The alpha subunit of toluene dioxygenase from Pseudomonas putida F1 can accept electrons from reduced Ferredoxin(TOL) but is catalytically inactive in the absence of the beta subunit

Authors
Jiang, HY Parales, RE Gibson, DT
Citation
Hy. Jiang et al., The alpha subunit of toluene dioxygenase from Pseudomonas putida F1 can accept electrons from reduced Ferredoxin(TOL) but is catalytically inactive in the absence of the beta subunit, APPL ENVIR, 65(1), 1999, pp. 315-318
Citations number
36
Categorie Soggetti
Biology,Microbiology
Journal title
APPLIED AND ENVIRONMENTAL MICROBIOLOGY
ISSN journal
00992240 → ACNP
Volume
65
Issue
1
Year of publication
1999
Pages
315 - 318
Database
ISI
SICI code
0099-2240(199901)65:1<315:TASOTD>2.0.ZU;2-D
Abstract
The oxygenase component of toluene dioxygenase from Pseudomonas putida Fl i s an iron-sulfur protein (ISPTOL) consisting of alpha (TodC1) and beta (Tod C2) subunits. Purified TodC1 gave absorbance and electron paramagnetic reso nance spectra identical to those given by purified ISPTOL. TodC1 was reduce d by NADH and catalytic amounts of Reductase(TOL) and Ferredoxin(TOL). Redu ced TodC1 did not oxidize toluene, and catalysis was strictly dependent on the presence of purified TodC2.