Biophysical analyses of designed and selected mutants of protocatechuate 3,4-dioxygenase1.

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

Index: Annu. Rev. Microbiol. 58 , 555-85, (2004)

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Abstract

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.