Suppression of the back proton-transfer from Asp85 to the retinal Schiff base in bacteriorhodopsin: a theoretical analysis of structural elements.
作者： Ana-Nicoleta Bondar , Sándor Suhai , Stefan Fischer , Jeremy C. Smith , Marcus Elstner
DOI: 10.1016/J.JSB.2006.10.007
关键词:
摘要: The transfer of a proton from the retinal Schiff base to nearby Asp85 protein group is an essential step in directional proton-pumping by bacteriorhodopsin. To avoid wasteful back reprotonation Asp85, must ensure that, following deprotonation, energy barrier for proton-transfer larger than that Asp85. Here, three structural elements may contribute suppressing are investigated: (i) twisting; (ii) hydrogen-bonding distances active site; and (iii) number location internal water molecules. impact pattern bond twisting on deprotonation dissected performing extensive set quantum-mechanical calculations. Structural rearrangements site, such as changes Thr89:Asp85 distance relocation molecules acceptor group, participate mechanism which ensures proceeds with subsequent photocycle steps, not base.
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