Correlation of thermostability and conformational changes of catechol 2, 3-dioxygenases from two disparate micro-organisms

Anna Sokolova*, Shir Ly Huang, Anthony Duff, Elliot Paul Gilbert, Wen Hsien Li

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


We have investigated the structure of recombinant catechol 2, 3-dioxygenase (C23O) purified from two species inwhich the enzyme has evolved to function at different temperature. The two species aremesophilic bacterium Pseudomonas putida strain mt-2 and thermophilic archaea Sulfolobus acidocaldarius DSM639. Using the primary sequence analysis, we show that both C23Os have only 30% identity and 48% similarity but contain conserved amino acid residues forming an active site area around the iron ion. The corresponding differences in homology, but structural similarity in active area residues, appear to provide completely different responses to heating the two enzymes. We confirm this bysmall angle X-ray scattering and demonstrate that the overall structure of C23O from P. putida is slightly different from its crystalline form whereas the solution scattering of C23O from S. acidocaldarius at temperatures between 4 and 85 °C ideally fits the calculated scattering from the single crystal structure. The thermostability of C23O from S. acidocaldarius correlateswellwith conformation in solution during thermal treatment. The similarity of the two enzymes in primary and tertiary structure may be taken as a confirmation that two enzymes have evolved from a common ancestor. Crown

Original languageEnglish
Pages (from-to)145-152
Number of pages8
JournalBiophysical Chemistry
StatePublished - 2013


  • Catechol 2, 3-dioxygenase
  • Modelling
  • Protein structure
  • Small angle X-ray scattering
  • Thermal effect


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