The ability of actinic light to modify the proportion of fast and slow forms of the M intermediate (i.e., Mf and M(s)) in the bacteriorhodopsin (BR) photocycle is lost by exposure of the purple membrane (PM) to 0.05% Triton for 1-2 min. The decay path of Mf through the O intermediate is also lost, and new, much slower kinetic forms of M appear. In this brief exposure, the trimer structure for BR, as measured by circular dichroism (CD) exciton coupling and sedimentability, is unaffected. The optical properties of the treated PM are affected within seconds of exposure to the detergent as indicated by an increase in transmittance and a blue shift in the wavelength of maximum absorbance for the ground state. Different concentrations of Triton cause reproducibly different changes in the kinetics of the system. These observations support the view that the BR trimer-membrane interaction is important in controlling the BR photocycle.