Deprotonation of D96 in bacteriorhodopsin opens the proton uptake pathway.
Deprotonation of D96 in bacteriorhodopsin opens the proton uptake pathway.
复制标题
细菌视紫红质中 D96 的去质子化打开质子摄取途径。
DOI：
10.1016/j.str.2012.12.018
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发表时间：
2013
期刊：
影响因子：
--
通讯作者：
Facciotti,MarcT
中科院分区：
文献类型：
--
作者：
Wang,Ting;Sessions,AylaO;Lunde,ChristopherS;Rouhani,Shahab;Glaeser,RobertM;Duan,Yong;Facciotti,MarcT
Despite extensive investigation, the precise mechanism controlling the opening of the cytoplasmic proton uptake pathway in bacteriorhodopsin (bR) has remained a mystery. From an analysis of the X-ray structure of the D96G/F171C/F219L triple mutant of bR and 60 independent molecular dynamics simulations of bR photointermediates, we report that the deprotonation of D96, a key residue in proton transfer reactions, serves two roles that occur sequentially. First, D96 donates a proton to the Schiff base. Subsequently, the deprotonation of D96 serves to "unlatch" the cytoplasmic side. The latching function of D96 appears to be remarkably robust, functioning to open hydration channels in all photointermediate structures. These results suggest that the protonation state of D96 may be the critical biophysical cue controlling the opening and closing of the cytoplasmic half-channel in bR. We suspect that this protonation-switch mechanism could also be utilized in other proton pumps to minimize backflow and reinforce directionality.
