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Volumn , Issue , 2011, Pages 63-86

Biological Chemistry of O-Quinones

Author keywords

1,2 benzoquinone; cycloaddition; electron transport; melanin; melanogenesis; pulse radiolysis; quinone; rate constants

Indexed keywords


EID: 84874405093     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9783527636150.ch3     Document Type: Chapter
Times cited : (14)

References (72)
  • 2
    • 0001840377 scopus 로고
    • Oxidative reaction mechanism by use of tyrosinase towards synthetic mytilid bivalve adhesive protein precursors
    • Yamamoto, H. and Tatehata, H. (1995) Oxidative reaction mechanism by use of tyrosinase towards synthetic mytilid bivalve adhesive protein precursors. J. Mar. Biotechnol., 2, 95-100
    • (1995) J. Mar. Biotechnol. , vol.2 , pp. 95-100
    • Yamamoto, H.1    Tatehata, H.2
  • 3
    • 0025944379 scopus 로고
    • Molecular mechanisms for mammalian melanogenesis-comparison with insect cuticular sclerotization
    • Sugumaran, M. (1991) Molecular mechanisms for mammalian melanogenesis-comparison with insect cuticular sclerotization. FEBS Lett., 293, 4-9
    • (1991) FEBS Lett , vol.293 , pp. 4-9
    • Sugumaran, M.1
  • 4
    • 0003981866 scopus 로고
    • The evolution of melanogenesis
    • (ed. L. Zeise, M.R. Chedekel, and T.B. Fitzpatrick), Valdemar, Overland Park, KS
    • Riley, P.A. (1995) The evolution of melanogenesis, in Melanin: Its Role in Human Photoprotection (ed. L. Zeise, M.R. Chedekel, and T.B. Fitzpatrick), Valdemar, Overland Park, KS, pp. 11-22
    • (1995) Melanin: Its Role in Human Photoprotection , pp. 11-22
    • Riley, P.A.1
  • 6
  • 7
    • 1342335876 scopus 로고
    • Melanin and melanocytes, in
    • (ed. A. Jarrett), Academic Press, London
    • Riley, P.A. (1974) Melanin and melanocytes, in The Physiology and Pathophysiology of the Skin, vol. 3 (ed. A. Jarrett), Academic Press, London, pp. 1104-1127
    • (1974) The Physiology and Pathophysiology of the Skin , vol.3 , pp. 1104-1127
    • Riley, P.A.1
  • 8
    • 0023322234 scopus 로고
    • Relationship between melanin content and superoxide dismutase (SOD) activity in the liver of various species of animals
    • Sichel, G., Corsaro, C., Scalia, M., Sciuto, S., and Geremia, E. (1987) Relationship between melanin content and superoxide dismutase (SOD) activity in the liver of various species of animals. Cell Biochem. Funct., 5, 123-128
    • (1987) Cell Biochem. Funct. , vol.5 , pp. 123-128
    • Sichel, G.1    Corsaro, C.2    Scalia, M.3    Sciuto, S.4    Geremia, E.5
  • 9
    • 0013608392 scopus 로고    scopus 로고
    • Epidermal melanin: sun screen or waste disposal?
