Peroxidase-catalyzed

Siegel S.M. (1957) Non-enzymic macromolecules as matrices in biological synthesis. The role of polysaccharides in peroxidase catalyzed lignin polymer formation from eugenol // J. Amer. Chem. Soc. V. 79. P. 1628-1632... 

Wasserman, B.P, Eiberger, L.L., and Guilfoy, M.P., Effect of hydrogen peroxide and phenolic compounds on horseradish peroxidase-catalyzed decolorization of betalain pigments, J. Food Sci., 49, 536, 557, 1984. 

The peroxidase-catalyzed polymerization of m-alkyl substituted phenols in aqueous methanol produced soluble phenolic polymers. The mixed ratio of buffer and methanol greatly affected the yields and the molecular weight of the polymer. The enzyme source greatly affected the polymerization pattern of m-substituted monomers. Using SBP catalyst, the polymer yield increased as a function of the bulkiness of the substituent, whereas the opposite tendency was observed when HRP was the catalyst. 

Fluorinated phenols, 3- and 4-fiuorophenols, and 2,6-difluorophenol, were subjected to peroxidase-catalyzed polymerization in an aqueous organic solvent, yielding fluorine-containing polymers. Elimination of fluorine atom partly took place during the polymerization to give polymers with complicated structures. 

A polynucleoside with an unnatural polymeric backbone was synthesized by SBP-catalyzed oxidative polymerization of thymidine 5 -p-hydroxyphenylacetate. Chemoenzymafic synthesis of a new class of poly(amino acid), poly(tyrosine) containing no peptide bonds, was achieved by the peroxidase-catalyzed oxidative polymerization of tyrosine ethyl esters, followed by alkaline hydrolysis. Amphiphile higher alkyl ester derivatives were also polymerized in... 

Liu, H. Qin,Z. Thatcher, G. R. Bolton, J.L. Uterine peroxidase-catalyzed formation of diquinone methides from the selective estrogen receptor modulators raloxifene and desmethylated arzoxifene. Chem. Res. Toxicol. 2007, 20, 1676-1684. 

Tobimatsu, Y. Takano, T. Kamitakahara, H. Nakatsubo, F. Azide ion as a quinone methide scavenger in the horseradish peroxidase catalyzed polymerization of sinapyl alcohol. J. WoodSci. 2008, 54, 87-89. 

Foumand, D. Cathala, B. Lapierre, C. Initial steps of the peroxidase-catalyzed polymerization of coniferyl alcohol and/or sinapyl aldehyde capillary zone electrophoresis study of pH effect. Phytochemistry 2003, 62, 139-146. 

Kazunga, C., Aitken, M.D., and Gold, A., Primary product of the horseradish peroxidase-catalyzed oxidation of pentachlorophenol, Environ. Sci. Technol., 33, 1408-1412, 1999. 

Allen, B.L. et al. (2009) Mechanistic investigations of horseradish peroxidase-catalyzed degradation of single-walled carbon nanotubes. Journal of the American Chemical Society,... 

How the aliphatic monomers are incorporated into the suberin polymer is not known. Presumably, activated co-hydroxy acids and dicarboxylic acids are ester-ified to the hydroxyl groups as found in cutin biosynthesis. The long chain fatty alcohols might be incorporated into suberin via esterification with phenylpro-panoic acids such as ferulic acid, followed by peroxidase-catalyzed polymerization of the phenolic derivative. This suggestion is based on the finding that ferulic acid esters of very long chain fatty alcohols are frequently found in sub-erin-associated waxes. The recently cloned hydroxycinnamoyl-CoA tyramine N-(hydroxycinnamoyl) transferase [77] may produce a tyramide derivative of the phenolic compound that may then be incorporated into the polymer by a peroxidase. The glycerol triester composed of a fatty acid, caffeic acid and a>-hydroxy acid found in the suberin associated wax [40] may also be incorporated into the polymer by a peroxidase. 

For oxalate detection, authors proposed a similar detection approach for recognition of oxalate via an immobilized oxalate oxidase/peroxidase couple and dye precursors MBTH (3-methyl-2-benzothiazolinone hydrazone) and DMAB (3-dimethylaminobenzoic acid). The peroxide generated by oxidation of oxalate to CO2 reacted with the dye precursors in a peroxidase-catalyzed reaction to yield an indamine dye with absorption maximum at 590 nm. The concentration of oxalate was correlated with increased absoiption from dye. 

Alternative metabolic pathways involve ring-oxidation and peroxidation of arylamines. Although ring-oxidation is generally considered a detoxification reaction, an electrophilic iminoquinone (X) can be formed by a secondary oxidation of the aminophenol metabolite (18,19). Lastly, reactive imines (XI) can be formed from the primary arylamines by peroxidase-catalyzed reactions that involve free radical intermediates (reviewed in 20). 

For example, peroxidase catalyzes the reaction of luminol derivatives with hydrogen peroxide and results in an increase of the CL reaction velocity and CL intensity. Therefore, intense CL can be obtained from the analyte labeled with luminol derivatives after HPLC separation, followed by reaction with peroxidase. 

For a long time one question remained unanswered the efficiency of the Fenton reaction as the in vivo producer of hydroxyl radicals due to the low rate of Reaction (2) (the rate constant is equal to 42.11 mol 1 s 1 [18]). It is known that under in vitro conditions the rate of Fenton reaction can be sharply enhanced by chelators such as EDTA, but for a long time no effective in vivo chelators have been found. From this point of view new findings obtained by Chen and Schopfer [19] who found that peroxidases catalyze hydroxyl radical formation in plants deserve consideration. These authors showed that horseradish peroxidase (HRP) compound III is a catalyst of the Fenton reaction and that this compound is one to two orders of magnitude more active than Fe EDTA. 

