메뉴 건너뛰기




Volumn 4, Issue 4, 2012, Pages 317-322

Self-assembly of the oxy-tyrosinase core and the fundamental components of phenolic hydroxylation

Author keywords

[No Author keywords available]

Indexed keywords

15 CROWN 5; 15-CROWN-5; COORDINATION COMPOUND; COPPER; CROWN ETHER; HYDROXYBENZOIC ACID DERIVATIVE; IMIDAZOLE; IMIDAZOLE DERIVATIVE; MONOPHENOL MONOOXYGENASE; OXYGEN; PHENOLIC ACID;

EID: 84858786896     PISSN: 17554330     EISSN: 17554349     Source Type: Journal    
DOI: 10.1038/nchem.1284     Document Type: Article
Times cited : (83)

References (47)
  • 1
    • 0001196571 scopus 로고
    • Self-Assembly in synthetic routes to molecular devices-Biological principles and chemical perspectives-A review
    • Lindsey, J. S. Self-assembly in synthetic routes to molecular devices-biological principles and chemical perspectives-a review. New J. Chem. 15, 153-180 (1991).
    • (1991) New J. Chem. , vol.15 , pp. 153-180
    • Lindsey, J.S.1
  • 2
    • 0029811409 scopus 로고    scopus 로고
    • Self-assembly in natural and unnatural systems
    • Philp, D. & Stoddart, J. F. Self-assembly in natural and unnatural systems. Angew. Chem. Int. Ed. 35, 1155-1196 (1996).
    • (1996) Angew. Chem. Int. Ed. , vol.35 , pp. 1155-1196
    • Philp, D.1    Stoddart, J.F.2
  • 3
    • 0037192505 scopus 로고    scopus 로고
    • Self-assembly at all scales
    • Whitesides, G. M. & Grzybowski, B. Self-assembly at all scales. Science 295, 2418-2421 (2002).
    • (2002) Science , vol.295 , pp. 2418-2421
    • Whitesides, G.M.1    Grzybowski, B.2
  • 4
    • 1542378729 scopus 로고    scopus 로고
    • Synthetic analogues of the active sites of iron-sulfur proteins
    • Rao, P. V. & Holm, R. H. Synthetic analogues of the active sites of iron-sulfur proteins. Chem. Rev. 104, 527-559 (2004).
    • (2004) Chem. Rev. , vol.104 , pp. 527-559
    • Rao, P.V.1    Holm, R.H.2
  • 5
    • 0015396025 scopus 로고
    • Structure and properties of a synthetic analog of bacterial iron-sulfur proteins
    • Herskovitz, T. et al. Structure and properties of a synthetic analog of bacterial iron-sulfur proteins. Proc. Natl Acad. Sci. 69, 2437-2442 (1972).
    • (1972) Proc. Natl Acad. Sci. , vol.69 , pp. 2437-2442
    • Herskovitz, T.1
  • 6
    • 38649087966 scopus 로고    scopus 로고
    • Iron-sulfur protein folds, iron-sulfur chemistry, and evolution
    • Meyer, J. Iron-sulfur protein folds, iron-sulfur chemistry, and evolution. J. Biol. Inorg. Chem. 13, 157-170 (2008).
    • (2008) J. Biol. Inorg. Chem. , vol.13 , pp. 157-170
    • Meyer, J.1
  • 7
    • 79959386984 scopus 로고    scopus 로고
    • 2 reactivity of tyrosinase models towards external monophenolic substrates: Molecular mechanism and comparison with the enzyme
    • 2 reactivity of tyrosinase models towards external monophenolic substrates: molecular mechanism and comparison with the enzyme. Chem. Soc. Rev. 40, 4077-4098 (2011).
