The chloride-activated peroxidation of catechol as a mechanistic probe of chloroperoxidase reactions

Libby, R. Daniel; Rotberg, N S; Emerson, Jeffrey; White, Tyler; Yen, G M; Friedman, Samuel; Sun, Nannan; Goldowski, R

doi:10.1016/s0021-9258(19)84823-8

Cited by 23 publications

(2 citation statements)

References 19 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In the case of the more reactive phenols (1-3), substrate inhibition was observed at high substrate concentrations (above ~30mM) (Figure 2). A similar effect was noted in the CPOcatalyzed peroxidation of catechol (Libby et al, 1989). The kinetic measurements were then performed at substrate concentrations lower than those causing inhibition.…”

Section: Resultsmentioning

confidence: 52%

“…The other conditions were the same as in the kinetic experiments. A similar procedure was followed by Libby et al (1989) in the analysis of the kinetic data for the CPO-catalyzed peroxidation of catechol, but apparently the catalatic activity of this enzyme was not considered. The rectilinear plot obtained in each series of experiments ensured that the composition of the product mixture was constant in all measurements.…”

Section: Methodsmentioning

confidence: 99%

See 1 more Smart Citation

The Chloroperoxidase-Catalyzed Oxidation of Phenols. Mechanism, Selectivity, and Characterization of Enzyme-Substrate Complexes

Casella¹,

Poli²,

Gullotti³

et al. 1994

Biochemistry

View full text Add to dashboard Cite

The reactivity of a series of para-substituted phenolic compounds in the peroxidation catalyzed by chloroperoxidase was investigated, and the results were interpreted on the basis of the binding characteristics of the substrates to the active site of the enzyme. Marked selectivity effects are observed. These operate through charge, preventing phenolic compounds carrying amino groups on the substituent chain to act as substrates for the enzyme, and through size, excluding potential substrates containing bulky substituents to the phenol nucleus. Also, chiral recognition is exhibited by chloroperoxidase in the oxidation of N-acetyltyrosine, where only the L isomer is oxidized. Kinetic measurements show that, in general, the efficiency of chloroperoxidase in the oxidation of phenols is lower than that of horseradish peroxidase. Paramagnetic NMR spectra and relaxation rate measurements of chloroperoxidase-phenol complexes are consistent with binding of the substrates close to the heme, in the distal pocket, with the phenol group pointing toward the iron atom. On the other hand, phenolic compounds which are not substrates for chloroperoxidase bind to the enzyme with a much different disposition, with the phenol group very distant from the iron and probably actually outside the active-site cavity.

show abstract

Section: Resultsmentioning

confidence: 52%

Section: Methodsmentioning

confidence: 99%

The Chloroperoxidase-Catalyzed Oxidation of Phenols. Mechanism, Selectivity, and Characterization of Enzyme-Substrate Complexes

Casella¹,

Poli²,

Gullotti³

et al. 1994

Biochemistry

View full text Add to dashboard Cite

show abstract

Expanding the Scope of Biocatalysis: Oxidative Biotransformations on Solid‐Supported Substrates

Brooks¹,

Coulombel²,

Ahuja³

et al. 2008

Adv Synth Catal

View full text Add to dashboard Cite

Oxidative biocatalytic reactions were performed on solid-supported substrates, thus expanding the repertoire of biotransformations that can be carried out on the solid phase. Various phenylacetic and benzoic acid analogs were attached to controlled pore glass beads via an enzyme-cleavable linker. Reactions catalyzed by peroxidases (soybean and chloro), tyrosinase, and alcohol oxidase/dehydrogenase gave a range of products, including oligophenols, halogenated aromatics, catechols, and aryl aldehydes. The resulting products were recovered following cleavage from the beads using α-chymotrypsin to selectively hydrolyze a chemically non-labile amide linkage. Controlled pore glass (CPG) modified with a polyethylene glycol (PEG) linker afforded substantially higher product yields than non-PEGylated CPG or non-swellable polymeric resins. This work represents the first attempt to combine solid-phase oxidative biotransformations with subsequent protease-catalyzed cleavage, and serves to further expand the use of biocatalysis in synthetic and medicinal chemistry.

show abstract

Oxidation of Chloride and Subsequent Chlorination of Organic Compounds by Oxoiron(IV) Porphyrin π‐Cation Radicals

Cong¹,

Kurahashi²,

Fujii³

2011

Angewandte Chemie

View full text Add to dashboard Cite

π‐Radikalkationenkomplexe von Oxoeisen(IV)‐porphyrin (siehe Bild) dienen als Modelle für die Oxidation von Cl− zu einem aktiven Chlorierungsreagens, das verschiedenste organische Verbindungen chloriert. Hinweise sprechen dafür, dass Cl− über Cl. zu Cl2 oxidiert wird. Der Mechanismus umfasst entweder einen direkten Elektronentransfer oder die Bildung eines Eisen(III)‐hypochlorits mit anschließender Homolyse der Cl‐O‐Bindung.

show abstract

The chloride-activated peroxidation of catechol as a mechanistic probe of chloroperoxidase reactions

Cited by 23 publications

References 19 publications

The Chloroperoxidase-Catalyzed Oxidation of Phenols. Mechanism, Selectivity, and Characterization of Enzyme-Substrate Complexes

The Chloroperoxidase-Catalyzed Oxidation of Phenols. Mechanism, Selectivity, and Characterization of Enzyme-Substrate Complexes

Expanding the Scope of Biocatalysis: Oxidative Biotransformations on Solid‐Supported Substrates

Oxidation of Chloride and Subsequent Chlorination of Organic Compounds by Oxoiron(IV) Porphyrin π‐Cation Radicals

Contact Info

Product

Resources

About