Inhibits the peroxidase-catalyzed oxidation of I- and, thus, interferes with the incorporation of T into an organic structure... 

Inhibits the peroxidase-catalyzed coupling of iodotyrosines to form iodothyronines... 

Microbial transformations of ellipticine (15) and 9-methoxyellipticine (16) were reported by Chien and Rosazza (143, 144). Of 211 cultures screened for their abilities to transform 9-methoxyellipticine (16), several, including Botrytis alii (NRRL 2502), Cunninghamella echinulata (NRRL 1386), C. echinulata (NRRL 3655), and Penicillium brevi-compactum (ATCC 10418), achieved O-demethylation of 16 in good yield (Scheme 9). P. brevi-compactum was used to prepare 9-hydroxyellipticine (22) from the methoxylated precursor, and 150 mg of product was obtained from 400 mg of starting material (37% yield). The structure of the metabolite was confirmed by direct comparison with authentic 9-hydroxyellipticine (143). O-Demethylation is a common microbial metabolic transformation with 16 and many other alkaloids (143). Meunier et al. have also demonstrated that peroxidases catalyze the O-demethylation reaction with 9-methoxyellipticine (145). 

The reactivity of compounds such as 28 was clearly demonstrated by the peroxidase-catalyzed covalent binding of A -methyW-hydroxyellipticine (27) to proteins (756). Using horseradish peroxidase and hydrogen peroxide, tritiated-27 was converted to the 9-oxoellipticine derivative in the presence of bovine serum albumin (BSA) and human antibovine IgG in vitro. Covalent binding to these proteins was confirmed by gel electrophoresis, combustion, and liquid scintillation analysis. Dissolution of the BSA-ellipticinium derivative with pronase and... 

Indicine IV-oxide (169) (Scheme 36) is a clinically important pyrrolizidine alkaloid being used in the treatment of neoplasms. The compound is an attractive drug candidate because it does not have the acute toxicity observed in other pyrrolizidine alkaloids. Indicine IV-oxide apparently demonstrates increased biological activity and toxicity after reduction to the tertiary amine. Duffel and Gillespie (90) demonstrated that horseradish peroxidase catalyzes the reduction of indicine IV-oxide to indicine in an anaerobic reaction requiring a reduced pyridine nucleotide (either NADH or NADPH) and a flavin coenzyme (FMN or FAD). Rat liver microsomes and the 100,000 x g supernatant fraction also catalyze the reduction of the IV-oxide, and cofactor requirements and inhibition characteristics with these enzyme systems are similar to those exhibited by horseradish peroxidase. Sodium azide inhibited the TV-oxide reduction reaction, while aminotriazole did not. With rat liver microsomes, IV-octylamine decreased... 

Josephy PD. The role of peroxidase-catalyzed activation of aromatic amines in breast cancer. Mutagenesis 1996 11 (1 ) 3—7. 

Miwa GT, Walsh JS, Kedderis GL, et al. The use of intramolecular isotope effects to distinguish between deprotonation and hydrogen atom abstraction mechanisms in cytochrome P-450- and peroxidase-catalyzed N-demethylation reactions. J Biol Chem 1983 258(23) 14445-14449. 

There is huge potential in the combination of biocatalysis and electrochemistry through reaction engineering as the linker. An example is a continuous electrochemical enzyme membrane reactor that showed a total turnover number of 260 000 for the enantioselective peroxidase catalyzed oxidation of a thioether into its sulfone by in situ cathodic generated hydrogen peroxide - much higher than achieved by conventional methods [52],... 

V. Christian, R. Shrivastava, D. Shukla, H. Modi and B.R. M. Vyas, Mediator role of veratryl alcohol in the lignin peroxidase-catalyzed oxidati decolorization of Remazol Brilliant Blue R. Enz. Microbiol. Technol., 36 (2005) 327-332. 

C. C. C. Vidigal, A. Faljoni-Alario, N. Duran, K. Zinner, Y. Shimizu, and G. Cilento, Electronically excited species in the peroxidase catalyzed oxidation of indoleacetic acid. Effect upon DNA and RNA, Photochem. Photobiol. 30, 195-198 (1979). 

Coulter et al. (1999,2000b) showed that, in vitro, D. vulgaris Rbr has the ability to function as the terminal component of an NADH peroxidase, catalyzing the reduction of hydrogen peroxide to water (Eq. 10.4). 

A broad spectrum of chemical reactions can be catalyzed by enzymes Hydrolysis, esterification, isomerization, addition and elimination, alkylation and dealkylation, halogenation and dehalogenation, and oxidation and reduction. The last reactions are catalyzed by redox enzymes, which are classified as oxidoreductases and divided into four categories according to the oxidant they utilize and the reactions they catalyze 1) dehydrogenases (reductases), 2) oxidases, 3) oxygenases (mono- and dioxygenases), and 4) peroxidases. The latter enzymes have received extensive attention in the last years as bio catalysts for synthetic applications. Peroxidases catalyze the oxidation of aromatic compounds, oxidation of heteroatom compounds, epoxidation, and the enantio-selective reduction of racemic hydroperoxides. In this article, a short overview... 

Horseradish peroxidase has been intensively studied for the elucidation of the mechanism of peroxidase catalysis [24-28]. Some important mechanistic features of peroxidase-catalyzed reaction are briefly described here. 

The peroxidase-catalyzed transformations are classified as (1) the peroxidase reaction (Table 2, entries 1 -4), (2) the peroxygenase reaction (Table 2, entries 4-6) [25], and (3) the oxidase reaction (Table 2,entries 7-9). 

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