    • (2011) Chem. Soc. Rev. , vol.40 , pp. 4077-4098
    • Rolff, M.1    Schottenheim, J.2    Decker, H.3    Tuczek, F.4
  • 10
    • 33646827679 scopus 로고    scopus 로고
    • Crystallographic evidence that the dinuclear copper center of tyrosinase is flexible during catalysis
    • Matoba, Y., Kumagai, T., Yamamoto, A., Yoshitsu, H. & Sugiyama, M. Crystallographic evidence that the dinuclear copper center of tyrosinase is flexible during catalysis. J. Biol. Chem. 281, 8981-8990 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 8981-8990
    • Matoba, Y.1    Kumagai, T.2    Yamamoto, A.3    Yoshitsu, H.4    Sugiyama, M.5
  • 11
    • 33746291588 scopus 로고    scopus 로고
    • The first crystal structure of tyrosinase: All questions answered?
    • Decker, H., Schweikardt, T. & Tuczek, F. The first crystal structure of tyrosinase: all questions answered? Angew. Chem. Int. Ed. 45, 4546-4550 (2006).
    • (2006) Angew. Chem. Int. Ed. , vol.45 , pp. 4546-4550
    • Decker, H.1    Schweikardt, T.2    Tuczek, F.3
  • 13
    • 0000910803 scopus 로고
    • Structural and functional models for the dicopper site in hemocyanin. Dioxygen binding by copper complexes of tris(1R-4R-imidazolyl-N)phosphines
    • Lynch, W. E., Kurtz, D. M., Wang, S. K. & Scott, R. A. Structural and functional models for the dicopper site in hemocyanin. dioxygen binding by copper complexes of tris(1R-4R-imidazolyl-N)phosphines. J. Am. Chem. Soc. 116, 11030-11038 (1994).
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 11030-11038
    • Lynch, W.E.1    Kurtz, D.M.2    Wang, S.K.3    Scott, R.A.4
  • 14
    • 33751155737 scopus 로고
    • Sterically hindered tris(imidazolyl)phosphinecopper complexes: Formation and reactivity of a peroxo-dicopper(II) adduct and structure of a dinuclear carbonate-bridged complex
    • Sorrell, T. N., Allen, W. E. & White, P. S. Sterically hindered tris(imidazolyl)phosphinecopper complexes: formation and reactivity of a peroxo-dicopper(II) adduct and structure of a dinuclear carbonate-bridged complex. Inorg. Chem. 34, 952-960 (1995).
    • (1995) Inorg. Chem. , vol.34 , pp. 952-960
    • Sorrell, T.N.1    Allen, W.E.2    White, P.S.3
  • 15
    • 0033486019 scopus 로고    scopus 로고
    • 2-binding of a room temperature stable m-h2-h2-peroxodicopper(II) complex of a sterically hindered hexapyridine dinucleating ligand
    • 2-binding of a room temperature stable m-h2-h2-peroxodicopper(II) complex of a sterically hindered hexapyridine dinucleating ligand. J. Am. Chem. Soc. 121, 11006-11007 (1999).
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 11006-11007
    • Kodera, M.1
  • 16
    • 0001084385 scopus 로고
    • Copper-dioxygen complexes. Inorganic and bioinorganic perspectives
    • Kitajima, N. & Moro-Oka, Y. Copper-dioxygen complexes. Inorganic and bioinorganic perspectives. Chem. Rev. 94, 737-757 (1994).
    • (1994) Chem. Rev. , vol.94 , pp. 737-757
    • Kitajima, N.1    Moro-Oka, Y.2
  • 17
    • 1542304579 scopus 로고    scopus 로고
    • Structure and spectroscopy of copper-dioxygen complexes
    • Mirica, L. M., Ottenwaelder, X. & Stack, T. D. P. Structure and spectroscopy of copper-dioxygen complexes. Chem. Rev. 104, 1013-1045 (2004).
    • (2004) Chem. Rev. , vol.104 , pp. 1013-1045
    • Mirica, L.M.1    Ottenwaelder, X.2    Stack, T.D.P.3
  • 18
    • 1542288709 scopus 로고    scopus 로고
    • Reactivity of dioxygen-copper systems
    • Lewis, E. A. & Tolman, W. B. Reactivity of dioxygen-copper systems. Chem. Rev. 104, 1047-1076 (2004).
