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Catechol, tyrosinase-catalyzed

These copper ion-dependent enzymes [EC 1.10.3.1] (also referred to as diphenol oxidases, O-diphenolase, phe-nolases, polyphenol oxidases, or tyrosinases) catalyze the reaction of two catechol molecules with dioxygen to produce two 1,2-benzoquinone and two water. A variety of substituted catechols can act as substrates. Many of the enzymes listed under this classification also catalyze a monophenol monooxygenase activity [/.c., EC 1.14.18.1]. See also Monophenol Monooxygenase Tyrosine Monooxygenase... [Pg.121]

While only tyrosinase catalyzes the ortho-hydroxylation of phenol moieties, both tyrosinase and catechol oxidase mediate the subsequent oxidation of the resulting catechols to the corresponding quinones. Various mono- and dinu-clear copper coordination compounds have been investigated as biomimetic catalysts for catechol oxidation [21,194], in most cases using 3,5-di-tert-butylcatechol (DTBC) as the substrate (Eq. 16). The low redox potential of DTBC makes it easy to oxidize, and its bulky tert-butyl groups prevent un-... [Pg.54]

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. 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.
Activation mechanism for tyrosinase-catalyzed oxidation of catechol with 02... [Pg.292]

Generally, the regioselective formation of o-quinones has been known to be accomplished by using polyphenol oxidase in chloroform and not in water, because of rapid inactivation of the enzyme in water. However, catechol underwent mushroom tyrosinase-catalyzed oxidation in phosphate buffer (pH 6.8) containing 4-hydroxycoumarin (322) to afford 321 in 96% yield, as shown in Scheme 69. [Pg.1219]

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... [Pg.523]

A apart. Dioxygen binding results in the two-electron reduced peroxide in a side-on bound dicopper(II) structure (Fig. 1). Crystallographic information is (also) established for the reduced, as well as the oxidized met forms (3-5). Based on their spectroscopic similarities, a similar active-site structure is proposed for the monooxygenase tyrosinase (Tyr) X-ray structures are available for catechol oxidase (CO) depicting a similar active-site structure to He and Tyr (6). However, unlike the reversible binding reactivity of hemocyanin, tyrosinase catalyzes the aromatic hydroxylation of tyrosine to 3,4-dihydroxyphenylalanine (l-DOPA), and can further perform catechol oxidase activity which oxidizes the catechol to the quinone (Fig. 2) (7). [Pg.132]

The enzyme tyrosinase catalyzes the oxidation of catechols to o-quinones (catecholase activity) and also the hydroxylation of phenols to o-diphenols (cresolase activity). This multisubunit enzyme contains several copper(I) sites in the active form. [Pg.253]

Tyrosinase-catalyzed transformations of catechols and o-benzoquinones were modeled by copper complexes which mimic both the spectroscopic characteristics [44-48] and the chemical behavior [49,50] of the biological systems. Tyrosinases have so-called copper type 3 centers, which are strongly antiferromagnetically coupled. The multicopper concept has emerged as an important feature in the modeling approach. [Pg.265]

Cosnier and Innocent [135] recognized tliat one of the problems with incorporation of enzymes from solutions into CP films during electropolymerization was that the concentration of the enzyme in the CP film could only be approximately controlled. They took a derivatized pyrrole monomer containing a surfactant group (Eq. (17.211 which has a strong affinity for the enzyme tyrosinase within specific pH ranges. A film of the monomer-tyrosinase complex, with predetermined monomer-tyrosinase concentrations, was cast from solution onto a Pt electrode. The electrode was then removed from this solution and immersed in a second electrolyte for polymerization of the adsorbed monomer-tyrosinase complex, yielding a P(Py)-derivative/tyrosinase film. Tyrosinase catalyzes the oxidation of monophenols and o-diphenols to o-quinones in the presence of O2. The sensor could thus be used for detection of such analytes as catechol, as shown in Fig. 17-12. Response times were of the order of seconds. [Pg.496]

