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When the retinal moiety in the rhodopsin molecule absorbs a photon, its configuration changes from the 11-cis isomer to all-trans retinal; this change then triggers a series of alterations in the protein component of the molecule. The changes lead, in turn, to the activation of an intracellular messenger called transducin, which activates a phosphodiesterase that hydrolyzes cGMP. All of these events take place within the disk membrane. The hydrolysis by phosphodiesterase at the disk membrane lowers the concentration of cGMP throughout the outer segment, and thus reduces the number of cGMP molecules that are available for binding to the channels in the surface of the outer segment membrane, leading to channel closure.