The Qo-site inhibitor DBMIB favours the proximal position of the chloroplast Rieske protein and induces a pK-shift of the redox-linked proton.
Schoepp, B
The Qo-site inhibitor DBMIB favours the proximal position of the chloroplast Rieske protein and induces a pK-shift of the redox-linked proton. [electronic resource] - FEBS letters May 1999 - 245-50 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
0014-5793
10.1016/s0014-5793(99)00511-6 doi
Ascorbic Acid--metabolism
Binding Sites
Chloroplasts--metabolism
Cytochrome b Group--antagonists & inhibitors
Cytochrome b6f Complex
Dibromothymoquinone--metabolism
Electron Spin Resonance Spectroscopy
Electron Transport Complex III
Iron-Sulfur Proteins--antagonists & inhibitors
Oxidation-Reduction
Protons
The Qo-site inhibitor DBMIB favours the proximal position of the chloroplast Rieske protein and induces a pK-shift of the redox-linked proton. [electronic resource] - FEBS letters May 1999 - 245-50 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
0014-5793
10.1016/s0014-5793(99)00511-6 doi
Ascorbic Acid--metabolism
Binding Sites
Chloroplasts--metabolism
Cytochrome b Group--antagonists & inhibitors
Cytochrome b6f Complex
Dibromothymoquinone--metabolism
Electron Spin Resonance Spectroscopy
Electron Transport Complex III
Iron-Sulfur Proteins--antagonists & inhibitors
Oxidation-Reduction
Protons