BIOPHYSICAL ANALYSES OF DESIGNED AND SELECTED MUTANTS OF PROTOCATECHUATE 3,4-DIOXYGENASE
1C. Kent Brown,1 Matthew W. Vetting,1,2 Cathleen A. Earhart,1 and Douglas H. Ohlendorf11Center for Metals in Biocatalysis and Department of Biochemistry, Molecular Biology, and Biophysics, Minneapolis, Minnesota 55455; email:
brow0927@umn.edu;
earhart@umn.edu;
ohlen@umn.edu 2Department of Biochemistry, Albert Einstein College of Medicine, Bronx, New York 10461-1602 email:
vetting@aecom.yu.edu;
▪ 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.
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