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Copper enzymes galactose oxidases

Recently, some low-molecular-weight catalysts have been found that mimic enzymes and have potential practical applications. Reactions of limited complexity, mediated by metalloenzymes, have been reported. One such example is a mimic of the copper enzyme galactose oxidase, which catalyzes the oxidation of primary alcohols to aldehydes in the presence of air. [Pg.346]

Copper(II) complexes with phenoxo ligands have attracted great interest, in order to develop basic coordination chemistry for their possible use as models for tyrosinase activity (dimeric complexes) and fungal enzyme galactose oxidase (GO) (monomeric complexes). The latter enzyme catalyzes the two-electron oxidation of primary alcohols with dioxygen to yield aldehyde and... [Pg.800]

Interest in this class of coordination compounds was sparked and fueled by the discovery that radical cofactors such as tyrosyl radicals play an important role in a rapidly growing number of metalloproteins. Thus, in 1972 Ehrenberg and Reichard (1) discovered that the R2 subunit of ribonucleotide reductase, a non-heme metal-loprotein, contains an uncoordinated, very stable tyrosyl radical in its active site. In contrast, Whittaker and Whittaker (2) showed that the active site of the copper containing enzyme galactose oxidase (GO) contains a radical cofactor where a Cu(II) ion is coordinated to a tyrosyl radical. [Pg.152]

The alcohol dehydrogenases were already described in Chapter 3. These enzymes are cofactor dependent and in the active site hydrogen transfer takes place from NADH or NADPH. In the reverse way they can, however, be applied for the oxidation of alcohols in some cases (see below). Oxidases are very appealing for biocatalytic purposes, because they use oxygen as the only oxidant without the need for a cofactor. Oxidases usually have flavins (glucose oxidase, alcohol oxidase) or copper (examples galactose oxidase, laccase and tyrosinase) in the active site [18]. The mechanism for glucose oxidase (GOD) is denoted in... [Pg.142]

Copper(m)—A copper(iii) complex of the enzyme galactose oxidase has been postulated as the active intermediate in the oxidation of D-galactose. Autoxidation of copper(ii)-peptide complexes leads to relatively long-lived copper(iii)-peptide species. ... [Pg.303]

We have shown, in stoichiometric experiments, that reaction of copper(I) with TEMPO affords a piperidinyloxyl copper(II) complex. Reaction of the latter with a molecule of alcohol afforded the alkoxycopper(II) complex and TEMPOH. Reaction of the alkoxycopper(II) complex with a second molecule of TEMPO gave the carbonyl compound, copper(I), and TEMPOH. This mechanism resembles that proposed for the aerobic oxidation of alcohols catalyzed by the copper-dependent enzyme, galactose oxidase, and mimics thereof. Finally, TEMPOH is reoxidized to TEMPO by oxygen. We have also shown that copper in combination with PIPO affords an active and recyclable catalyst for alcohol oxidation [18]. [Pg.173]

Another oxidizing enzyme with very interesting synthetic potential is galactose oxidase [14]. This copper protein oxidizes primary hydroxy functions in polyols enantioselectively to the corresponding aldehydes. Thus, sugar alcohols may be transformed into the interesting non-natural L-configurated... [Pg.105]

Interest is mounting in this state, promoted once again by its possible implication in biological systems. Galactose oxidase, for example, is a copper enzyme which catalyses the oxidation of galactose to the corresponding aldehyde. The tervalent oxidation state may be prepared from Cu(II) by chemical, anodic and radical oxidation. Cu(III) complexes of peptides and macrocycles have been most studied, particularly from a mechanistic viewpoint. The oxidation of I" by Cu(III)-deprotonated peptide complexes and by imine-oxime complexes have a similar rate law... [Pg.418]

There are a number of excellent sources of information on copper proteins notable among them is the three-volume series Copper Proteins and Copper Enzymes (Lontie, 1984). A review of the state of structural knowledge in 1985 (Adman, 1985) included only the small blue copper proteins. A brief review of extended X-ray absorption fine structure (EXAFS) work on some of these proteins appeared in 1987 (Hasnain and Garner, 1987). A number of new structures have been solved by X-ray diffraction, and the structures of azurin and plastocyanin have been extended to higher resolution. The new structures include two additional type I proteins (pseudoazurin and cucumber basic blue protein), the type III copper protein hemocyanin, and the multi-copper blue oxidase ascorbate oxidase. Results are now available on a copper-containing nitrite reductase and galactose oxidase. [Pg.147]

