Bacterial ring hydroxylating dioxygenases are multicomponent enzymatic
complexes composed of a hydroxylase component and an electron transfer
component. The hydroxylase component is itself composed of two subunits: an
α-subunit of about 50 Kd, and a β-subunit of about 20 Kd. The electron
transfer component is either composed of two subunits: a ferredoxin and a
ferredoxin reductase or by a single bifunctional ferredoxin/reductase subunit.
The α-subunit of hydroxylase components are evolutionary related [1]. The
currently known members of this family are listed below.
- Benzene 1,2-dioxygenase (EC 1.14.12.3) (gene bnzA) from Pseudomonas putida.
- phthalate 4,5-dioxygenase (EC 1.14.12.7) (gene pht3) from Pseudomonas.
- Benzoate 1,2-dioxygenase (EC 1.14.12.10) (gene benA) from Acinetobacter
calcoaceticus.
- Naphthalene 1,2-dioxygenase (EC 1.14.12.12) (gene ndoC) from Pseudomonas.
- 3-chlorobenzoate-3,4-dioxygenase (EC 1.14.12-.-) (gene cbaA) from
Alcaligenes.
- Biphenyl dioxygenase (EC 1.14.99.-) (gene bphA) from Pseudomonas.
- Toluate 1,2-dioxygenase (EC 1.14.12.-) (gene xylX) from Pseudomonas putida.
- Toluene 2,3-dioxygenase (EC 1.14.12.-) (gene todC1) from Pseudomonas
putida.
The α-subunit of the hydroxylase components bind both a 2Fe-2S type iron-sulfur center and an iron atom. There is, in the N-terminal section of these
proteins, a conserved region of 24 residues which contains two cysteines and
two histidines which have been shown [2] to be involved in the binding of the
iron-sulfur center. We have used this region has a signature pattern.
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