Schoepp, Barbara and Brugna, Myriam and Riedel, Astrid and Nitschke, Wolfgang and Kramer, David M. (1999) The Q(o)-site inhibitor DBMIB favours the proximal position of the chloroplast Rieske protein and induces a pK-shift of the redox-linked proton. FEBS LETTERS, 450 (3). pp. 245-250. ISSN 1873-3468,
Full text not available from this repository. (Request a copy)Abstract
The interaction of the inhibitor 2,5-dibromo-3-methyl-6-isopropylbenzoquinone (DBMIB) with the Rieske protein of the chloroplast b(6)f complex has been studied by EPR, All three redox: states of DBMIB were found to interact with the iron-sulphur cluster. The presence of the oxidised form of DBMIB altered the equilibrium distribution of the Rieske protein's conformational substates, strongly favouring the proximal position close to heme DL, In addition to this conformational effect, DBMIB shifted the pK-value of the redox-linked proton involved in the iron-sulphur cluster's redox transition by about 1.5 pH units towards more acidic values. The implications of these results with respect to the interaction of the native quinone substrate and the Rieske cluster in cytochrome be complexes are discussed. (C) 1999 Federation of European Biochemical Societies.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | CYTOCHROME BC(1) COMPLEX; IRON-SULFUR CLUSTERS; RHODOPSEUDOMONAS-SPHAEROIDES; QUINOL OXIDATION; 2FE-2S CLUSTER; MAGNETIC AXES; ORIENTATION; MEMBRANE; BINDING; SITE; Rieske; DBMIB; redox-linked proton; Rieske protein's domain movement; EPR |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 14 Feb 2023 15:07 |
| Last Modified: | 14 Feb 2023 15:07 |
| URI: | https://pred.uni-regensburg.de/id/eprint/49249 |
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