The Microcalorimetric Studies on the Inhibition Kinetics of Enzyme-catalyzed Reaction──Fluoride Ion Inhibiting Laccase-catalyzed Oxidation Reaction of o-Phenylenediamine

Abstract

Abstract: Thermokinetic equation is proposed as Ω₀^-1=A[S₀]^-1 + B,which is available for all kinds of reversible inhibitions of single-substrate enzyme-catalyzed reactions.According to the relations between A/B, Band K_m,Ω_m,the type of the reversible inhibition can be judged as competitive, non-competitive and uncompetitive inhibitions.The thermokinetic formula which can be used to calculated the apparent Michelis constant K_m,app,inhibition constant Kand so on are given.The theory proposed has been applied to the kinetic determination of laccase-catalyzed oxidation reaction of o-phenylenediamine inhibited by fluoride ion.The experimental result shows that this reaction belongs to non-competitive inhibition,K_m.app=9.712×10^-2mol·L^-1,K_t=2.090×10^-2mol·L^-1.

Key words: Microcalorimetry, Thermokinetics, Inhibition, Laccase

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XIONG Ya, WU Ding-Quan, ZHOU Guang-Ming, DU Yu-Min, QU Song-Sheng. The Microcalorimetric Studies on the Inhibition Kinetics of Enzyme-catalyzed Reaction──Fluoride Ion Inhibiting Laccase-catalyzed Oxidation Reaction of o-Phenylenediamine[J]. Chem. J. Chinese Universities, 1996, 17(3): 460.

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The Microcalorimetric Studies on the Inhibition Kinetics of Enzyme-catalyzed Reaction──Fluoride Ion Inhibiting Laccase-catalyzed Oxidation Reaction of o-Phenylenediamine

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