Redox-linked proton translocation by direct-coupled ligand conduction

1991 ◽  
Vol 23 (5) ◽  
pp. 703-714 ◽  
Author(s):  
Ian C. West
Keyword(s):  
Proton Translocation ◽  
Ligand Conduction

scholarly journals The site of attachment of retinal in bacteriorhodopsin. The epsilon-amino group in Lys-41 is not required for proton translocation.

1982 ◽  
Vol 257 (15) ◽  
pp. 8596-8599 ◽  
Author(s):  
K S Huang ◽  
M J Liao ◽  
C M Gupta ◽  
N Royal ◽  
K Biemann ◽  
...  
Keyword(s):  
Proton Translocation ◽  
Amino Group

scholarly journals Cryo-EM structure and dynamics of the green-light absorbing proteorhodopsin

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Stephan Hirschi ◽  
David Kalbermatter ◽  
Zöhre Ucurum ◽  
Thomas Lemmin ◽  
Dimitrios Fotiadis
Keyword(s):  
Proton Translocation ◽  
Functional Characterization ◽  
Green Light ◽  
Proton Donor ◽  
Molecular Organization ◽  
Primary Proton ◽  
Proton Pumps ◽  
Model Protein ◽  
Dynamics Simulations ◽  
And Function

AbstractThe green-light absorbing proteorhodopsin (GPR) is the archetype of bacterial light-driven proton pumps. Here, we present the 2.9 Å cryo-EM structure of pentameric GPR, resolving important residues of the proton translocation pathway and the oligomerization interface. Superposition with the structure of a close GPR homolog and molecular dynamics simulations reveal conformational variations, which regulate the solvent access to the intra- and extracellular half channels harbouring the primary proton donor E109 and the proposed proton release group E143. We provide a mechanism for the structural rearrangements allowing hydration of the intracellular half channel, which are triggered by changing the protonation state of E109. Functional characterization of selected mutants demonstrates the importance of the molecular organization around E109 and E143 for GPR activity. Furthermore, we present evidence that helices involved in the stabilization of the protomer interfaces serve as scaffolds for facilitating the motion of the other helices. Combined with the more constrained dynamics of the pentamer compared to the monomer, these observations illustrate the previously demonstrated functional significance of GPR oligomerization. Overall, this work provides molecular insights into the structure, dynamics and function of the proteorhodopsin family that will benefit the large scientific community employing GPR as a model protein.

scholarly journals A redirected proton pathway in the bacteriorhodopsin mutant Tyr-57–>Asp. Evidence for proton translocation without Schiff base deprotonation.

1994 ◽  
Vol 269 (46) ◽  
pp. 28851-28858
Author(s):  
S Sonar ◽  
T Marti ◽  
P Rath ◽  
W Fischer ◽  
M Coleman ◽  
...  
Keyword(s):  
Schiff Base ◽  
Proton Translocation
Sign in / Sign up

Export Citation Format

Share Document