The results of the experiments just described provide strong, although indirect, evidence for quinone formation during the conversion of dopamine to norepinephrine and during the conversion of phenylethylamine to phenylethanolamine (in the presence of catechol). The spectral changes which occur during the latter reaction were found (Levin and Kaufman, 1961) to be virtually identical with those reported for the tyrosinase-catalyzed oxidation of pyrocatechol to o-benzoquinone (Mason, 1949) and this result provides direct evidence in favor of the view that Eq. (19) correctly describes the hydroxylation of phenylethylamine in the absence of ascorbate. [Pg.168]

Increased selectivity and prevention of passivation of the BDD surface may be also achieved by its modification. An enzyme-based amperometric sensor was proposed for detection of phenolic compounds by Notsu et al. BDD was anod-ically polarized for the introduction of hydroxyl groups onto its surface, then treated with (3-aminopropyl)triethoxysilane (APTES), and finally coated with a tyrosinase film cross-linked with glutaraldehyde. Tyrosinase catalyzes oxidadmi of phenol and various phenol derivatives to o-benzoquinone derivatives via catechol derivatives and thus the quinones generated are ready to be reduced electrochemically at an appropriate potential and obtained reduction currents serve as good analytical signals for the determination of the phenol derivatives. Bisphenol A and 17-/ -estradiol were detected at —0.3 V vs. Ag/AgCl with the detection limit of 1 pmol in FIA. However, the biosensor retained its activity only for a few days due to weak bonding of APTES to BDD surface. [Pg.233]

In 1996, the first successful combination of an enzymatic with a nonenzymatic transformation within a domino process was reported by Waldmann and coworkers [6]. These authors described a reaction in which functionalized bicy-clo[2.2.2]octenediones were produced by a tyrosinase (from Agaricus bisporus) -catalyzed oxidation of para-substituted phenols, followed by a Diels-Alder reaction with an alkene or enol ether as dienophile. Hence, treatment of phenols such as 8-1 and an electron-rich alkene 8-4 in chloroform with tyrosinase in the presence of oxygen led to the bicyclic cycloadducts 8-5 and 8-6 in moderate to good yield (Scheme 8.1). It can be assumed that, in the first step, the phenol 8-1 is hydroxylated by tyrosinase, generating the catechol intermediate 8-2, which is then again oxidized enzy-... [Pg.530]

Tyrosinase is a monooxygenase which catalyzes the incorporation of one oxygen atom from dioxygen into phenols and further oxidizes the catechols formed to o-quinones (oxidase action). A comparison of spectral (EPR, electronic absorption, CD, and resonance Raman) properties of oxy-tyrosinase and its derivatives with those of oxy-Hc establishes a close similarity of the active site structures in these proteins (26-29). Thus, it seems likely that there is a close relationship between the binding of dioxygen and the ability to "activate" it for reaction and incoiporation into organic substrates. Other important copper monooxygenases which are however of lesser relevance to the model studies discussed below include dopamine p-hydroxylase (16,30) and a recently described copper-dependent phenylalanine hydroxylase (31). [Pg.86]

Tyrosinase. This enzyme is found in numerous organisms ranging tom bacteria and fungi to plants and animals. The best characterized tyrosinases are those tom mushrooms and tom N. crassa (11-14). The reactions catalyzed by tyrosinase are the hydroxylation of phenols to give catechols and the subsequent oxi tion of catechols to give o-quinones. [Pg.106]

This copper-dependent enzyme [EC 1.14.18.1] (also known as tyrosinase, phenolase, monophenol oxidase, and cresolase) catalyzes the reaction of L-tyrosine with L-dopa and dioxygen to produce L-dopa, dopaquinone, and water. This classification actually represents a set of copper proteins that also catalyze the reaction of catechol oxidase [EC 1.10.3.1] if only 1,2-benzenediols are available as substrates. [Pg.489]

The first of two conversions catalyzed by the metalloenzyme tyrosinase is the selective ortho-hydroxylation of a phenol moiety, yielding catechol. Few synthetic systems exist that are capable of selectively performing the same monooxygenase reaction [172-178]. The group of Casella has studied a series of dicopper complexes based on 2,6-disubstituted benzene hgands providing two N3 compartments [179-181] (26a,b) as well as the asymmetrically substituted tripodal amine-based ligand (27) [182]. [Pg.51]

