References
27
30. G.H. Hogeboom, M.H. Adams, Mammalian tyrosinase and dopa oxidase. J. Biol. Chem. 145,
273–279 (1942)
31. A.B. Lerner, T.B. Fitzpatrick, E. Calkins, W.H. Summerson, Mammalian tyrosinase: preparation and properties. J. Biol. Chem. 178, 185–195 (1949)
32. H.S. Raper, XCV. The tyrosinase-tyrosine reaction V. J. Biol. Chem. 20, 735–742 (1926)
33. H.S. Raper, XIV. The tyrosinase-tyrosine reaction VI. J. Biol. Chem. 21, 89–96 (1927)
34. K. Wakamatsu, S. Ito, Preparation of eumelanin-related metabolites 5,6-dihydroxyindole 5,6dihydroxyindole-2-carboxylic acid and their O-methyl derivatives. Anal. Biochem. 170, 335–
340 (1988)
35. H.S. Mason, The chemistry of melanin. III. mechanism of the oxidation of dihydroxyphenylalanine by tyrosinase. J. Biol. Chem. 172, 83–99 (1948)
36. J.D. Bu’Lock, J. Harley-Mason, Melanin and its precursors. Part II. Model experiments on
the reactions between quinones and indoles and consideration of a possible structure for the
melanin polymer. J. Chem. Soc. 703–712 (1951)
37. R.J.S. Beer, T. Broadhurst, A. Robertson, The chemistry of the melanins. Part V. The
autoxidation of 5,6-dihydroxyindoles. J. Chem. Soc. 1947–1953 (1954)
38. T.B. Fitzpatrick, A.B. Lerner, Terminology of pigment cells. Science 117, 640–645 (1953)
39. A.M. Körner, J.M. Pawelek, Dopachrome conversion: a possible control point in melanin
biosynthesis. J. Invest. Dermatol. 75, 192–195 (1980)
40. A.M. Körner, P. Gettins, Synthesis in vitro of 5,6-dihydroxyindole-2-carboxylic acid by
dopachrome conversion factor from Cloudman S91 melanoma cells. J. Invest. Dermatol.
85, 229–231 (1985)
41. S. Ito, Reexamination of the structure of eumelanin. Biochim. Biophys. Acta 883, 155–161
(1986)
42. J.M. Pawelek, After dopachrome? Biochim. Biophys. Acta 883, 155–161 (1986)
43. M. Sugumaran, V. Semensi, Quinone methide as a new intermediate in eumelanin biosynthesis. J. Biol. Chem. 266, 6073–6078 (1991)
44. I.J. Jackson, D.M. Chambers, K. Tsukamoto, N.G. Copeland, D.J. Gilbert, N.A. Jenkins, V.
Hearing, A second tyrosinase-related protein TRP-2 maps to and is mutated at the mouse
slaty locus. EMBO J. 11, 527–535 (1992)
45. F. Solano, J.H. Martinez-Liarte, C. Jiménz-Cervantes, J.C. García-Borrón, J.A. Lozano,
Dopachrome tautomerase is a zinc-containing enzyme. Biochem. Biophys. Res. Commun.
204, 1243–1250 (1994)
46. F. Solano, C. Jiménez-Cervantes, J.H. Martínez-Liarte, J.C. García-Borrón, J.R. Jara, J.A.
Lozano, Molecular mechanism for catalysis by a new zinc-enzyme dopachrome tautomerase.
Biochem. J. 313, 447–453 (1996)
47. W.T. Ismaya, H.J. Rozeboom, A. Weijn, J.J. Mes, F. Fusetti, H.J. Wichers, B.W. Dijkstra,
Crystal structure of Agaricus bisporus mushroom tyrosinase: identity of the tetramer subunits
and interaction with tropolone. Biochemistry 50, 5477–5486 (2011)
48. C.A. Ramsden, P.A. Riley, Tyrosinase: the four oxidation states of the active site and their
relevance to enzymatic activation oxidation and inactivation. Bioorg. Med. Chem. 22, 2388–
2395 (2014)
49. S. Naish-Byfield, P.A. Riley, Oxidation of monohydric phenol substrates by tyrosinase. An
oximetric study. Biochem. J. 288, 63–67 (1992)
50. C.J. Cooksey, P.J. Garratt, E.J. Land, S. Pavel, C.A. Ramsden, P.A. Riley, N.P.M. Smit,
Evidence of the indirect formation of the catecholic intermediate substrate responsible for
the autoactivation kinetics of tyrosinase. J. Biol. Chem. 272, 26226–26235 (1997)
51. E. Pelizzetti, E. Mentasti, E. Pramauro, G. Giraudi, Kinetic determination of adrenaline, Ldopa and their mixtures with a stopped-flow spectrophotometric technique. Anal. Chim. Acta
85, 161–168 (1976)
52. D. Kertesz, M. Brunori, R. Zito, E. Antonini, Transient kinetic studies of dopa oxidation by
polyphenoloxidase. Biochim. Biophys. Acta 250, 306–310 (1971)
53. M.R. Chedekel, E.J. Land, A. Thompson, T.G. Truscott, Early steps in the free radical
polymerisation of 3,4-dihydroxyphenylalanine (dopa) into melanin. J. Chem. Soc. Chem.
