Catechol melanin

It is interesting to underline that there is another (plant) enzyme which possesses a coordinatively similar dicopper environment catechol oxidase.11 As already mentioned in Chapter 6, Section 3, such an ubiquitous enzyme catalyses the two-electron oxidation by molecular dioxygen of catechols to the corresponding quinones (the so-generated quinones in turn polymerize to form brown polyphenolic catechol melanins, which protect damaged plants from pathogens or insects). 

Catechol melanin, a black pigment of plants, is a polymeric product formed by the oxidative polymerization of catechol. The formation route of catechol melanin (Eq. 5) is described as follows [33-37] At first, 3-(3, 4 -dihydroxyphe-nyl)-L-alanine (DOPA) is derived from tyrosine. It is oxidized to dopaquinone and forms dopachrome. 5,6-Dihydroxyindole is formed, accompanied by the elimination of C02. The oxidative coupling polymerization produces a melanin polymer whose primary structure contains 4,7-conjugated indole units, which exist as a three-dimensional irregular polymer similar to lignin. Multistep oxidation reactions and coupling reactions in the formation of catechol melanin are catalyzed by a copper enzyme such as tyrosinase. Tyrosinase is an oxidase con-... 

Natural melanins are generally differentiated by their origin, e.g., bovine eye, melanoma, sepia melanin. They usually occur in the form of granular particles, the melanosomes, and are secretory products of pigment-producing cells, the melanocytes. Synthetic melanins are named after the compound from which they were prepared via chemical or enzymatic oxidation (e.g., (/./-dopa, 5,6-dihydroxyindole, catechol melanin). 

Hydrogen peroxide, which oxidatively degrades eumelanins, undergoes disproportionation with catechol melanin to produce oxygen and water 205). 

Catechin, 2314, 2335, 2342, 2452, 2568 (+)-Catechiii, 1605 Catechinpyiylium, 1784 Catechins, 1178, 2285, 2334 Catechol, 1548 Catecholamines, 598, 967 Catechol melanins, 1564 Catechol-O-methyl transferase, 2475 P-Catenin, 2194 Catha edulis, 1221... 

Allomelanins — These are structurally different compounds containing little or no nitrogen. They are considered polymers of phenolic compounds like catechol. Fnngi prodnce melanin pigments, predominantly dihydroxyphenylalanine (DOPA)-melanin and dihydroxynaphthalene (DHN)-melanin. ... 

With tyrosinase, on the contrary, a two-electron oxidation occurs, as no EPR signal was detected in the catechol oxidation at pH 5.3 Melanins are polymerization products of tyrosine, whereby tyrosinase catalyses the first steps the formation of dopa (3,4-dihydroxyphenylalanine) and of dopaquinone, leading to an indolequi-none polymer The peroxidase mechanism for the conversion of tyrosine into dopa in melanogenesis was not substantiated In natural and synthetic melanins free radicals of a semiquinone type were detected by EPR 4-10 x 10 spins g of a hydrated suspension (the material was modified on drying and the number of free spins increased). The fairly symmetrical EPR signal had a g-value of 2.004 and a line-width of 4-10 G The melanins seem to be natural radical scavengers. 

In his classical studies on melanin formation from DOPA (3), Raper proposed the following scheme for the formation of the red pigment now known to be the aminochrome dopachrome (4). The first stage involved the oxidation of the catechol nucleus of-3 to give the quinone dopa-quinone (16). The second stage was the non-oxidative intramolecular cyclization of 16 to leuco-dopachrome (17), which was in turn oxidized to dopachrome (4).72,73 Since... 

The presence of catechols and more complex, oxidizable polyphenols in nature is widespread, and their functions are not limited to chemical defense. However, biological control of their oxidation is usually a feature of their function, as it is (1) in melanin synthesis,3 (2) in immunologically mediated delayed-type hypersensitivity responses,4 (3) in the hardening or curing of arthropod secretions (for example, as in the surface attachment adhesives of the barnacle and in tanning of the cuticle in insects),5 as well as (4) in defensive mechanisms in higher plants, particularly in the unleashing of immediate necrotrophic responses.6... 

A combination of decarboxylation and hydroxyla-tion of the ring of tyrosine produces derivatives of o-dihydroxybenzene (catechol), which play important roles as neurotransmitters and are also precursors to melanin, the black pigment of skin and hair. Catecholamines may be formed by decarboxylation of tyrosine into tyramine (step e, Fig. 25-5) and subsequent oxidation. However, the quantitatively more important route is hydroxylation by the reduced pterin-dependent tyrosine hydroxylase (Chapter 18) to 3,4-dihydroxyphenylalanine, better known as dopa. The latter is decarboxylated to dopamine.1313 Hydroxylation of dopamine by an ascorbic acid and... 