    • Riley, P.A. (1997) Epidermal melanin: sun screen or waste disposal? Biologist, 44, 408-411
    • (1997) Biologist , vol.44 , pp. 408-411
    • Riley, P.A.1
  • 11
    • 0011111187 scopus 로고
    • The crystal structure of catechol
    • Brown, C.J. (1966) The crystal structure of catechol. Acta Crystallogr., 21, 170-174
    • (1966) Acta Crystallogr , vol.21 , pp. 170-174
    • Brown, C.J.1
  • 12
    • 68949218843 scopus 로고    scopus 로고
    • The quinones of benzocyclobutadiene: a computational study
    • Golas, E., Lewars, E., and Liebman, J.F. (2009) The quinones of benzocyclobutadiene: a computational study. J. Phys. Chem. A, 113, 9485-9500
    • (2009) J. Phys. Chem. A , vol.113 , pp. 9485-9500
    • Golas, E.1    Lewars, E.2    Liebman, J.F.3
  • 13
    • 84969764544 scopus 로고    scopus 로고
    • Heterocycle -forming reactions of 1,2-benzoquinones
    • Ramsden, C.A. (2010) Heterocycle -forming reactions of 1,2-benzoquinones. Adv. Heterocycl. Chem., 100, 1-51
    • (2010) Adv. Heterocycl. Chem. , vol.100 , pp. 1-51
    • Ramsden, C.A.1
  • 14
    • 0000979725 scopus 로고
    • Synthetic 1,2-quinones: synthesis and thermal reactions
    • Horspool, W.M. (1969) Synthetic 1,2-quinones: synthesis and thermal reactions. Quart. Rev., 23, 204-235
    • (1969) Quart. Rev. , vol.23 , pp. 204-235
    • Horspool, W.M.1
  • 15
    • 84985598633 scopus 로고
    • Mechanism of purpurogallin formation: an adduct from 3-hydroxy-o-benzoquinone and 4,5 dimethyl-o-benzoquinone
    • D ü rckheimer, W. and Paulus, E.F. (1985) Mechanism of purpurogallin formation: an adduct from 3-hydroxy-o -benzoquinone and 4,5 dimethyl-o -benzoquinone. Angew. Chem. Int. Ed. Engl., 24, 224-225
    • (1985) Angew. Chem. Int. Ed. Engl. , vol.24 , pp. 224-225
    • Dürckheimer, W.1    Paulus, E.F.2
  • 16
    • 0542389349 scopus 로고
    • Hydriergeschwindigkeit und Redoxpotential bei Chinonen
    • Musso, H., Figge, K., and Becker, D.J. (1961) Hydriergeschwindigkeit und Redoxpotential bei Chinonen. Chem. Ber., 94, 1107-1115
    • (1961) Chem. Ber. , vol.94 , pp. 1107-1115
    • Musso, H.1    Figge, K.2    Becker, D.J.3
  • 18
    • 0013595908 scopus 로고
    • Redox reactions of 3,5-di-tert-butyl-12-benzoquinone. Implications for reversal of paper yellowing
    • Jovanovic, S.V., Kónya, K., and Scaiano, J.C. (1995) Redox reactions of 3,5-di-tert -butyl-1,2-benzoquinone. Implications for reversal of paper yellowing. Can. J. Chem., 73, 1803-1810
    • (1995) Can. J. Chem. , vol.73 , pp. 1803-1810
    • Jovanovic, S.V.1    Kónya, K.2    Scaiano, J.C.3
  • 19
    • 32644459309 scopus 로고    scopus 로고
    • Calculation of two-electron reduction potentials for some quinone derivatives in aqueous solution using M ø ller-Plesset perturbation theory
    • Namazian, M., Siahrostami, S., Noorbala, M.R., and Coote, M.L. (2006) Calculation of two-electron reduction potentials for some quinone derivatives in aqueous solution using M ø ller-Plesset perturbation theory. J. Mol. Struct., 759, 245-247
    • (2006) J. Mol. Struct. , vol.759 , pp. 245-247
    • Namazian, M.1    Siahrostami, S.2    Noorbala, M.R.3    Coote, M.L.4
  • 22
    • 84889625604 scopus 로고    scopus 로고
    • Chemistry of melanins
    • 2nd edn (eds J.J. Nordlund R. E. Boissy, V. J. Hearing, R. A. King, W. S. Oetting, and J. -P. Ortonne), Blackwell, Malden, MA
    • Ito, S. and Wakamatsu, K. (2006) Chemistry of melanins, in The Pigmentary System: Physiology and Pathophysiology, 2nd edn (eds J.J. Nordlund, R.E. Boissy, V.J. Hearing, R.A. King, W.S. Oetting, and J.-P. Ortonne), Blackwell, Malden, MA, pp. 282-310
    • (2006) The Pigmentary System: Physiology and Pathophysiology , pp. 282-310