Commun. 1170–1172 (1984)
27
30. G.H. Hogeboom, M.H. Adams, Mammalian tyrosinase and dopa oxidase. J. Biol. Chem. 145,
273–279 (1942)
31. A.B. Lerner, T.B. Fitzpatrick, E. Calkins, W.H. Summerson, Mammalian tyrosinase: preparation and properties. J. Biol. Chem. 178, 185–195 (1949)
32. H.S. Raper, XCV. The tyrosinase-tyrosine reaction V. J. Biol. Chem. 20, 735–742 (1926)
33. H.S. Raper, XIV. The tyrosinase-tyrosine reaction VI. J. Biol. Chem. 21, 89–96 (1927)
34. K. Wakamatsu, S. Ito, Preparation of eumelanin-related metabolites 5,6-dihydroxyindole 5,6dihydroxyindole-2-carboxylic acid and their O-methyl derivatives. Anal. Biochem. 170, 335–
340 (1988)
35. H.S. Mason, The chemistry of melanin. III. mechanism of the oxidation of dihydroxyphenylalanine by tyrosinase. J. Biol. Chem. 172, 83–99 (1948)
36. J.D. Bu’Lock, J. Harley-Mason, Melanin and its precursors. Part II. Model experiments on
the reactions between quinones and indoles and consideration of a possible structure for the
melanin polymer. J. Chem. Soc. 703–712 (1951)
37. R.J.S. Beer, T. Broadhurst, A. Robertson, The chemistry of the melanins. Part V. The
autoxidation of 5,6-dihydroxyindoles. J. Chem. Soc. 1947–1953 (1954)
38. T.B. Fitzpatrick, A.B. Lerner, Terminology of pigment cells. Science 117, 640–645 (1953)
39. A.M. Körner, J.M. Pawelek, Dopachrome conversion: a possible control point in melanin
biosynthesis. J. Invest. Dermatol. 75, 192–195 (1980)
40. A.M. Körner, P. Gettins, Synthesis in vitro of 5,6-dihydroxyindole-2-carboxylic acid by
dopachrome conversion factor from Cloudman S91 melanoma cells. J. Invest. Dermatol.
85, 229–231 (1985)
41. S. Ito, Reexamination of the structure of eumelanin. Biochim. Biophys. Acta 883, 155–161
(1986)
42. J.M. Pawelek, After dopachrome? Biochim. Biophys. Acta 883, 155–161 (1986)
43. M. Sugumaran, V. Semensi, Quinone methide as a new intermediate in eumelanin biosynthesis. J. Biol. Chem. 266, 6073–6078 (1991)
44. I.J. Jackson, D.M. Chambers, K. Tsukamoto, N.G. Copeland, D.J. Gilbert, N.A. Jenkins, V.
Hearing, A second tyrosinase-related protein TRP-2 maps to and is mutated at the mouse
slaty locus. EMBO J. 11, 527–535 (1992)
45. F. Solano, J.H. Martinez-Liarte, C. Jiménz-Cervantes, J.C. García-Borrón, J.A. Lozano,
Dopachrome tautomerase is a zinc-containing enzyme. Biochem. Biophys. Res. Commun.
204, 1243–1250 (1994)
46. F. Solano, C. Jiménez-Cervantes, J.H. Martínez-Liarte, J.C. García-Borrón, J.R. Jara, J.A.
Lozano, Molecular mechanism for catalysis by a new zinc-enzyme dopachrome tautomerase.
Biochem. J. 313, 447–453 (1996)
47. W.T. Ismaya, H.J. Rozeboom, A. Weijn, J.J. Mes, F. Fusetti, H.J. Wichers, B.W. Dijkstra,
Crystal structure of Agaricus bisporus mushroom tyrosinase: identity of the tetramer subunits
and interaction with tropolone. Biochemistry 50, 5477–5486 (2011)
48. C.A. Ramsden, P.A. Riley, Tyrosinase: the four oxidation states of the active site and their
relevance to enzymatic activation oxidation and inactivation. Bioorg. Med. Chem. 22, 2388–
2395 (2014)
49. S. Naish-Byfield, P.A. Riley, Oxidation of monohydric phenol substrates by tyrosinase. An
oximetric study. Biochem. J. 288, 63–67 (1992)
50. C.J. Cooksey, P.J. Garratt, E.J. Land, S. Pavel, C.A. Ramsden, P.A. Riley, N.P.M. Smit,
Evidence of the indirect formation of the catecholic intermediate substrate responsible for
the autoactivation kinetics of tyrosinase. J. Biol. Chem. 272, 26226–26235 (1997)
51. E. Pelizzetti, E. Mentasti, E. Pramauro, G. Giraudi, Kinetic determination of adrenaline, Ldopa and their mixtures with a stopped-flow spectrophotometric technique. Anal. Chim. Acta
85, 161–168 (1976)
52. D. Kertesz, M. Brunori, R. Zito, E. Antonini, Transient kinetic studies of dopa oxidation by
polyphenoloxidase. Biochim. Biophys. Acta 250, 306–310 (1971)
53. M.R. Chedekel, E.J. Land, A. Thompson, T.G. Truscott, Early steps in the free radical
polymerisation of 3,4-dihydroxyphenylalanine (dopa) into melanin. J. Chem. Soc. Chem.
Commun. 1170–1172 (1984)