A structural investigation of cytochrome c binding to photosynthetic reaction centers in reconstituted membranes

Abstract

Mammalian cytochrome c can effectively replace bacterial cytochrome c2 as the electron donor to the bacterial photosynthetic reaction center in either the natural chromatophore or a reconstituted reaction center/phospholipid membrane. In this paper, the reconstituted membrane was used to describe the nature of cytochrome c binding to the reaction center, the location of bound cytochrome c in the membrane profile and the perturbation of the reaction center and phospholipid profile structures indicated by cytochrome c binding. These structural studies utilized the combined techniques of X-ray and neutron diffraction.