Rosche, Bettina and Fetzner, Susanne and Lingens, Franz and Nitschke, Wolfgang and Riedel, Astrid (1995) The 2Fe2S centres of the 2-oxo-1,2-dihydroquinoline 8-monooxygenase from Pseudomonas putida 86 studied by EPR spectroscopy. BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY, 1252 (2). pp. 177-179. ISSN 0167-4838
Full text not available from this repository.Abstract
The 2-oxo-1,2-dihydroquinoline 8-monooxygenase from Pseudomonas putida 86 comprises two components with four redox active sites necessary for activity. We present an EPR characterization of the iron-sulfur centres in the purified reductase and oxygenase component of this novel enzyme system. The oxygenase component was identified as a Rieske [2Fe2S] protein on the basis of its characteristic EPR spectrum with g(z,y,x) = 2.01, 1.91, 1.76 and g(av) = 1.893. The reductase component, an iron-sulfur flavoprotein, contained a [2Fe2S] cluster with g(z,y,x) = 2.03, 1.94, 1.89 and the average g-value(g(av)) of 1.953, typical of a ferredoxin-type centre. In redox titrations at pH 7, the midpoint potentials were determined to be -180 mV +/- 30 mV and -100 mV +/- 10 mV for the reductase and oxygenase component, respectively. A detailed comparison to other multicomponent enzyme systems is presented pointing out the EPR and redox properties of the FeS centres involved.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | ELECTRON-SPIN-RESONANCE; THERMUS RIESKE PROTEIN; SP STRAIN NCIB-9816; NAPHTHALENE DIOXYGENASE; PHTHALATE DIOXYGENASE; TOLUENE DIOXYGENASE; 4-CHLOROPHENYLACETATE 3,4-DIOXYGENASE; PURIFICATION; COMPONENT; REDUCTASE; EPR; IRON-SULFUR CENTER; RIESKE CENTER; FERREDOXIN; MONOOXYGENASE; DIOXYGENASE; (P-PUTIDA) |
| Subjects: | 500 Science > 540 Chemistry & allied sciences 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie |
| Depositing User: | Petra Gürster |
| Date Deposited: | 07 Nov 2024 09:27 |
| Last Modified: | 07 Nov 2024 09:27 |
| URI: | https://pred.uni-regensburg.de/id/eprint/52256 |
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