    • Ito, S.1    Wakamatsu, K.2
  • 23
    • 0034700680 scopus 로고    scopus 로고
    • Oxidative cyclisation of N, N -dialkylcatecholamines to heterocyclic betaines via ortho-quinones: synthetic, pulse radiolytic and enzyme studies
    • Clews, J., Cooksey, C.J., Garratt, P.J., Land, E.J., Ramsden, C.A., and Riley, P.A. (2000) Oxidative cyclisation of N, N-dialkylcatecholamines to heterocyclic betaines via ortho-quinones: synthetic, pulse radiolytic and enzyme studies. J. Chem. Soc. Perkin Trans., 1, 4306-4315
    • (2000) J. Chem. Soc. Perkin Trans. , vol.1 , pp. 4306-4315
    • Clews, J.1    Cooksey, C.J.2    Garratt, P.J.3    Land, E.J.4    Ramsden, C.A.5    Riley, P.A.6
  • 24
    • 0030722720 scopus 로고    scopus 로고
    • Evidence of the indirect formation of the catecholic intermediate substrate responsible for the autoactivation kinetics of tyrosinase
    • Cooksey, C.J., Garratt, P.J., Land, E.J., Pavel, S., Ramsden, C.A., Riley, P.A., and Smit, N.P.M. (1997) Evidence of the indirect formation of the catecholic intermediate substrate responsible for the autoactivation kinetics of tyrosinase. J. Biol. Chem., 272, 26226-26235
    • (1997) J. Biol. Chem. , vol.272 , pp. 26226-26235
    • Cooksey, C.J.1    Garratt, P.J.2    Land, E.J.3    Pavel, S.4    Ramsden, C.A.5    Riley, P.A.6    Smit, N.P.M.7
  • 25
    • 0037841882 scopus 로고    scopus 로고
    • Tyrosinase autoactivation and the chemistry of ortho-quinone amines
    • Land, E.J., Ramsden, C.A., and Riley, P.A. (2003) Tyrosinase autoactivation and the chemistry of ortho-quinone amines. Acc. Chem. Res., 36, 300-308
    • (2003) Acc. Chem. Res. , vol.36 , pp. 300-308
    • Land, E.J.1    Ramsden, C.A.2    Riley, P.A.3
  • 26
    • 0017388583 scopus 로고
    • A facile one-step synthesis of cysteinyldopas using mushroom tyrosinase
    • Ito, S. and Prota, G. (1977) A facile one-step synthesis of cysteinyldopas using mushroom tyrosinase. Experientia, 33, 1118-1119
    • (1977) Experientia , vol.33 , pp. 1118-1119
    • Ito, S.1    Prota, G.2
  • 27
    • 0021892899 scopus 로고
    • Tyrosinase-catalyzed conjugation of dopa with glutathione
    • Ito, S., Palumbo, A., and Prota, G. (1985) Tyrosinase-catalyzed conjugation of dopa with glutathione. Experientia, 41, 960-961
    • (1985) Experientia , vol.41 , pp. 960-961
    • Ito, S.1    Palumbo, A.2    Prota, G.3
  • 29
    • 33646472149 scopus 로고    scopus 로고
    • An MO study of regioselective amine addition to ortho -quinones relevant to melanogenesis
    • Land, E.J., Ramsden, C.A., and Riley, P.A. (2006) An MO study of regioselective amine addition to ortho-quinones relevant to melanogenesis. Tetrahedron, 62, 4884-4891
    • (2006) Tetrahedron , vol.62 , pp. 4884-4891
    • Land, E.J.1    Ramsden, C.A.2    Riley, P.A.3
  • 30
    • 0041695546 scopus 로고    scopus 로고
    • Mechanistic studies of catechol generation from secondary quinone amines relevant to indole formation and tyrosinase activation
    • Land, E.J., Ramsden, C.A., Riley, P.A., and Yoganathan, G. (2003) Mechanistic studies of catechol generation from secondary quinone amines relevant to indole formation and tyrosinase activation. Pigment Cell Res., 16, 397-406
    • (2003) Pigment Cell Res , vol.16 , pp. 397-406
    • Land, E.J.1    Ramsden, C.A.2    Riley, P.A.3    Yoganathan, G.4
  • 31
    • 33846318894 scopus 로고    scopus 로고
    • ortho-Quinone amines and derivatives: the infl uence of structure on the rates and modes of intramolecular reaction
    • 7 (x i)
    • Land, E.J., Ramsden, C.A., and Riley, P.A. (2007) ortho-Quinone amines and derivatives: the infl uence of structure on the rates and modes of intramolecular reaction. A rkivoc, 2007 (x i), 23-36