Tyrosinase, a copper-containing oxidoreductase, catalyzes the orthohydroxy-lation of monophenols and the aerobic oxidation of catechols. The enzyme activity will be assayed by monitoring the oxidation of 3,4-dihydroxyphenyl-alanine (dopa) to the red-colored dopachrome. The kinetic parameters Ku and Vmax will be evaluated using Lineweaver-Burk or direct linear plots. Inhibition of tyrosinase by thiourea and cinnamate will also be studied. Two stereoisomers, L-dopa and D-dopa, will be tested and compared as substrates. [Pg.279]

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-... [Pg.538]

There is evidence that quinone methides form as intermediates in the metabolic oxidation of catechol derivatives, a key step in a variety of biosynthetic processes such as melanization and sclerotization of animal cells. Tyrosinase from mushrooms catalyzes the oxidation of a-methyldopa methyl ester 54a. It has been proposed that this reaction observed in vitro is part of a metabolic pathway for the metabolism of 54a. This reaction proceeds by oxidation of ct-methyl dopa methyl ester 54a to give 54b, which cyclizes and is further oxidized to quinone methide 54c (Scheme 26).101 This quinone methide was identified by comparison to authentic 54c, which was prepared by chemical oxidation of 54a to 54c.102... [Pg.61]

Naidja A, Huang PM, Bollag J-M. Comparison of reaction products from the transformation of catechol catalyzed by bimessite or tyrosinase. Soil Sci Am J... [Pg.474]

Tyrosinase. The oxidation of catechol with 02, catalyzed by tyrosinase, was concluded by Mason (I) in 1961 not to involve any radical species therefore, an ionic mechanism was proposed by Hamilton (2). A possible activation mechanism seems to involve the interaction between Cu(I)-protein and 02 to give an active Cu(II)—O—OH species in which Cu(II) and OH act as electron-deficient centers, withdrawing electrons from the substrate (Figure 1). [Pg.291]

A conducting, polymeric film of poly(indole-5-carboxylic acid) has been employed for covalent immobilization of tyrosinase, which retains catalytic activity and catalyzes oxidation of catechol to the quinone <2006MI41>. Poly(l-vinylpyrrole), polyfl-vinylindole), and some methyl-substituted compounds of poly(l-vinylindole) are of potential interest as photorefractive materials with a relatively low glass-transition temperature and requiring a lower quantity of plasticizer in the final photorefractive blend <2001MI253>. Polymers of 5,6-dihydroxyindoles fall within the peculiar class of pigments known as eumelanins and their chemistry has been reviewed <2005AHC(89)1>. [Pg.356]

FIGURE 57.12. Reactions catalyzed by the two activities of tyrosinase. Phenol is first oxidized to catechol and then to o-quinone. Reproduced with permission from Kohli et al. (2007a). [Pg.870]

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. [Pg.289]

Laccase shares with tyrosinase the ability to oxidize dihydric phenols, like catechol, to the corresponding quinones. Whether the enzyme is active in the oxidation of monohydric phenols like cresol is a matter of controversy since the purity of preparations said to catalyze such oxidations has been questioned 107), Much more important is the ability of laccase to oxidize various aminophenols, like p-phenylenediamine, which is in fact the best substrate for the enzyme (Table III). The enzyme is important commercially because it oxidizes some complex... [Pg.289]


See other pages where Catechol, tyrosinase-catalyzed is mentioned: [Pg.761]    [Pg.296]    [Pg.1398]    [Pg.45]    [Pg.32]    [Pg.508]    [Pg.928]    [Pg.328]    [Pg.502]    [Pg.43]    [Pg.302]    [Pg.492]    [Pg.1065]    [Pg.53]    [Pg.371]    [Pg.68]    [Pg.88]    [Pg.90]    [Pg.103]    [Pg.241]   


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Catechol

Catechol, tyrosinase-catalyzed oxidation

Catecholate

Tyrosinases

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