Pp. Knox et al., Slowing of proton transport processes in the structure of bacterial reaction centers and bacteriorhodopsin in the presence of dipyridamole, BIOCHEM-MOS, 65(2), 2000, pp. 213-217
Dipyridamole, 2,6-bis(diethanolamino)-4,8-dipiperidinopyrimido, is employed
in clinical practice as a vasodilator. It can also inhibit a specific memb
rane protein (glycoprotein P) which pumps anticancer drugs out of tumor cel
ls. Dipyridamole (10(-4) M) markedly slows down the kinetics of the electro
genic phase of the photoelectric response in Rhodobacter sphaeroides chroma
tophores. This phase is due to proton transfer from the external medium to
the secondary quinone acceptor in the reaction center. In purple membranes
of bacterium Halobacterium salinarium containing bacteriorhodopsin dipyrida
mole (in its charged state) significantly slowed the kinetics of proton tra
nsfer from the primary donor, Asp-96 (in membranes from bacteria of wild ty
pe), or from the external medium (in D96N mutant) to the Schiff base. It is
suggested that dipyridamole can influence the structural-dynamic state of
membrane proteins including modification of the structure of their hydrogen
bonds involved in proton-transport processes.