    • (2004) Chem. Rev. , vol.104 , pp. 1047-1076
    • Lewis, E.A.1    Tolman, W.B.2
  • 20
    • 0000410535 scopus 로고    scopus 로고
    • Tyrosinase models. Synthesis; Structure; catechol oxidase activity; And phenol monooxygenase activity of a dinuclear copper complex derived from a triamino pentabenzimidazole ligand
    • Monzani, E. et al. Tyrosinase models. Synthesis; structure; catechol oxidase activity; and phenol monooxygenase activity of a dinuclear copper complex derived from a triamino pentabenzimidazole ligand. Inorg. Chem. 37, 553-562 (1998).
    • (1998) Inorg. Chem. , vol.37 , pp. 553-562
    • Monzani, E.1
  • 21
    • 0034603043 scopus 로고    scopus 로고
    • Reversible dioxygen binding and phenol oxygenation in a tyrosinase model system
    • Santagostini, L. et al. Reversible dioxygen binding and phenol oxygenation in a tyrosinase model system. Chem. Eur. J. 6, 519-522 (2000).
    • (2000) Chem. Eur. J. , vol.6 , pp. 519-522
    • Santagostini, L.1
  • 22
    • 0034801452 scopus 로고    scopus 로고
    • Effects of metal ions on physicochemical properties and redox reactivity of phenolates and phenoxyl radicals: Mechanistic insight into hydrogen atom abstraction by phenoxyl radical-metal complexes
    • Itoh, S., Kumei, H., Nagatomo, S., Kitagawa, T. & Fukuzumi, S. Effects of metal ions on physicochemical properties and redox reactivity of phenolates and phenoxyl radicals: mechanistic insight into hydrogen atom abstraction by phenoxyl radical-metal complexes. J. Am. Chem. Soc. 123, 2165-2175 (2001).
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 2165-2175
    • Itoh, S.1    Kumei, H.2    Nagatomo, S.3    Kitagawa, T.4    Fukuzumi, S.5
  • 23
    • 29844438770 scopus 로고    scopus 로고
    • Hydroxylation of phenolic compounds by a peroxodicopper(II) complex: Further insight into the mechanism of tyrosinase
    • Palavicini, S., Granata, A., Monzani, E. & Casella, L. Hydroxylation of phenolic compounds by a peroxodicopper(II) complex: further insight into the mechanism of tyrosinase. J. Am. Chem. Soc. 127, 18031-18036 (2005).
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 18031-18036
    • Palavicini, S.1    Granata, A.2    Monzani, E.3    Casella, L.4
  • 24
    • 21344458566 scopus 로고    scopus 로고
    • Tyrosinase reactivity in a model complex: An alternative hydroxylation mechanism
    • Mirica, L. M. et al. Tyrosinase reactivity in a model complex: an alternative hydroxylation mechanism. Science 308, 1890-1892 (2005).
    • (2005) Science , vol.308 , pp. 1890-1892
    • Mirica, L.M.1
  • 25
    • 72949110855 scopus 로고    scopus 로고
    • 2 chemistry with imidazole containing tripodal tetradentate ligands leading to m-1,2-peroxo-dicopper (II) species
    • 2 chemistry with imidazole containing tripodal tetradentate ligands leading to m-1,2-peroxo-dicopper(II) species. Inorg. Chem. 48, 11297-11309 (2009).
    • (2009) Inorg. Chem. , vol.48 , pp. 11297-11309
    • Lee, Y.1
  • 26
    • 84970562806 scopus 로고
    • The oxidation of phenols with copper-amine catalysts and its relation to the mode of action of tyrosinase: I-V
    • 1021, 1070, 1100, 1107
    • Brackman, W. & Havinga, E. The oxidation of phenols with copper-amine catalysts and its relation to the mode of action of tyrosinase: I-V. Recueil des Travaux Chimiques des Pays-Bas 74, 937, 1021, 1070, 1100, 1107 (1955).