So-called blue multinuclear copper oxidase enzymes, such as laccase and ascorbate oxidase, catalyze the stepwise oxidation of organic substrates (most likely in successive one-electron steps) in tandem with the four-electron reduction of O2 to water, i.e. no oxygen atom(s) from O2 are incorporated into the substrate (Eq. 4) [15]. Catechol oxidase, containing a type 3 center, mediates a two-electron substrate oxidation (o-diphenols to o-chinones), and turnover of two substrate molecules is coupled to the reduction of O2 to water [34,35]. The non-blue copper oxidases, e.g. galactose oxidase and amine oxidases [27,56-59], perform similar oxidation catalysis at a mononuclear type 2 Cu site, but H2O2 is produced from O2 instead of H2O, in a two-electron reduction. [Pg.31]

The selective oxidation of alcohols to the corresponding aldehydes and ketones is of prime importance for organic synthesis, and various types of reagents have been described that achieve this transformation selectively and efficiently [141,142]. However, the number of sub-stoichiometric, nontoxic, non-hazardous oxidation systems has been relatively Umited. As copper enzymes such as galactose oxidase are known to catalyze this oxidation reaction, bioinspired homogeneous catalysts based on copper species have also been developed in recent years. [Pg.40]

Galactose oxidase is an extracellular enzyme secreted by the fungus Dactylium den-droides. It is monomeric (M = 68000), contains a single copper site and catalyses the oxidation of a wide range of primary alcohols to the corresponding aldehydes. The two-electron transfer reaction RCH2OH - RCHO + 2H+ + 2e does not utilise a Cu(III)/Cu(I) couple, but a second redox site, involving a tyrosine radical which mediates the transfer of the second electron. [Pg.136]

Figure 3. Copper absorbance spectrum of galactose oxidase (775 nm not recorded) (----) and the enzyme in the presence of sodium azide (-). Spectra... Figure 3. Copper absorbance spectrum of galactose oxidase (775 nm not recorded) (----) and the enzyme in the presence of sodium azide (-). Spectra...
Table III). Atomic absorption analysis shows that the copper is still present in the enzyme. These two facts coupled with the 600-nm region intensity increase might be interpreted to suggest that a stereochemical distortion accompanies tryptophan oxidation in galactose oxidase. For example, a saddling of the planar environment would be expected to lower the reduction potential of the Cu(II)-Cu(I) couple. [Pg.277]

Galactose oxidase exhibits a mononuclear copper-active site, which is flanked by a tyrosinyl radical. In a single step, a two-electron oxidation of alcohols can be performed by this enzyme, where one electron is extracted by copper and the other by the tyrosine residue [19]. [Pg.143]

Copper would seem to be an appropriate choice of metal for the catalytic oxidation of alcohols with dioxygen since it comprises the catalytic centre in a variety of enzymes, e.g. galactose oxidase, which catalyze this conversion in vivo [188, 189]. Several catalytically active biomimetic models for these enzymes have been designed which are seminal examples in this area [190-193]. A complete overview of this field can be found in a review [194]. [Pg.179]

Galactose oxidase hinds a single copper ion within Domain 11 on the axis of the wheel. The active site (Fig. 5) is unhke any other biological copper complex, an appropriate distinction for this remarkable enzyme. To explore the site in more detail, the protein environment of the mononuclear copper center may be separated into (A) direcdy coordinated metal hgands (hrst shell, inner sphere interactions) and (B) the extended active site environment (the second shell or outer coordination sphere). [Pg.11]


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See also in sourсe #XX -- [ Pg.183 ]




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Copper enzymes

Copper enzymes oxidase

Enzyme oxidase

Galactose enzymes

Galactose oxidase

Galactose oxidase copper

Oxidases copper

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