Transient model of thermal deactivation of enzymes

G. Chen*, Kalvin Gregory, Ye Sun, Val Golovlev

*Corresponding author for this work

Research output: Contribution to journalArticle

6 Scopus citations


The kinetics of enzyme deactivation provide useful insights on processes that determine the level of biological function of any enzyme. Photinus pyralis (firefly) luciferase is a convenient enzyme system for studying mechanisms and kinetics of enzyme deactivation, refolding, and denaturation caused by various external factors, physical or chemical by nature. In this report we present a study of luciferase deactivation caused by increased temperature (i.e., thermal deactivation). We found that deactivation occurs through a reversible intermediate state and can be described by a Transient model that includes active and reversibly inactive states. The model can be used as a general framework for analysis of complex, multiexponential transient kinetics that can be observed for some enzymes by reaction progression assays. In this study the Transient model has been used to develop an analytical model for studying a time course of luciferase deactivation. The model might be applicable toward enzymes in general and can be used to determine if the enzyme exposed to external factors, physical or chemical by nature, undergoes structural transformation consistent with thermal mechanisms of deactivation.

Original languageEnglish
Pages (from-to)1318-1324
Number of pages7
JournalBiochimica et Biophysica Acta - Proteins and Proteomics
Issue number10
StatePublished - 1 Oct 2011


  • Deactivation
  • Denaturation
  • Enzyme
  • Heating
  • Protein

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