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. 1992 Oct;58(10):3407-9.
doi: 10.1128/aem.58.10.3407-3409.1992.

Stereospecific hydroxylation of indan by Escherichia coli containing the cloned toluene dioxygenase genes from Pseudomonas putida F1

J M Brand  1 , D L Cruden, G J Zylstra, D T Gibson
Affiliations

Stereospecific hydroxylation of indan by Escherichia coli containing the cloned toluene dioxygenase genes from Pseudomonas putida F1

J M Brand et al. Appl Environ Microbiol. 1992 Oct.

Erratum in

  • Appl Environ Microbiol 1993 Jan;59(1):351

Abstract

Escherichia coli JM109(pDTG601), containing the todC1C2BA genes encoding toluene dioxygenase from Pseudomonas putida F1, oxidizes indan to (-)-(1R)-indanol (83% R) and trans-1,3-indandiol. Under similar conditions, P. putida F39/D oxidizes indan to (-)-(1R)-indanol (96% R), 1-indanone, and trans-1,3-indandiol. The differences in the enantiomeric composition of the 1-indanols formed by the two organisms are due to the presence of a 1-indanol dehydrogenase in P. putida F39/D that preferentially oxidizes (+)-(1S)-indanol.

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