[Molecular organization of the long-wave complexes of purple photosynthesizing bacteria. Effect of pronase on the B890 complex of Chromatium minutissium and Rhodopseudomonas palustris].

The pronase action on the long-wave complexes B890 from two different purple bacteria has been investigated. Differences in the kinetics of decrease of the reaction center photochemical activity of electron-donor activity of cytochromes and of destruction of Bx890 (875) forms have been discovered. Different rates of the proteolysis of RC proteins were revealed by SDS-gel-electrophoresis. The heavy protein of RC was the first to degrade. The photochemical transformations deltaA890(875) in B890 complexes was observed during formation of peptides with molecular weight about 17 000 from two other RC proteins. On the basis of obtained data the model of molecular organization of B890 complexes from purple bacteria is discussed.