|
pubmed:abstractText |
3,4-Dihydroxyphenylacetate 2,3-dioxygenase, an enzyme which catalyzes the extradiol cleavage of catechols, has been purified from Bacillus brevis. Like other extradiol-cleaving dioxygenases, this enzyme has a molecular weight of 140,000 with four subunits of 36,000 each. Unlike the other enzymes, this dioxygenase is not activated by added ferrous ion, not inhibited by cyanide or diethyldithiocarbamate, and not inactivated by H2O2. X-ray fluorescence and atomic absorption analyses show the enzyme to contain approximately 2 g atoms of manganese per mol of protein. EPR spectra are consistent with a manganese(II) center in an environment of low symmetry. This is the first report of an oxygen-activating manganese enzyme.
|
