Biophysical analyses of designed and selected mutants of protocatechuate 3,4-dioxygenase

C. Kent Brown, Matthew W. Vetting, Cathleen A. Earhart, Douglas H. Ohlendorf

Research output: Contribution to journalReview articlepeer-review

12 Scopus citations


The catechol dioxygenases allow a wide variety of bacteria to use aromatic compounds as carbon sources by catalyzing the key ring-opening step. These enzymes use specifically either catechol or protocatechuate (2,3- dihydroxybenozate) as their substrates; they use a bare metal ion as the sole cofactor. To learn how this family of metalloenzymes functions, a structural analysis of designed and selected mutants of these enzymes has been undertaken. Here we review the results of this analysis on the nonheme ferric iron intradiol dioxygenase protocatechuate 3,4-dioxygenase.

Original languageEnglish (US)
Pages (from-to)555-585
Number of pages31
JournalAnnual Review of Microbiology
StatePublished - Dec 7 2004


  • Catechol
  • Crystallography
  • Dioxygenase
  • Iron
  • Metalloenzyme
  • Protocatechuate

ASJC Scopus subject areas

  • Microbiology


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