    • (2007) A rkivoc , vol.200 , pp. 23-36
    • Land, E.J.1    Ramsden, C.A.2    Riley, P.A.3
  • 32
    • 0025177271 scopus 로고
    • Oxygenation of fl uorinated tyrosines by mushroom tyrosinase releases fl uoride ion
    • Phillips, R.S., Fletcher, J.G., Von Tersch, R.L., and Kirk, K.L. (1990) Oxygenation of fl uorinated tyrosines by mushroom tyrosinase releases fl uoride ion. Arch. Biochem. Biophys., 276, 65-69
    • (1990) Arch. Biochem. Biophys. , vol.276 , pp. 65-69
    • Phillips, R.S.1    Fletcher, J.G.2    Von Tersch, R.L.3    Kirk, K.L.4
  • 33
    • 0000537283 scopus 로고
    • The aerobic oxidases
    • Raper, H.S. (1928) The aerobic oxidases. Physiol. Rev., 8, 245-282
    • (1928) Physiol. Rev. , vol.8 , pp. 245-282
    • Raper, H.S.1
  • 34
    • 0002518418 scopus 로고
    • The chemistry of melanin. Mechanism of the oxidation of dihydroxyphenylalanine by tyrosinase
    • Mason, H.S. (1948) The chemistry of melanin. Mechanism of the oxidation of dihydroxyphenylalanine by tyrosinase. J. Biol. Chem., 172, 83-92
    • (1948) J. Biol. Chem. , vol.172 , pp. 83-92
    • Mason, H.S.1
  • 36
    • 0001547199 scopus 로고
    • Pulse radiolysis apparatus
    • Keene, J.P. (1964) Pulse radiolysis apparatus. J. Sci. Instrum., 41, 493-496
    • (1964) J. Sci. Instrum. , vol.41 , pp. 493-496
    • Keene, J.P.1
  • 37
    • 0041835977 scopus 로고    scopus 로고
    • Rate constants for the fi rst two chemical steps of eumelanogenesis
    • Land, E.J., Ito, S., Wakamatsu, K., and Riley, P.A. (2003) Rate constants for the fi rst two chemical steps of eumelanogenesis. P igment Cell Res., 16, 487-493
    • (2003) P igment Cell Res , vol.16 , pp. 487-493
    • Land, E.J.1    Ito, S.2    Wakamatsu, K.3    Riley, P.A.4
  • 38
    • 0022406455 scopus 로고
    • A pulse radiolysis investigation of the oxidation of the melanin precursors 3,4-dihydroxyphenylalanine (dopa) and the cysteinyldopas
    • Thompson, A., Land, E.J., Chedekel, M.R., Subbarao, K.V., and Truscott, T.G. (1985) A pulse radiolysis investigation of the oxidation of the melanin precursors 3,4-dihydroxyphenylalanine (dopa) and the cysteinyldopas. Biochim. Biophys. Acta, 843, 49-57
    • (1985) Biochim. Biophys. Acta , vol.843 , pp. 49-57
    • Thompson, A.1    Land, E.J.2    Chedekel, M.R.3    Subbarao, K.V.4    Truscott, T.G.5
  • 39
    • 0033858051 scopus 로고    scopus 로고
    • Spontaneous redox reactions of dopaquinone and the balance between the eumelanic and phaeomelanic pathways
    • Land, E.J. and Riley, P.A. (2000) Spontaneous redox reactions of dopaquinone and the balance between the eumelanic and phaeomelanic pathways. P igment Cell Res., 13, 273-277
    • (2000) P igment Cell Res , vol.13 , pp. 273-277
    • Land, E.J.1    Riley, P.A.2
  • 40
    • 0032868621 scopus 로고    scopus 로고
    • Transient quinonimines and 1,4-benzothiazines of pheomelanogenesis: new pulse radiolytic and spectrophotometric evidence
    • Napolitano, A., Di Donato, P., Prota, G., and Land, E.J. (1999) Transient quinonimines and 1,4-benzothiazines of pheomelanogenesis: new pulse radiolytic and spectrophotometric evidence. Free Radic. Biol. Med., 27, 521-528
    • (1999) Free Radic. Biol. Med. , vol.27 , pp. 521-528
    • Napolitano, A.1    Di Donato, P.2    Prota, G.3    Land, E.J.4
  • 42
    • 84908857557 scopus 로고
    • Oxygen transfer and electron transport by the phenolase complex
    • Mason, H.S., Fowlks, W.L., and Peterson, E. (1955) Oxygen transfer and electron transport by the phenolase complex. J. Am. Chem. Soc., 77, 2914-2915
