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In this work, we have purified the His-tagged oxygenase (ht-oxygenase) component of Rhodococcus globerulus P6 biphenyl dioxygenase. The α or β subunit of P6 oxygenase was exchanged with the corresponding subunit of Pseudomonas sp. strain LB400 or of Comamonas testosteroni B-356 to create new chimeras that were purified ht-proteins and designated ht-α P6 β P6 , ht-α P6 β LB400 , ht-α P6 β B-356 , ht-α LB400 β P6 , and ht-α B-356 β P6 . ht-α P6 β P6 , ht-α P6 β LB400 , ht-α P6 β B-356 were not expressed active in recombinant Escherichia coli cells carrying P6 bphA1 and bphA2 , P6 bphA1 and LB400 bphE , or P6 bphA1 and B-356 bphE because the [2Fe-2S] Rieske cluster of P6 oxygenase α subunit was not assembled correctly in these clones. On the other hand ht-α LB400 β P6 and ht-α B-356 β P6 were produced active in E. coli . Furthermore, active purified ht-α P6 β P6 , ht-α P6 β LB400 , ht-α P6 β B-356 , showing typical spectra for Rieske-type proteins, were obtained from Pseudomonas putida KT2440 carrying constructions derived from the new shuttle E. coli-Pseudomonas vector pEP31, designed to produce ht-proteins in Pseudomonas . Analysis of the substrate selectivity pattern of these purified chimeras toward selected chlorobiphenyls indicate that the catalytic capacity of hybrid enzymes comprised of an α and a β subunit recruited from distinct biphenyl dioxygenases is not determined specifically by either one of the two subunits.

journal of bacteriology

Heterologous Expression and Characterization of the Purified Oxygenase Component of Rhodococcus globerulusP6 Biphenyl Dioxygenase and of Chimeras Derived from It