Melanin complexes

Iron-melanin complex in substantia nigra of parkinsonian brains an X-ray microanalysis. J. Neurochem. 59 1168-1171. 

Chitin-protein fibers or chitin-melanin complex... 

Guyon A, Banisadr G, Rovere C, Cervantes A, Kitabgi P, MeUk-Parsadaniantz S, Nahon JL (2005b) Complex effects of stromal cell-derived factor-1 alpha on melanin-concentrating hormone neuron excitabUity. Eur J Neurosci 21 701-710... 

Melanins are complex polymeric structures, which are usually mixtures of macromolecules. Melanins are classified as eumelanins, phaeomelanins and allomelanins. ... 

Melanin biosynthesis in animals is a complex process starting with the L-tyrosine amino acid. In the first step, L-tyrosine is converted first into DOPA and then into dopaquinone, a process catalyzed by tyrosinase. In the biosynthesis of eumelanins, dopaquinone undergoes a cyclization to form dopachrome and subsequently a tau-tomerization into 5,6-dihydroxyindole-2-carboxylic acid (DHICA). DHICA is further oxidized to indole-5,6-quinone2-carboxylic acid, the precnrsor of DHICA eumelanins. Tyrosinase-related proteins TRP-2 and TRP-1, respectively, are responsible for the last two steps, and they are under the control of the tyrosinase promoter. 

Because of their very complex chemical structures and heterogeneity, melanins are difficult to extract, separate, and characterize from tissues. Eumelanins are insoluble in water and organic solvents. They can be extracted from tissues with strong chemicals that are capable of removing lipids, proteins, and other tissue components but also lead to the formation of degradation products. Enzymatic procedures were developed for the isolation of eumelanins from mammalian hair and irises. The first step is sequential digestion with protease, proteinase K, and papaine in the presence... 

Polyphenoloxidase (PPO, EC 1.14.18.1) is one of the most studied oxidative enzymes because it is involved in the biosynthesis of melanins in animals and in the browning of plants. The enzyme seems to be almost universally distributed in animals, plants, fungi, and bacteria (Sanchez-Ferrer and others 1995) and catalyzes two different reactions in which molecular oxygen is involved the o-hydroxylation of monophenols to o-diphenols (monophenolase activity) and the subsequent oxidation of 0-diphenols to o-quinones (diphenolase activity). Several studies have reported that this enzyme is involved in the degradation of natural phenols with complex structures, such as anthocyanins in strawberries and flavanols present in tea leaves. Several polyphenols... 

Materials such as humates, fulvates, and melanins are related to, or contain, peptide or protein molecules or moieties. Kinetic patterns for their interactions with metal ions may be complicated by the probability that more than one complex species will be involved. Thus it has been demonstrated that Ni2+-fulvate solutions contain at least four kinetically distinct species, i.e. Ni2+aq and three complexes, as indicated in reactions of such solutions with for example par (514). Moreover in a metal-exchange reaction the metal ions M and M may complex at some... 

Copper is part of several essential enzymes including tyrosinase (melanin production), dopamine beta-hydroxylase (catecholamine production), copper-zinc superoxide dismutase (free radical detoxification), and cytochrome oxidase and ceruloplasmin (iron conversion) (Aaseth and Norseth 1986). All terrestrial animals contain copper as a constituent of cytochrome c oxidase, monophenol oxidase, plasma monoamine oxidase, and copper protein complexes (Schroeder et al. 1966). Excess copper causes a variety of toxic effects, including altered permeability of cellular membranes. The primary target for free cupric ions in the cellular membranes are thiol groups that reduce cupric (Cu+2) to cuprous (Cu+1) upon simultaneous oxidation to disulfides in the membrane. Cuprous ions are reoxidized to Cu+2 in the presence of molecular oxygen molecular oxygen is thereby converted to the toxic superoxide radical O2, which induces lipoperoxidation (Aaseth and Norseth 1986). 

Polyphenol oxidase occurs within certain mammalian tissues as well as both lower (46,47) and higher (48-55) plants. In mammalian systems, the enzyme as tyrosinase (56) plays a significant role in melanin synthesis. The PPO complex of higher plants consists of a cresolase, a cate-cholase and a laccase. These copper metalloproteins catalyze the one and two electron oxidations of phenols to quinones at the expense of 02. Polyphenol oxidase also occurs in certain fungi where it is involved in the metabolism of certain tree-synthesized phenolic compounds that have been implicated in disease resistance, wound healing, and anti-nutrative modification of plant proteins to discourage herbivory (53,55). This protocol presents the Triton X-114-mediated solubilization of Vida faba chloroplast polyphenol oxidase as performed by Hutcheson and Buchanan (57). 

In the present paper we describe the catalytic mechanisms of synthetic polymer-Cu complexes a catalytic interaction between the metal ions which attached to a polymer chain at high concentration and an environmental effect of polymer surrounding Cu ions. In the latter half, the catalytic behavior is compared with the specific one of tyrosinase enzyme in the melanin-formation reaction which is a multi-step reaction. To the following polymers Cu ions are combined. 

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... 

Nevertheless, some issues have to be addressed before this approach can be applied. Firstly, the tyrosinase gene is quite large and would be difficult to add to a delivery vector. Secondly, melanin production may be too low in vivo for effective MR detection of its metal complex [100]. Finally, potentially high toxicity of melanin and its precursors could restrict the applicability of this reporter gene [99]. 

Oxidative coupling polymerization provides great utility for the synthesis of high-performance polymers. Oxidative polymerization is also observed in vivo as important biosynthetic processes that, when catalyzed by metalloenzymes, proceed smoothly under an air atmosphere at room temperature. For example, lignin, which composes 30% of wood tissue, is produced by the oxidative polymerization of coniferyl alcohol catalyzed by laccase, an enzyme containing a copper complex as a reactive center. Tyrosine is an a-amino acid and is oxidatively polymerized by tyrosinase (Cu enzyme) to melanin, the black pigment in animals. These reactions proceed efficiently at room temperature in the presence of 02 by means of catalysis by metalloenzymes. Oxidative polymerization is observed in vivo as an important biosynthetic process that proceeds efficiently by oxidases. 

Kinetically slow steps in the formation of melanin from DOPA are the formation of dopaquinone from DOPA (step 1, kD), the reaction of dopachrome to dihydroxyindole (step 2), and the polymerization to form melanin (step 3, kM). Step 1 and step 2 proceed with about the same rate in the oxidative coupling polymerization catalyzed by tyrosinase. However, step 1 becomes remarkably slow when a macromolecule-metal complex is used as a catalyst. The copper complex in poly(l-vinylimidazole-co-vinylpyrrolidone) has been found [38] to act as an excellent catalyst and to exhibit the highest activity for melanin formation. The ratio of the rate constants ( m/ d) is approximately 3 (tyrosinase... 

Melanin, which is prepared by polymerization with a macromolecule-metal complex, is isolated as a black powder and shows strong absorption in the ultraviolet and visible regions. The free radical species is stable against heat, acid, and base, and the EPR shows a singlet signal at g = 2.00. These properties are also important in the physiological characteristics of melanin. 

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