S.5    Pochapsky, T.C.6
  • 87
    • 4544384632 scopus 로고    scopus 로고
    • Hydroxamic acids-an intriguing family of enzyme inhibitors and biomedical ligands
    • Marmion, C. J., D. Griffith, and K. B. Nolan, 2004. Hydroxamic acids-an intriguing family of enzyme inhibitors and biomedical ligands. Eur. J. Inorg. Chem., 3003-3016.
    • (2004) Eur. J. Inorg. Chem , pp. 3003-3016
    • Marmion, C.J.1    Griffith, D.2    Nolan, K.B.3
  • 88
    • 0016800324 scopus 로고
    • Inhibition of jack bean urease (EC 3.5.1.5) by acetohydroxamic acid and by phosphoramidate. Equivalent weight for urease
    • Dixon, N. E., C. Gazzola, J. J. Watters, R. I. Blakeley, and B. Zerner, 1975. Inhibition of jack bean urease (EC 3.5.1.5) by acetohydroxamic acid and by phosphoramidate. Equivalent weight for urease. J. Am. Chem. Soc., 97, 4130-4131.
    • (1975) J. Am. Chem. Soc , vol.97 , pp. 4130-4131
    • Dixon, N.E.1    Gazzola, C.2    Watters, J.J.3    Blakeley, R.I.4    Zerner, B.5
  • 89
    • 0019249993 scopus 로고
    • Jack bean urease (EC 3.5.1.5). IV. The molecular size and the mechanism of inhibition by hydroxamic acids. Spectrophotometric titration of enzymes with reversible inhibitors
    • Dixon, N. E., J. A. Hinds, A. K. Fihelly, C. Gazzola, D. J. Winzor, R. L. Blakeley, and B. Zerner, 1980. Jack bean urease (EC 3.5.1.5). IV. The molecular size and the mechanism of inhibition by hydroxamic acids. Spectrophotometric titration of enzymes with reversible inhibitors. Can. J. Biochem., 58, 1323-1334.
    • (1980) Can. J. Biochem , vol.58 , pp. 1323-1334
    • Dixon, N.E.1    Hinds, J.A.2    Fihelly, A.K.3    Gazzola, C.4    Winzor, D.J.5    Blakeley, R.L.6    Zerner, B.7
  • 90
    • 0024514293 scopus 로고
    • Microbial ureases: Significance, regulation, and molecular characterization
    • Mobley, H. L. T. and R. P. Hausinger, 1989. Microbial ureases: Significance, regulation, and molecular characterization. Microbiol. Rev., 53, 85-108.
    • (1989) Microbiol. Rev , vol.53 , pp. 85-108
    • Mobley, H.L.T.1    Hausinger, R.P.2
  • 91
    • 0029163026 scopus 로고    scopus 로고
    • Mobley, H. L. T., M. D. Island, and R. P. Hausinger, 1995. Molecular biology of microbial ureases. Microbiol. Rev., 59, 451-480.
    • Mobley, H. L. T., M. D. Island, and R. P. Hausinger, 1995. Molecular biology of microbial ureases. Microbiol. Rev., 59, 451-480.
  • 92
    • 0024459370 scopus 로고
    • Competitive inhibitors of Klebsiella aerogenes urease. Mechanisms of interaction with the nickel active site
    • Todd, M. J. and R. P. Hausinger, 1989. Competitive inhibitors of Klebsiella aerogenes urease. Mechanisms of interaction with the nickel active site. J. Biol. Chem., 264, 15835-15842.
    • (1989) J. Biol. Chem , vol.264 , pp. 15835-15842
    • Todd, M.J.1    Hausinger, R.P.2
  • 94
    • 0034000386 scopus 로고    scopus 로고
    • The complex of Bacillus pasteurii urease with acetohydroxamate anion from X-ray data at 1.55 Å resolution
    • Benini, S., W. R. Rypniewski, K. S. Wilson, S. Miletti, S. Ciurli, and S. Mangani, 2000. The complex of Bacillus pasteurii urease with acetohydroxamate anion from X-ray data at 1.55 Å resolution. J. Biol. Inorg. Chem., 5, 110-118.
    • (2000) J. Biol. Inorg. Chem , vol.5 , pp. 110-118
    • Benini, S.1    Rypniewski, W.R.2    Wilson, K.S.3    Miletti, S.4    Ciurli, S.5    Mangani, S.6
  • 97
    • 0025298551 scopus 로고
    • The glyoxalase system: New developments towards functional characterization of a metabolic pathway fundamental to biological life
    • Thornalley, P. J. 1990. The glyoxalase system: New developments towards functional characterization of a metabolic pathway fundamental to biological life. Biochem. J., 269, 1-11.
    • (1990) Biochem. J , vol.269 , pp. 1-11
    • Thornalley, P.J.1
  • 98
    • 0032537553 scopus 로고    scopus 로고
    • Overproduction and characterization of a dimeric non-zinc glyoxalase I from Escherichia coli: Evidence for optimal activation by nickel ions
    • Clugston, S. L., J. F. J. Barnard, R. Kinach, D. Miedema, R. Ruman, E. Daub, and J. F. Honek, 1998. Overproduction and characterization of a dimeric non-zinc glyoxalase I from Escherichia coli: Evidence for optimal activation by nickel ions. Biochemistry, 37, 8754-8763.
