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.