Isolation, Characterization, and Comparison of a Ubiquitous Pigment-Protein Complex Consisting of a Reaction Center and Light-Harvesting Bacteriochlorophyll Proteins Present in Purple Photosynthetic Bacteria1

1985 ◽  
Vol 98 (6) ◽  
pp. 1487-1498 ◽  
Author(s):  
Tetsuya UEDA ◽  
Yukio MORIMOTO ◽  
Mamoru SATO ◽  
Tomisaburo KAKUNO ◽  
Jinpei YAMASHITA ◽  
...  
Keyword(s):  
Reaction Center ◽  
Protein Complex ◽  
Light Harvesting ◽  
Pigment Protein Complex

scholarly journals Analysis of the Light-harvesting Pigment-Protein Complex of Wild Type and a Chlorophyll-b-less Mutant of Barley

1979 ◽  
Vol 63 (2) ◽  
pp. 237-243 ◽  
Author(s):  
John J. Burke ◽  
Katherine E. Steinback ◽  
Charles J. Arntzen
Keyword(s):  
Protein Complex ◽  
Light Harvesting ◽  
Chlorophyll B ◽  
Wild Type ◽  
Pigment Protein Complex

Characterization of Reaction Center-B875 Complex of Rhodocyclus gelatinosus: QB Site Properties Derived from Reconstitution Experiments

1991 ◽  
Vol 46 (1-2) ◽  
pp. 99-105 ◽  
Author(s):  
I. Agalidis ◽  
E. Rivas ◽  
F. Reiss-Husson
Keyword(s):  
Reaction Center ◽  
Protein Complex ◽  
Electron Acceptors ◽  
Rhodocyclus Gelatinosus ◽  
Pigment Protein Complex ◽  
Ubiquinone Binding ◽  
Dodecyl Ether ◽  
Particle Weight

Abstract Purified reaction center-B875 pigment-protein complex isolated from Rc. gelatinosus (I. Agalidis, E. Rivas, and F. Reiss-Husson, Photosynth. Res. 23, 249 - 255 (1990)) was further characterized. In the chromatophores, the quinone content was shown to be 6 menaquinones 8 and 16 ubiquinones 8 per reaction center, indicating that the pool contained both quinone types. Besides the primary (MK8) and secondary (UQ8 ) electron acceptors of the reaction cen­ter, the complex contains residual quinones from the membrane pool (about 3 MK8 and 5 UQ8) probably associated with the phospholipids. Apparent particle weight of the complex including bound detergent was 520 ± 46 kDa. The secondary quinone QB was partially removed from the RC by treatment with 2 -3 % octaethyleneglycol dodecyl ether and 3 -4 mᴍ orthophenanthroline. Reconstitution experi­ments showed that UQ6, UQ9 and UQ10 could replace QB but that MK8 and MK9 could not. It was concluded that QB site has a clear specificity towards ubiquinone binding.

Sign in / Sign up

Export Citation Format

Share Document