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Applied and Environmental Microbiology, January 1999, p. 315-318, Vol. 65, No. 1
0099-2240/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

The alpha  Subunit of Toluene Dioxygenase from Pseudomonas putida F1 Can Accept Electrons from Reduced FerredoxinTOL but Is Catalytically Inactive in the Absence of the beta  Subunit

Haiyan Jiang,dagger Rebecca E. Parales, and David T. Gibson*

Department of Microbiology and Center for Biocatalysis and Bioprocessing, The University of Iowa, Iowa City, Iowa 52242

Received 29 July 1998/Accepted 22 October 1998

The oxygenase component of toluene dioxygenase from Pseudomonas putida F1 is an iron-sulfur protein (ISPTOL) consisting of alpha  (TodC1) and beta  (TodC2) subunits. Purified TodC1 gave absorbance and electron paramagnetic resonance spectra identical to those given by purified ISPTOL. TodC1 was reduced by NADH and catalytic amounts of ReductaseTOL and FerredoxinTOL. Reduced TodC1 did not oxidize toluene, and catalysis was strictly dependent on the presence of purified TodC2.

* Corresponding author. Mailing address: Department of Microbiology, The University of Iowa, Iowa City, IA 52242-1109. Phone: (319) 335-7980. Fax: (319) 335-9999. E-mail: david-gibson{at}uiowa.edu.

dagger Present address: Lilly Research Laboratories, Indianapolis, IN 46285.

Applied and Environmental Microbiology, January 1999, p. 315-318, Vol. 65, No. 1
0099-2240/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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