Phthalate dioxygenase reductase, structure

Phthalate dioxygenase, 47 119 ENDOR and ESEEM studies, 47 132 spin-spin interactions, 47 466 Phthalate dioxygenase reductase, structure, 47 150... 

The structure of phthalate dioxygenase reductase that transfers electrons directly from NADPH to phthalate dioxygenase has been determined by X-ray crystallography (119). In class II or class III dioxygenases, the ferredoxin obligately transfers electrons from the reductase to the terminal dioxygenase (64a) it can be either a Rieske-type ferredoxin or a ferredoxin containing a 4-cysteine coordinated [2Fe-2S] cluster. 

Correll, C. C., Batie, C. J., Ballou, D. P., and Ludwig, M. L., 1992, Phthalate dioxygenase reductase a modular structure for electron transfer from pyridine nucleotides to [2Ee-2S], Science 258 1604nl610. 

One of the two important parts of enzyme is a flavo-iron-sulfur protein with NADH-dependent oxidoreductase activity. The reductase is a monomeric 34 kDa (in case of phthalate dioxygenase reductase) flavo-iron-sulfur protein containing flavin mononucleotide (FMN) and a plant-ferredoxin-type [2Fe-2S] center in a 1 1 ratio [372]. Structure of this part of the enzyme has been studied recently by X-ray crystallographic analysis [375], low-temperature EPR [383], and kinetically [378]. 

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