Catechol enzymatic preparation

For determination of free PPO activity, different concentrations of catechol were prepared. Solutions contain 1.0 ml citrate buffer, 0.5 ml MBTH (0.3% in ethanol) and 0.5 ml catechol. 1 minute of reaction time was given after the addition of 0.5 ml enzyme solution (O.lmg/ml). 0.5 ml sulfuric acid (5% v/v) was added to stop the enzymatic reaction. Quinone produced reacts with MBTH to form a red color complex and this complex was dissolved by adding 3.0 ml acetone in the test tube. After mixing, absorbance was measured at 495 nm by using a Shimadzu UV-Visible spectrophotometer. 

In fluorine-18 chemistry some enzymatic transformations of compounds already labelled with fluorine-18 have been reported the synthesis of 6-[ F] fluoro-L-DOPA from 4-[ F]catechol by jS-tyrosinase [241], the separation of racemic mixtures of p F]fluoroaromatic amino acids by L-amino acylase [242] and the preparation of the coenzyme uridine diphospho-2-deoxy-2-p F]fluoro-a-o-glucose from [ F]FDG-1-phosphate by UDP-glucose pyrophosphorylase [243]. In living nature compounds exhibiting a carbon-fluorine bond are very rare. 

With the assumption that reticulines are also precursors in mammalian synthesis of morphine, it was challenging to investigate whether they could be produced by enzymatic reactions similar to those utilized in benzylisoquinoline-producing plants (274). This plan focused attention on reactions controlled by the enzyme catechol 0-methyltransferase (COMT), using 5-adenosyl-L-methionine (SAM) for the methylation reaction. Mammalian COMT is present in mammalian tissues, particularly the liver, and an enzyme preparation from rat liver was used for the experiments. It was found that (S)-norcoclaurine, which is the first isoquinoline produced in benzylisoquinoline-producing plants, was similarly O-methylated in vitro by SAM in the presence of COMT, and a reverse proportion of methylated products was obtained with the (/ )-enantiomer (277). Similar 0-methylation of (5)-4 -demethylreticuline (3 -hydroxy-N-methylcoclaurine), prepared by total synthesis (162), however, afforded almost exclusively (5)-orientaline, with a methoxy group at C-3 and not at C-4 as in (5)-reticuline (Fig. 37) (762). 

Enzymatically synthesized polyphenol derivatives are expected to have great potential for electronic applications. The surface resistivity of poly(p-phe-nylphenol) doped with nitrosylhexafluorophosphate was around 105 Q.4a The iodine-labeled poly(catechol) showed low electrical conductivity in the range from 10 6 to 10 9 S/cm.48 The iodine-doped thin film of poly (phenol- co- tetradecyloxyphenol) showed a conductivity of 10 2 S/cm, which was much larger than that obtained in aqueous 1,4-dioxane.24a The third-order optical nonlinearity (%3) of this film was 10 9 esu. An order of magnitude increase in the third-order nonlinear optical properties was observed in comparison with that prepared in the aqueous organic solution. 

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). 

It is now well-established that some enzyme families, including various peroxidases and laccases, catalyze the polymerization of vinyl monomers and other redox active species such as phenol-type structures. Vinyl polymerization by these redox catalysts has recently been reviewed 93). These catalysts have been used to prepare polyanilines 94) and polyphenols 95,96). A few examples of related research are included in this book. For example. Smith et al (57) described a novel reaction catalyzed by horseradish peroxidase (HRP). In the presence of HRP and oxygen, D-glucuronic acid was polymerized to a high molecular weight (60,000) polyether. However, the authors have not yet illucidated the polyether structure. Two other oxidative biotransformations were discussed above i) the sono-enzymatic polymerization of catechol via laccase 31), and ii) the oxidation of aryl silanes via aromatic dioxygenases 30). 

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