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pubmed-article:15487948pubmed:abstractTextThe 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.lld:pubmed
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pubmed-article:15487948pubmed:articleTitleBiophysical analyses of designed and selected mutants of protocatechuate 3,4-dioxygenase1.lld:pubmed
pubmed-article:15487948pubmed:affiliationCenter for Metals in Biocatalysis and Department of Biochemistry, Molecular Biology, and Biophysics , Minneapolis, Minnesota 55455, USA. brow0927@umn.edulld:pubmed
pubmed-article:15487948pubmed:publicationTypeJournal Articlelld:pubmed
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