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Chemoselective Preparation of 1-Iodoalkynes, 1,2-Diiodoalkenes, and 1,1,2-Triiodoalkenes Based on the Oxidative Iodination of Terminal Alkynes
Published on: September 12, 2018
Laccase-catalysed iodide oxidation in presence of methyl syringate
Juozas Kulys1, Irina Bratkovskaja, Regina Vidziunaite
1Department of Enzyme Chemistry, Institute of Biochemistry, Mokslininku 12, LT-08662 Vilnius, Lithuania. jkulys@bchi.lt
Abstract:
The kinetics of potassium triiodide (KI(3)) formation during fungal laccase action was investigated in presence of methyl syringate (MS). The recombinant forms of Polyporus pinsitus (rPpL), Myceliophthora thermophila (rMtL), Coprinus cinereus (rCcL), and Rhizoctonia solani (rRsL) laccases were used. The triiodide formation rate reached 6.1, 5.5, 6.0, and 2.1 microM/min at saturated rPpL, rCcL, rRsL, and rMtL concentration, respectively, in acetate buffer solution pH 5.5 and in presence of 10 microM of MS and 1 mM of potassium iodide. The triiodide formation rate increased if pH decreased from 6.5 to 4.5. The scheme of laccase-catalysed iodide oxidation includes stadium of MS interaction with oxidized laccase with concomitant production of MS(ox). The reaction of MS(ox) with iodide produced triiodide. The turnover number of MS was 93 and 44 at pH 5.5 for rPpL and rMtL, respectively. The scheme also contained a stadium of reversible reduction of laccase active centre with the mediator explaining the different saturation rate of triiodide production. The fitting kinetic data revealed that the reversibility of the reaction increased for laccases containing lower redox potential of copper type I.
Insights
Fungal laccases catalyze potassium triiodide (KI(3)) formation using methyl syringate (MS) as a mediator. Reaction rates vary with laccase type and pH, influenced by redox potential and reversible reaction steps.
Area of Science:
- Biocatalysis
- Enzyme kinetics
- Environmental chemistry
Background:
- Fungal laccases are versatile oxidoreductases with potential applications in various industrial processes.
- Understanding the kinetics of laccase-mediated reactions is crucial for optimizing their use.
- Potassium triiodide (KI(3)) formation is a relevant reaction pathway involving iodide oxidation.
Purpose of the Study:
- To investigate the kinetics of potassium triiodide (KI(3)) formation catalyzed by fungal laccases.
- To elucidate the reaction mechanism involving methyl syringate (MS) as a mediator.
- To compare the activity and kinetic parameters of different recombinant fungal laccase forms.
Main Methods:
- Utilized recombinant fungal laccase forms: Polyporus pinsitus (rPpL), Myceliophthora thermophila (rMtL), Coprinus cinereus (rCcL), and Rhizoctonia solani (rRsL).
- Measured triiodide formation rates spectrophotometrically under varying pH conditions (4.5-6.5) and substrate concentrations.
- Analyzed kinetic data to determine reaction rates, turnover numbers, and reversibility of the catalytic cycle.
Main Results:
- Triiodide formation rates varied significantly among laccases, with rPpL, rCcL, and rRsL showing higher rates than rMtL at pH 5.5.
- The reaction rate increased as pH decreased from 6.5 to 4.5.
- A reaction mechanism was proposed involving methyl syringate oxidation and subsequent reaction with iodide, with reversibility influenced by the laccase's redox potential.
Conclusions:
- Fungal laccases, particularly rPpL, rCcL, and rRsL, efficiently catalyze KI(3) formation with MS as a mediator.
- pH significantly impacts the reaction rate, with optimal activity observed at lower pH values.
- The reversibility of the laccase-mediator interaction plays a key role in the observed kinetic differences and saturation rates.
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