    • (1955) Recueil des Travaux Chimiques des Pays-Bas , vol.74 , pp. 937
    • Brackman, W.1    Havinga, E.2
  • 29
    • 0001079697 scopus 로고
    • Chemistry and structural studies on the dioxygen-binding copper-1,2-dimethylimidazole system
    • Sanyal, I., Karlin, K. D., Strange, R. W. & Blackburn, N. J. Chemistry and structural studies on the dioxygen-binding copper-1,2- dimethylimidazole system. J. Am. Chem. Soc. 115, 11259-11270 (1993).
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 11259-11270
    • Sanyal, I.1    Karlin, K.D.2    Strange, R.W.3    Blackburn, N.J.4
  • 30
  • 31
    • 0000035583 scopus 로고
    • Separation and absorption spectra of a-and b-haemocyanin of helix pomatia
    • Heirwegh, K., Borginon, H. & Lontie, R. Separation and absorption spectra of a-and b-haemocyanin of Helix pomatia. Biochim. Biophys. Acta 48, 517-526 (1961).
    • (1961) Biochim. Biophys. Acta , vol.48 , pp. 517-526
    • Heirwegh, K.1    Borginon, H.2    Lontie, R.3
  • 32
    • 0001400297 scopus 로고
    • Chemical and spectroscopic comparison of the binuclear copper active-site of mollusk and arthropod hemocyanins
    • Himmelwright, R. S., Eickman, N. C., LuBien, C. D. & Solomon, E. I. Chemical and spectroscopic comparison of the binuclear copper active-site of mollusk and arthropod hemocyanins. J. Am. Chem. Soc. 102, 5378-5388 (1980).
    • (1980) J. Am. Chem. Soc. , vol.102 , pp. 5378-5388
    • Himmelwright, R.S.1    Eickman, N.C.2    Lubien, C.D.3    Solomon, E.I.4
  • 33
    • 0142019336 scopus 로고    scopus 로고
    • Complexity with simplicity: A steric continuum of chelating diamines with copper(I) and dioxygen
    • Stack, T. D. P. Complexity with simplicity: a steric continuum of chelating diamines with copper(I) and dioxygen. Dalton Trans. 10, 1881-1889 (2003).
    • (2003) Dalton Trans. , vol.10 , pp. 1881-1889
    • Stack, T.D.P.1
  • 34
    • 78650239137 scopus 로고    scopus 로고
    • Bis(m-oxo) dicopper(III) species of the simplest peralkylated diamine: Enhanced reactivity toward exogenous substrates
    • Kang, P. et al. Bis(m-oxo) dicopper(III) species of the simplest peralkylated diamine: enhanced reactivity toward exogenous substrates. Inorg. Chem. 49, 11030-11038 (2010).
    • (2010) Inorg. Chem. , vol.49 , pp. 11030-11038
    • Kang, P.1
  • 35
    • 61749101090 scopus 로고    scopus 로고
    • Phenolate hydroxylation in a bis(m-oxo)dicopper(III) complex: Lessons from the guanidine/amine series
    • Herres-Pawlis, S. et al. Phenolate hydroxylation in a bis(m-oxo)dicopper(III) complex: lessons from the guanidine/amine series. J. Am. Chem. Soc. 131, 1154-1169 (2009).
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 1154-1169
    • Herres-Pawlis, S.1
  • 37
    • 0142214624 scopus 로고    scopus 로고
    • Kinetic evaluation of phenolase activity of tyrosinase using simplified catalytic reaction system
    • Yamazaki, S. & Itoh, S. Kinetic evaluation of phenolase activity of tyrosinase using simplified catalytic reaction system. J. Am. Chem. Soc. 125, 13034-13035 (2003).