    • (1955) J. Am. Chem. Soc. , vol.77 , pp. 2914-2915
    • Mason, H.S.1    Fowlks, W.L.2    Peterson, E.3
  • 43
    • 0014010123 scopus 로고
    • The tyrosine hydroxylase activity of mammalian tyrosinase
    • Pomerantz, S.H. (1966) The tyrosine hydroxylase activity of mammalian tyrosinase. J. Biol. Chem., 241, 161-168
    • (1966) J. Biol. Chem. , vol.241 , pp. 161-168
    • Pomerantz, S.H.1
  • 44
    • 77049203277 scopus 로고
    • Comparative biochemistry of the phenolase complex, in
    • (ed. F.F. Nord), Interscience, New York
    • Mason, H.S. (1955) Comparative biochemistry of the phenolase complex, in Advances in Enzymology, vol. 16 (ed. F.F. Nord), Interscience, New York, pp. 105-184
    • (1955) Advances in Enzymology , vol.16 , pp. 105-184
    • Mason, H.S.1
  • 46
    • 0001064298 scopus 로고
    • Copper monooxygenases: tyrosinase and dopamine-beta -hydroxylase, in
    • (ed. H. Sigel), Decker, New York
    • Lerch, K. (1981) Copper monooxygenases: tyrosinase and dopamine-beta -hydroxylase, in Metal Ions in Biological Systems, vol. 13 (ed. H. Sigel), Decker, New York, pp. 143-186
    • (1981) Metal Ions in Biological Systems , vol.13 , pp. 143-186
    • Lerch, K.1
  • 47
    • 85050054836 scopus 로고
    • Tyrosinase, in
    • (eds F.F. Nord and C.H. Werkman), Interscience, New York
    • Nelson, J.M. and Dawson, C.R. (1944) Tyrosinase, in Advances in Enzymology, vol. 4 (eds F.F. Nord and C.H. Werkman), Interscience, New York, pp. 99-152
    • (1944) Advances in Enzymology , vol.4 , pp. 99-152
    • Nelson, J.M.1    Dawson, C.R.2
  • 48
    • 1842372406 scopus 로고
    • On the reaction inactivation of tyrosinase during aerobic oxidation of catechol
    • Asimov, I. and Dawson, C.R. (1950) On the reaction inactivation of tyrosinase during aerobic oxidation of catechol. J. Am. Chem. Soc., 72, 820-828
    • (1950) J. Am. Chem. Soc. , vol.72 , pp. 820-828
    • Asimov, I.1    Dawson, C.R.2
  • 49
    • 0000273832 scopus 로고
    • Enzymatic browning of fruits. III. Kinetics of the reaction inactivation of polyphenoloxidase
    • Ingraham, L.L., Corse, J., and Makower, B. (1952) Enzymatic browning of fruits. III. Kinetics of the reaction inactivation of polyphenoloxidase. J. Am. Chem. Soc., 74, 2623-2626
    • (1952) J. Am. Chem. Soc. , vol.74 , pp. 2623-2626
    • Ingraham, L.L.1    Corse, J.2    Makower, B.3
  • 50
    • 0018184565 scopus 로고
    • Nature of tyrosinase inactivation in melanosomes
    • Seiji, M., Sasaki, M., and Tomita, Y. (1978) Nature of tyrosinase inactivation in melanosomes. Tohoku J. Exp. Med., 125, 233-245
    • (1978) Tohoku J. Exp. Med. , vol.125 , pp. 233-245
    • Seiji, M.1    Sasaki, M.2    Tomita, Y.3
  • 54
    • 0001639883 scopus 로고    scopus 로고
    • Reaction inactivation of tyrosinase, in
    • (eds T.E. King, H.S. Mason, and M. Morrison), Pergamon, New York
    • Dietler. C,. Lerch K. Reaction inactivation of tyrosinase, in Oxidases and Related Redox Systems (eds T.E. King, H.S. Mason, and M. Morrison), Pergamon, New York 305- 317
    • Oxidases and Related Redox Systems , pp. 305-317
    • Dietler, C.1    Lerch, K.2
  • 55
    • 38449116139 scopus 로고    scopus 로고
    • The mechanism of suicide -inactivation of tyrosinase: a substrate structure investigation
    • Land, E.J., Ramsden, C.A., and Riley, P.A. (2007) The mechanism of suicide -inactivation of tyrosinase: a substrate structure investigation. Tohoku J. Exp. Med., 212, 341-348
    • (2007) Tohoku J. Exp. Med. , vol.212 , pp. 341-348
    • Land, E.J.1    Ramsden, C.A.2    Riley, P.A.3
  • 56
    • 59849124373 scopus 로고    scopus 로고
