Photochemical electron transfer reactions in the acceptor complex of reaction centers of Rhodopseudomonas spheroides treated with sodium dodecyl sulfate.

We have compared some photochemical properties of the reaction-center complex of Rhodopseudomonas spheroides (wild-type) treated with various amounts of either sodium dodecyl sulfate (SDS) or dodecyl dimethylamine N-oxide. In the presence of the latter, the native structure and activity of the reaction center are preserved even at high concentrations of detergent. In contrast, SDS denatures the protein. It does this by a cooperative process, as shown by the sigmoidal relationship between primary photochemical activity and SDS concentration. SDS binds to the reaction center at up to about 6 g SDS/g protein. The most notable modifications brought about by low SDS concentrations are: a slowing down of rereduction of P+ by Q-B from 1 s-1 to 0.25 s-1 and, to a lesser extent, of P+ by Q-A; the reoxidation of Q-A and Q-B by N,N,N',N'-tetramethyl-1,4-phenylenediamine is accelerated as an exponential function of SDS concentration. In this case Q-A become more accessible to external acceptors but not Q-B. It is thought that these changes are mainly due to progressive binding of SDS resulting in the unfolding of the protein, probably accompanied by the loss of the metal. Herbicides partly protect the reaction center against SDS denaturation, but their efficiency to block electron transfer between QA and QB is greatly reduced in the altered reaction centers present in the transition region of the denaturation curve. It is concluded that in the early region of the SDS denaturation curve, no dissociation of the reaction center in subunits occurs. In the transition region, it appears that the reaction center reaches the critical state in which mainly dissociation of polypeptide H from the complex of chains L and M and loss of QA take place.