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J. Biol. Chem., Vol. 262, Issue 4, 1510-1518, Feb, 1987
CJ Batie, E LaHaie and DP Ballou
An enzymatic system has been isolated that catalyzes dihydroxylation of
phthalate to form 1,2-dihydroxy-4,5-dicarboxy-3,5-cyclohexadiene with
consumption of NADH and O2. This system is comprised of two proteins: a
flavo-iron-sulfur protein with NADH-dependent oxidoreductase activity and a
nonheme iron protein with oxygenase activity. Phthalate oxygenase is a
large (approximately 217 kDa) protein composed of apparently identical
48-kDa monomers. The active enzyme has one Rieske-type [2Fe- 2S] center and
one mononuclear iron/monomer. Removal of the mononuclear iron by incubation
with EDTA or with o-phenanthroline inhibits oxygenation; ferrous ion
completely restores activity. No other metals are effective. Phthalate
oxygenase is specific for phthalate or other closely related compounds.
However, only phthalate is tightly coupled to NADH oxidation and O2
consumption with a stoichiometry of 1:1:1. Phthalate oxygenase is
chemically competent to oxygenate phthalate when artificially supplied with
reducing equivalents and O2. Phthalate oxygenase reductase is required,
however, for efficient catalytic activity. The reductase is a monomeric
34-kDa flavo-iron-sulfur protein containing FMN and a plant-ferredoxin-type
[2Fe-2S] center in a 1:1 ratio. Phthalate oxygenase reductase is specific
for NADH but can pass electrons to a variety of acceptors, including:
phthalate oxygenase, cytochrome c, ferricyanide, and
dichlorophenolindophenol. This system is similar to other bacterial
oxygenase systems involved in aromatic degradation including: benzoate
dioxygenase, toluene dioxygenase, benzene dioxygenase, and
4-methoxybenzoate demethoxylase. However, phthalate oxygenase can be
isolated in large quantities and is more stable than most other such
systems.
Purification and characterization of phthalate oxygenase and phthalate oxygenase reductase from Pseudomonas cepacia
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