    • Evidence consistent with the requirement of cresolase activity for suicide inactivation of tyrosinase
    • Land, E.J., Ramsden, C.A., Riley, P.A., and Stratford, M.R.L. (2008) Evidence consistent with the requirement of cresolase activity for suicide inactivation of tyrosinase. Tohoku J. Exp. Med., 216, 231-238
    • (2008) Tohoku J. Exp. Med. , vol.216 , pp. 231-238
    • Land, E.J.1    Ramsden, C.A.2    Riley, P.A.3    Stratford, M.R.L.4
  • 57
    • 70349290601 scopus 로고    scopus 로고
    • The infl uence of catechol structure on the suicide inactivation of tyrosinase
    • Ramsden, C.A., Stratford, M.R.L., and Riley, P.A. (2009) The infl uence of catechol structure on the suicide inactivation of tyrosinase. Org. Biomol. Chem., 7, 3388-3390
    • (2009) Org. Biomol. Chem. , vol.7 , pp. 3388-3390
    • Ramsden, C.A.1    Stratford, M.R.L.2    Riley, P.A.3
  • 58
    • 0030749392 scopus 로고    scopus 로고
    • Mutational analysis of copper binding by human tyrosinase
    • Spritz, R.A., Ho, L., Furumara, M., and Hearing, V.J. (1997) Mutational analysis of copper binding by human tyrosinase. J. Invest. Dermatol., 109, 207-212
    • (1997) J. Invest. Dermatol. , vol.109 , pp. 207-212
    • Spritz, R.A.1    Ho, L.2    Furumara, M.3    Hearing, V.J.4
  • 60
    • 77958450802 scopus 로고    scopus 로고
    • Mechanistic studies of tyrosinase suicide inactivation
    • Ramsden, C.A. and Riley, P.A. (2010) Mechanistic studies of tyrosinase suicide inactivation. Arkivoc, 2010 (i), 260-274
    • (2010) Arkivoc , vol.2010 , Issue.1 , pp. 260-274
    • Ramsden, C.A.1    Riley, P.A.2
  • 61
    • 0032476050 scopus 로고    scopus 로고
    • Biochemical and spectroscopic characterization of catechol oxidase from sweet potatoes ( Ipomoea batatas ) containing a type-3 dicopper center
    • Eicken, C., Zippel, F., B ü ldt -Karentzopoulos, K., and Krebs, B. (1998) Biochemical and spectroscopic characterization of catechol oxidase from sweet potatoes (Ipomoea batatas) containing a type-3 dicopper center. FEBS Lett., 436, 293-299
    • (1998) FEBS Lett , vol.436 , pp. 293-299
    • Eicken, C.1    Zippel, F.2    Büldt -Karentzopoulos, K.3    Krebs, B.4
  • 62
    • 0036009142 scopus 로고    scopus 로고
    • The crystal structure of catechol oxidase: new insight into the function of type-3 copper proteins
    • Gerdemann, C., Eicken, C., and Krebs, B. (2002) The crystal structure of catechol oxidase: new insight into the function of type-3 copper proteins. Acc. Chem. Res., 35, 183-191
    • (2002) Acc. Chem. Res. , vol.35 , pp. 183-191
    • Gerdemann, C.1    Eicken, C.2    Krebs, B.3
  • 63
    • 0031760504 scopus 로고    scopus 로고
    • Crystal structure of a plant catechol oxidase containing a dicopper center
    • Klabunde, T., Eicken, C., Sacchettini, J.C., and Krebs, B. (1998) Crystal structure of a plant catechol oxidase containing a dicopper center. Nat. Struct. Biol., 5, 1084-1090
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 1084-1090
    • Klabunde, T.1    Eicken, C.2    Sacchettini, J.C.3    Krebs, B.4
  • 64
    • 33646827679 scopus 로고    scopus 로고
    • Crystallographic evidence that dinuclear copper center of tyrosinase is fl exible during catalysis
    • Matoba, Y., Kumagai, T., Yamamoto, A., Yoshitsu, H., and Sugiyama, M. (2006) Crystallographic evidence that dinuclear copper center of tyrosinase is fl exible during catalysis. J. Biol. Chem., 281, 8981-8990
    • (2006) J. Biol. Chem. , vol.281 , pp. 8981-8990
    • Matoba, Y.1    Kumagai, T.2    Yamamoto, A.3    Yoshitsu, H.4    Sugiyama, M.5
  • 65
    • 33746291588 scopus 로고    scopus 로고
    • The fi rst crystal structure of tyrosinase: all questions answered?
