Slowing of proton transport processes in the structure of bacterial reaction centers and bacteriorhodopsin in the presence of dipyridamole

Citation
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
Citations number
23
Categorie Soggetti
Biochemistry & Biophysics
Journal title
BIOCHEMISTRY-MOSCOW
ISSN journal
00062979 → ACNP
Volume
65
Issue
2
Year of publication
2000
Pages
213 - 217
Database
ISI
SICI code
0006-2979(200002)65:2<213:SOPTPI>2.0.ZU;2-3
Abstract
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.