The simplest, but least accurate, method of assaying DPO activity is to record the final color yield when the enzyme is incubated with a suitable chromogenic substrate such as catechol, DOPA, or 4-methylcatechol. DOPA is the most frequently used substrate in colorimetric assays because it yields a dark brown/black end-product. In this reaction, catecholase catalyzes the conversion of DOPA to dopaquinone and then to the red dopachrome, which subsequently polymerizes to yield dark brown melanin-type pigments. Unfortunately, this simple procedure has serious limitations, as it measures the end-product of a sequence of reactions rather than the true initial reaction rate. Furthermore, because different substrates yield different final colors, valid kinetic comparisons between substrates are not possible. Nevertheless, this simple assay technique has proved adequate for useful comparative studies of the levels of enzymic browning in different fruit varieties and similar problems (Vamos-Vigyazo, 1981 Machiex et al., 1990). 

Figure 2.21. Mechanisms of the oxidative polymerization of catechol to melanins (humic polymers) in the presence of tyrosinase or birnessite. Reprinted with permission from Naidja, A., Huang, P. M., Dec, J., and Bollag, J.-M. (1999). Kinetics of catechol oxidation catalyzed by tyrosinase or 8-Mn02. In Effect of Mineral-Organic-Microorganism Interactions on Soil and Freshwater Environments, Berthelin, J., Huang, P. M., Bollag, J.-M., and Andreux, F., eds., Kluwer Academic/Plenum Publishers, New York, 181-188.

With branched catechols carrying nucleophilic groups in the side chains, the ring closure reaction occurs. Typical examples are the peroxidase oxidation of dopa and dopamine, which produce a series of compounds such as dopachrome and dopami-nechrome, respectively, which further evolve to compounds related to melanin pigments [46] (Fig. 6.3c). 

The distinguishing feature of tyrosinase is that it catalyzes the oxidation of monohydric phenols, like tyrosine, to the dihydric form and dihydric phenols, like DOPA and catechol, to the corresponding quinones. The striking biological effects of this enzyme arise from quinones which polymerize to produce the darkening of various plants on injury and melanin in mammals. The relative oxidation rates of several dihydric phenols by tyrosinase are given in Table III. 

Melanins have been prepared by air oxidation of dopa and other substrates (including catechol) (2//) in alkaline medium (pH > 8). These melanins are described by the base used in the synthetic procedure, such as NaOH-melanin, ammonia-melanin, diethylamine-melanin (2/2), to characterize eventual structural differences. In a typical experiment (253) air was bubbled for 3 days through a solution of t/,/-dopa (10 g) in deionized water (2 liters) adjusted with concentrated ammonia to pH 8 ... 

Natural black (human hair, bovine eyes) and synthetic (tyrosine, dopa, and dopamine) melanins were investigated by Curie point pyrolysis-gas chromatography-mass spectrometry (86,96). The pigments were characterized by different ratios of degradation products identified as aromatic hydrocarbons, phenols, catechols, pyrroles, and indoles. The amount of ash in karakul lamb wool was correlated to its color, with black producing the most (3.9%) and white the least (1.2%). Similar studies showed a correlation with the calcium content (317,318). 

Similar redox equilibria are felt [68] to be present in melanins, the final polymeric products of tyrosinase oxidation of catechols and catecholamines. Whereas natural... 

Tyrosine also has an important role in the central nervous system and melanocyte and is the precursor of both melanins and catecholamines (epinephrine and norepinephrine). The conversion to these products takes place in the appropriate tissues, usually melanocyte, the central nervous system, or the adrenal gland. In each of these tissues, the enzyme tyrosinase catalyzes the conversion of tyrosine to dihydroxyphenylalanine (DOPA) by hydroxylating the ring adjacent to the parahydroxy group. This is a catechol ring. If this were an amine instead of an amino acid, it would be a catecholamine. The DOPA is a precursor of catecholamines in the adrenal gland and central nervous system. In melanocyte, the DOPA is converted to melanine. In the disease albinism, the tyrosinase in the... 

These two processes are also referred as cresolase activity or monophenolase activity and diphenolase activity, respectively. Such reactions represent the initial steps of vertebrate pigmentation (melanin biosynthesis) and the browning of fruits and vegetables.Catechol oxidases (EC 1.10.3.1) are ubiquitous plant enzymes, which also catalyze the oxidation of a broad... 

Hydroquinone and its derivatives p-hydroxypropiophenone, pyridine derivatives, catechol, mercaptamine derivatives, etc., inhibit melanin formation by blocking tyrosinase activity (56, 67). 

Classical tyrosinase (catechol oxygenase, EC 1.10.3.1) catalyses the first step in the synthesis of Melanin (see) from tyrosine. 

Tyrosinase. Tyrosinase is a very well-studied multicopper oxygenase, which contains a magnetically coupled dinuclear copper center. This enzyme catalyzes the ortho-hydroxylation of phenols to catechols (phenolase activity, also called cresolase activity), as well as the 2-electron oxidation of catechols to 0-quinones (catecholase activity), which is the initial step for the biosynthesis of melanin (Scheme 1) (7,13). 

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