    • Decker, H., Schweikardt, T., and Tuczek, F. (2006) The fi rst crystal structure of tyrosinase: all questions answered? Angew. Chem. Int. Ed., 45, 4546-4550
    • (2006) Angew. Chem. Int. Ed. , vol.45 , pp. 4546-4550
    • Decker, H.1    Schweikardt, T.2    Tuczek, F.3
  • 67
    • 0037470072 scopus 로고    scopus 로고
    • Spectroscopic characterization of the electronic changes in the active site of Streptomyces antibioticus tyrosinase upon binding of transition state analogue inhibitors
    • Bubacco, L., van Gastel, M., Groenen, E.J.J., Vijgenboom, E., and Canters, G.W. (2003) Spectroscopic characterization of the electronic changes in the active site of Streptomyces antibioticus tyrosinase upon binding of transition state analogue inhibitors. J. Biol. Chem., 278, 7381-7389
    • (2003) J. Biol. Chem. , vol.278 , pp. 7381-7389
    • Bubacco, L.1    van Gastel, M.2    Groenen, E.J.J.3    Vijgenboom, E.4    Canters, G.W.5
  • 68
    • 77958507457 scopus 로고    scopus 로고
    • Studies of the competing rates of catechol oxidation and suicide inactivation of tyrosinase
    • Ramsden, C.A. and Riley, P.A. (2010) Studies of the competing rates of catechol oxidation and suicide inactivation of tyrosinase. Arkivoc, 2010 (x), 248-255
    • (2010) Arkivoc , vol.2010 , Issue.10 , pp. 248-255
    • Ramsden, C.A.1    Riley, P.A.2
  • 69
    • 0018862553 scopus 로고
    • 5-Hydroxydopa, a new compound in the Raper-Mason scheme of melanogenesis
    • Hansson, C., Rorsman, H., and Rosengren, E. (1980) 5-Hydroxydopa, a new compound in the Raper-Mason scheme of melanogenesis. Acta Derm. Venereol., 60, 281-186
    • (1980) Acta Derm. Venereol. , vol.60 , pp. 281-186
    • Hansson, C.1    Rorsman, H.2    Rosengren, E.3
  • 70
    • 0019973389 scopus 로고
    • 5-OH-dopa, product of and substrate for tyrosinase
    • Agrup, G., Rorsman, H., and Rosengren, E. (1982) 5-OH-dopa, product of and substrate for tyrosinase. Acta Derm. Venereol., 62, 371-376
    • (1982) Acta Derm. Venereol. , vol.62 , pp. 371-376
    • Agrup, G.1    Rorsman, H.2    Rosengren, E.3
  • 71
    • 0021276204 scopus 로고
    • Enzymatic 5-hydroxylation of l-dopa by a tyrosinase isolated from the sea anemone
    • Carlberg, M., Jergil, B., Lindbladh, C., and Rosengren, E. (1984) Enzymatic 5-hydroxylation of l-dopa by a tyrosinase isolated from the sea anemone Metrium senile. Gen. Pharmacol., 15, 301-307
    • (1984) Metrium senile Gen. Pharmacol. , vol.15 , pp. 301-307
    • Carlberg, M.1    Jergil, B.2    Lindbladh, C.3    Rosengren, E.4
  • 72
    • 0036629205 scopus 로고    scopus 로고
    • The other Topa: formation of 3,4,5-trihydroxyphenylalanine in peptides
    • Burzio, L.A. and Waite, J.H. (2002) The other Topa: formation of 3,4,5-trihydroxyphenylalanine in peptides. Anal. Biochem., 306, 108-114.
    • (2002) Anal. Biochem. , vol.306 , pp. 108-114
    • Burzio, L.A.1    Waite, J.H.2


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