    • (1998) Biochemistry , vol.37 , pp. 8754-8763
    • Clugston, S.L.1    Barnard, J.F.J.2    Kinach, R.3    Miedema, D.4    Ruman, R.5    Daub, E.6    Honek, J.F.7
  • 99
    • 0942301191 scopus 로고    scopus 로고
    • Investigation of metal binding and activation of Escherichia coli glyoxalase I: Kinetic, thermodynamic and mutagenesis studies
    • Clugston, S. L., R. Yajima, and J. F. Honek, 2004. Investigation of metal binding and activation of Escherichia coli glyoxalase I: Kinetic, thermodynamic and mutagenesis studies. Biochem. J., 377, 309-316.
    • (2004) Biochem. J , vol.377 , pp. 309-316
    • Clugston, S.L.1    Yajima, R.2    Honek, J.F.3
  • 100
    • 4444278762 scopus 로고    scopus 로고
    • A trypanothionedependent glyoxalase I with a prokaryotic ancestry in Leishmania major
    • Vickers, T. J., N. Greig, and A. H. Fairlamb, 2004. A trypanothionedependent glyoxalase I with a prokaryotic ancestry in Leishmania major. Proc Natl. Acad. Sci., 101, 13186-13191.
    • (2004) Proc Natl. Acad. Sci , vol.101 , pp. 13186-13191
    • Vickers, T.J.1    Greig, N.2    Fairlamb, A.H.3
  • 101
    • 0034254431 scopus 로고    scopus 로고
    • Determination of the structure of Escherichia coli glyoxalase I suggests a structural basis for differential metal activation
    • He, M. M., S. L. Clugston, J. F. Honek, and B. W. Matthews, 2000. Determination of the structure of Escherichia coli glyoxalase I suggests a structural basis for differential metal activation. Biochemistry, 39, 8719-8727.
    • (2000) Biochemistry , vol.39 , pp. 8719-8727
    • He, M.M.1    Clugston, S.L.2    Honek, J.F.3    Matthews, B.W.4
  • 102
    • 33751246489 scopus 로고    scopus 로고
    • Klinker, E. J., T. A. Jackson, M. P. Jensen, A. Stubna, G. Juhasz, E. L. Bominaar, E. Munck, and L. Que, Jr., 2006. A tosylimido analogue of a nonheme oxoiron(IV) complex. Angew. Chem. Int. Ed., 45, 7394-7397.
    • Klinker, E. J., T. A. Jackson, M. P. Jensen, A. Stubna, G. Juhasz, E. L. Bominaar, E. Munck, and L. Que, Jr., 2006. A tosylimido analogue of a nonheme oxoiron(IV) complex. Angew. Chem. Int. Ed., 45, 7394-7397.
  • 104
    • 0742287185 scopus 로고    scopus 로고
    • Cupins: The most functionally diverse protein superfamily?
    • Dunwell, J. M., A. Purvis, and S. Khuri, 2004. Cupins: The most functionally diverse protein superfamily? Phytochemistry, 65, 7-17.
    • (2004) Phytochemistry , vol.65 , pp. 7-17
    • Dunwell, J.M.1    Purvis, A.2    Khuri, S.3
  • 106
    • 0347785486 scopus 로고    scopus 로고
    • Heavy atom isotope effects on the reaction catalyzed by the oxalate decarboxylase from Bacillus subtilis
    • Reinhardt, L. A., D. Svedruzic, C. H. Chang, W. W. Cleland, and N. G. J. Richards, 2003. Heavy atom isotope effects on the reaction catalyzed by the oxalate decarboxylase from Bacillus subtilis. J. Am. Chem. Soc., 125, 1244-1252.
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 1244-1252
    • Reinhardt, L.A.1    Svedruzic, D.2    Chang, C.H.3    Cleland, W.W.4    Richards, N.G.J.5
  • 107
    • 2942753912 scopus 로고    scopus 로고
    • Analogs of 1 -phosphonooxy-2,2-dihydroxy-3-oxo-5-(methylthio)pentane, an acyclic intermediate in the methionine salvage pathway: A new preparation and characterization of activity with El enolase/phosphatase from Klebsiella oxytoca
    • Zhang, Y., M. H. Heinsen, M. Kostic, G. M. Pagani, T. V. Riera, I. Perovic, L. Hedstrom, B. B. Snider, and T. C. Pochapsky, 2004. Analogs of 1 -phosphonooxy-2,2-dihydroxy-3-oxo-5-(methylthio)pentane, an acyclic intermediate in the methionine salvage pathway: A new preparation and characterization of activity with El enolase/phosphatase from Klebsiella oxytoca. Bioorg. Med. Chem., 12, 3847-3855.
    • (2004) Bioorg. Med. Chem , vol.12 , pp. 3847-3855
    • Zhang, Y.1    Heinsen, M.H.2    Kostic, M.3    Pagani, G.M.4    Riera, T.V.5    Perovic, I.6    Hedstrom, L.7    Snider, B.B.8    Pochapsky, T.C.9
  • 108
    • 34548490946 scopus 로고    scopus 로고
    • MS Thesis, Utah State University
    • Fuller, A. L. 2005. MS Thesis, Utah State University.
    • (2005)
    • Fuller, A.L.1
  • 110
    • 33751155031 scopus 로고
    • Magnetic exchange through oxalate bridges: Synthesis and characterization of (μ-oxalato)dimetal(II) complexes of manganese, iron, cobalt, nickel, copper, and zinc
    • Glerup, J., P. A. Goodson, D. J. Hodgson, and K. Michelsen, 1995. Magnetic exchange through oxalate bridges: Synthesis and characterization of (μ-oxalato)dimetal(II) complexes of manganese, iron, cobalt, nickel, copper, and zinc. Inorg. Chem., 34, 6255-6264.
    • (1995) Inorg. Chem , vol.34 , pp. 6255-6264
    • Glerup, J.1    Goodson, P.A.2    Hodgson, D.J.3    Michelsen, K.4


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