1.
Photosynth Res
; 39(2): 175-81, 1994 Feb.
Article
in English
| MEDLINE
| ID: mdl-24311069
ABSTRACT
The reduction by sulfide of exogenous ubiquinone is compared to the reduction of cytochromes in chromatophores of Rhodobacter capsulatus. From titrations with sulfide values for Vmax of 300 and 10 µmoles reduced/mg bacteriochlorophyll a·h, and for Km of 5 and 3 µM were estimated, for decyl-ubiquinone-and cytochrome c-reduction, respectively. Both reactions are sensitive to KCN, as has been found for sulfide-quinone reductase (SQR) in Oscillatoria limnetica, which is a flavoprotein. Effects of inhibitors interfering with quinone binding sites suggest that at least part of the electron transport from sulfide in R. capsulatus employs the cytochrome bc 1-complex via the ubiquinone pool.
2.
Nature
; 225(5237): 1056-8, 1970 Mar 14.
Article
in English
| MEDLINE
| ID: mdl-5416477