Kinetics of N-substituted phenothiazines and N-substituted phenoxazines oxidation catalyzed by fungal laccases |
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Authors: | Lidija Tetianec Juozas Kulys |
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Institution: | (1) Department of Enzyme Chemistry, Institute of Biochemistry, 08662 Vilnius, Lithuania;(2) Faculty of Fundamental Sciences, Department of Chemistry and Bioengineering, Vilnius Gediminas Technical University, 10223 Vilnius, Lithuania |
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Abstract: | Laccase-catalyzed oxidation of N-substituted phenothiazines and N-substituted phenoxazines was investigated at pH 5.5 and
25°C. The recombinant laccase from Polyporus pinsitus (rPpL) and the laccase from Myceliophthora thermophila (rMtL) were used. The dependence of initial reaction rate on substrate concentration was analyzed by applying the laccase
action scheme in which the laccase native intermediate (NI) reacts with a substrate forming reduced enzyme. The reduced laccase
produces peroxide intermediate (PI) which in turn decays to the NI. The calculated constant (kox) values of the PI formation are (6.1±3.1)×105 M−1s−1 for rPpL and (2.5±0.9)×104 M−1s−1 for rMtL. The bimolecular constants of the reaction of the native intermediate with electron donor (kred) vary in the interval
from 2.2×105 to 2.1×107 M−1s−1 for rPpL and from 1.3×102 to 1.8×105 M-1s−1 for rMtL. The larger reactivity of rPpL in comparison to rMtL is associated with the higher redox potential of type I Cu
of rPpL. The variation of kred values for both laccases correlates with the change of the redox potential of substrates. Following outer sphere (Marcus)
electron transfer mechanism the calculated activationless electron transfer rate and the apparent reorganization energy are
5.0×107 M−1s−1 and 0.29 eV, respectively. |
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Keywords: | Laccase Kinetics Phenoxazine Phenothiazine Oxygen Bimolecular rate constant Redox potential |
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