Mechanistic studies of catechol generation from secondary quinone amines relevant to indole formation and tyrosinase activation

Pigment Cell Research

Volumn 16, Issue 4, 2003, Pages 397-406

  Land, Edward J ^a   Ramsden, Christopher A ^a   Riley, Patrick A ^b   Yoganathan, Gnanamoly ^a  

^a KEELE UNIVERSITY   (United Kingdom)

^b MOUNT VERNON HOSPITAL   (United Kingdom)

Author keywords

Catecholamines; Enzyme activation; ortho Quinone amines; Pulse radiolysis; Tyrosinase

Indexed keywords

CATECHOL; HETEROCYCLIC COMPOUND; INDOLE DERIVATIVE; MELANIN; MONOPHENOL MONOOXYGENASE; QUINONE DERIVATIVE;

ARTICLE; CATALYSIS; CHEMICAL MODIFICATION; COMPUTER MODEL; CYCLIZATION; ENZYME ACTIVATION; ISOMERISM; OXIDATION REDUCTION REACTION; PROTON TRANSPORT; RADIOLYSIS; REACTION ANALYSIS; STOICHIOMETRY;

AMINES; CATECHOLS; CYCLIZATION; DOPAMINE; ENZYME ACTIVATION; INDOLES; MONOPHENOL MONOOXYGENASE; OXIDATION-REDUCTION; PROTONS; PULSE RADIOLYSIS; QUINONES;

EID: 0041695546     PISSN: 08935785     EISSN: None     Source Type: Journal    
DOI: 10.1034/j.1600-0749.2003.00063.x     Document Type: Article

References (32)