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 13034-13035
    • Yamazaki, S.1    Itoh, S.2
  • 38
    • 0034804162 scopus 로고    scopus 로고
    • 2-peroxo)dicopper(II) complex: Mechanistic insight into the phenolase activity of tyrosinase
    • 2-peroxo)dicopper(II) complex: mechanistic insight into the phenolase activity of tyrosinase. J. Am. Chem. Soc. 123, 6708-6709 (2001).
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 6708-6709
    • Itoh, S.1
  • 39
    • 33845283452 scopus 로고
    • X-Ray absorption edge determination of the oxidation state and coordination number of copper-Application to the type 3 site in rhus vernicifera laccase and its reaction with oxygen
    • Kau, L. S., Spira-Solomon, D. J., Penner-Hahn, J. E., Hodgson, K. O. & Solomon, E. I. X-ray absorption edge determination of the oxidation state and coordination number of copper-application to the type 3 site in Rhus Vernicifera laccase and its reaction with oxygen. J. Am. Chem. Soc. 109, 6433-6442 (1987).
    • (1987) J. Am. Chem. Soc. , vol.109 , pp. 6433-6442
    • Kau, L.S.1    Spira-Solomon, D.J.2    Penner-Hahn, J.E.3    Hodgson, K.O.4    Solomon, E.I.5
  • 40
    • 0030804536 scopus 로고    scopus 로고
    • 2 core: Direct experimental evidence for the presence of Cu(III)
    • 2 core: direct experimental evidence for the presence of Cu(III). J. Am. Chem. Soc. 119, 8578-8579 (1997).
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 8578-8579
    • Dubois, J.L.1
  • 41
    • 7744243956 scopus 로고
    • An electronic structural comparison of copper peroxide complexes of relevance to hemocyanin and tyrosinase active sites
    • Ross, P. K. & Solomon, E. I. An electronic structural comparison of copper peroxide complexes of relevance to hemocyanin and tyrosinase active sites. J. Am. Chem. Soc. 113, 3246-3259 (1991).
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 3246-3259
    • Ross, P.K.1    Solomon, E.I.2
  • 42
    • 0035905357 scopus 로고    scopus 로고
    • Oxygen binding, activation, and reduction to water by copper proteins
    • Solomon, E. I., Chen, P., Metz, M., Lee, S. K. & Palmer, A. E. Oxygen binding, activation, and reduction to water by copper proteins. Angew. Chem. Int. Ed. 40, 4570-4590 (2001).
    • (2001) Angew. Chem. Int. Ed. , vol.40 , pp. 4570-4590
    • Solomon, E.I.1    Chen, P.2    Metz, M.3    Lee, S.K.4    Palmer, A.E.5
  • 43
    • 0037444696 scopus 로고    scopus 로고
    • Natural transition orbitals
    • Martin, R. L. Natural transition orbitals. J. Chem. Phys. 118, 4775-4777 (2003).
    • (2003) J. Chem. Phys. , vol.118 , pp. 4775-4777
    • Martin, R.L.1
  • 45
    • 44149120269 scopus 로고    scopus 로고
    • Copper dioxygen adducts: Formation of bis(m-oxo)dicopper(III) versus (m-1,2)peroxodicopper(II) complexes with small changes in one pyridyl-ligand substituent
    • Maiti, D., Woertink, J. S., Narducci Sarjeant, A. A., Solomon, E. I. & Karlin, K. D. Copper dioxygen adducts: formation of bis(m-oxo) dicopper(III) versus (m-1,2)peroxodicopper(II) complexes with small changes in one pyridyl-ligand substituent. Inorg. Chem. 47, 3787-3800 (2008).
    • (2008) Inorg. Chem. , vol.47 , pp. 3787-3800
    • Maiti, D.1    Woertink, J.S.2    Narducci Sarjeant, A.A.3    Solomon, E.I.4    Karlin, K.D.5
  • 46
    • 0037464327 scopus 로고    scopus 로고
    • 6Tren) ligand
    • 6Tren) ligand. Inorg. Chem. 42, 1800-1806 (2003).
    • (2003) Inorg. Chem. , vol.42 , pp. 1800-1806
    • Weitzer, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.