1. Mason HS. Structure and functions of the phenolase complex. Nature 1965;34:595-856
2. Solomon EI, Tuczek F, Root DE, Brown CA. Spectroscopy of binuclear dioxygen complexes. Chem Rev 1994;94:827-856
3. Solomon EI, Sundaram UM, Machonkin TE. Multicopper oxygenases and oxygenases. Chem Rev 1996;96:2563-2605
4. Decker H, Rimke T. Tarantula haemocyanin shows phenoloxidase activity. J Biol Chem 1998;273:25 889-25 892
5. Decker H, Tuczek F. Tyrosinase/catecholoxidase activity of haemocyanins: structural basis and molecular mechanism. TIBS 2000;25:392-397
6. Oetting W. The tyrosinase gene and oculocutaneous albinism type 1 (OCA): a model for understanding the molecular biology of melanin formation. Pigment Cell Res 2000;13:320-325
7. Lerner AB, Fitzpatrick TB, Calkins E, Summerson WH. Mammalian tyrosinase: preparation and properties. J Biol Chem 1949;178: 185-195
8. Lerch K. Copper monooxygenases: tyrosinase and dopa β-hydroxylase. In: Sigel H. Metal Ions in Biological Systems, Vol. 13. New York: Marcel Dekker; 1981. pp. 143-186.
9. Pomerantz SM, Warner MC. 3,4-Dihydroxy-L-phenylalanine as the tyrosinase cofactor. J Biol Chem 1967;242:5308-5314
10. Evans WC, Raper HS. The accumulation of 3,4-dihydroxyphenylalanine in the tyrosine-tyrosinase reaction. Biochem J 1937;31:2162-2170
11. Pomerantz SM. The tyrosinase hydroxylase activity of mammalian tyrosinase. J Biol Chem 1966;241:161-168
12. Wyler H, Chiovini J. Die synthese von cyclodopa (leukodopachrom). Helv Chim Acta 1968;51:1476-1494
13. Chedekel MR, Land EJ, Thompson A, Truscott TG. Early steps in the free radical polymerisation of 3,4-dihydroxyphenylalanine (Dopa) to melanin. J Chem Soc Chem Commun 1984;1170-1172
14. Land EJ, Riley PA. Spontaneous redox reactions of dopaquinone and the balance between the eumelanic and pheomelanic pathways. Pigment Cell Res 2000;13:273-277
15. Cooksey CJ, Garratt PJ, Land EJ, Pavel S, Ramsden CA, Riley PA, Smit NPM. Evidence of the indirect formation of the catecholic intermediate substrate responsible for the autoactivation kinetics of tyrosinase. J Biol Chem 1997;272:26 226-26 235
16. Fenoll LG, Rodrigues-López JN, Garcia-Sevilla F, Garcia-Ruiz PA, Varón R, García-Cánovas F, Tudela J. Analysis and interpretation of the action mechanism of mushroom tyrosinase on monophenols and diphenols generating highly unstable o-quinones. Biochim Biophys Acta 2001;1548:1-22
17. Rodrigues-López JN, Fenoll LG, Peñalver MJ, García-Ruiz PA, Varón R, Martínez-Ortíz F, García-Cánovas F, Tudela J. Tyrosinase action on monophenols: evidence for direct enzymatic release of o-diphenol. Biochim Biophys Acta 2001;1548:238-256
18. Pefialver MJ, Hiner ANP, Rodrigues-López JN, Garcia-Cánovas F, Tudela J. Mechanistic implications of variable stoichiometries of oxygen consumption during tyrosinase catalysed oxidation of monophenols and ortho-diphenols. Biochim Biophys Acta 2002;1597:140-148
19. Sugumaran M, Semensi V, Kalyanaraman B, Bruce JM, Land EJ. Evidence for the formation of a quinone methide during the oxidation of the insect cuticular sclerotizing precursor 1,2-dehydro-N-acetyldopamine. J Biol Chem 1992;267:10 355-10 361
20. Land EJ. Preparation of unstable quinones in aqueous solution via pulse radiolytic one-electron oxidation of dihydroxybenzenes. J Chem Soc Faraday Trans 1993;89:803-810
21. Keene JP. Pulse radiolysis apparatus. J Sci Instrum 1964;41:493-496
22. Butler J, Hodgson BW, Hoey BM, Land EJ, Lea JS, Lindley EJ, Rushton FAP, Swallow AJ. Experimental studies of some moderately fast processes initiated by radiation. Radiat Phys Chem 1989;34:633-641
23. Adams GE, Boag JW, Currant J, Michael BD. The pulse radiolysis of aqueous solutions of thiocyanate ion. In: Ebert M, Keene JP, Swallow AJ, Baxendale JH. Pulse Radiolysis. London: Academic Press; 1965. pp. 117-129.
24. Buxton GV, Stuart CR. Re-evaluation of thiocyanate dosimeter for pulse radiolysis. J Chem Soc Faraday Trans 1995;91:279-281
25. Naish-Byfield S, Riley PA. Oxidation of monohydric phenol substrates by tyrosinase. Biochem J 1992;288:63-67
26. Lambert C, Truscott TG, Land EJ, Riley PA. Role of azide concentration in pulse radiolysis studies of oxidation: 3,4-dihydroxyphenylalanine. J Chem Soc Faraday Trans 1991;87:2939-2942
27. Clews J, Cooksey CJ, Garratt PJ, Land EJ, Ramsden CA, Riley PA. Oxidative cyclisation of N,N-dialkylcatechol amines to heterocyclic betaines via o-quinones: synthetic, pulse radiolytic and enzyme studies. J Chem Soc Perkin Trans 2000;1:4306-4315
28. Cooksey CJ, Land EJ, Rushton FAP, Ramsden CA, Riley PA. Tyrosinase-mediated cytotoxicity of 4-substituted phenols: use of QSAR to forecast reactivities of thiols towards the derived orthoquinones. Quant Struct-Act Relat 1996;15:498-503
29. Heacock RA. The chemistry of adrenochrome and related compounds. Chem Rev 1959;59:181-237
30. Cooksey CJ, Garratt PJ, Land EJ, Ramsden CA, Riley PA. Tyrosinase kinetics: failure of the autoactivation mechanism of monohydric phenol oxidation by rapid formation of a quinomethane intermediate. Biochem J 1998;333:685-691
31. Baldwin JE. Rules for ring closure. J Chem Soc Chem Commun 1976;734-736
32. Jordan AM, Khan TH, Malkin H, Osborn HMI, Photiou A, Riley PA. Melanocyte-directed enzyme prodrug therapy (MDEPT): development of second-generation prodrugs for targeted treatment of malignant melanoma. Bioorg Med Chem 2001;9:1549-1558