Evidence for the Rate of the Final Step in the Bacteriorhodopsin Photocycle Being Controlled by the Proton Release Group:  R134H Mutant†

Biochemistry ◽  
2000 ◽  
Vol 39 (9) ◽  
pp. 2325-2331 ◽  
Author(s):  
Miao Lu ◽  
Sergei P. Balashov ◽  
Thomas G. Ebrey ◽  
Ning Chen ◽  
Yumei Chen ◽  
...  
Keyword(s):  
Proton Release ◽  
Release Group ◽  
Bacteriorhodopsin Photocycle

scholarly journals Structure Changes upon Deprotonation of the Proton Release Group in the Bacteriorhodopsin Photocycle

2012 ◽  
Vol 103 (3) ◽  
pp. 444-452 ◽  
Author(s):  
Joel E. Morgan ◽  
Ahmet S. Vakkasoglu ◽  
Janos K. Lanyi ◽  
Johan Lugtenburg ◽  
Robert B. Gennis ◽  
...  
Keyword(s):  
Proton Release ◽  
Structure Changes ◽  
Release Group ◽  
Bacteriorhodopsin Photocycle

The Proton Release Group of Bacteriorhodopsin Controls the Rate of the Final Step of Its Photocycle at Low pH†

Biochemistry ◽  
1999 ◽  
Vol 38 (7) ◽  
pp. 2026-2039 ◽  
Author(s):  
Sergei P. Balashov ◽  
Miao Lu ◽  
Eleonora S. Imasheva ◽  
Rajni Govindjee ◽  
Thomas G. Ebrey ◽  
...  
Keyword(s):  
Low Ph ◽  
Proton Release ◽  
Release Group

scholarly journals Structural Changes Due to the Deprotonation of the Proton Release Group in the M-Photointermediate of Bacteriorhodopsin as Revealed by Time-Resolved FTIR Spectroscopy†

Biochemistry ◽  
2008 ◽  
Vol 47 (44) ◽  
pp. 11598-11605 ◽  
Author(s):  
Joel E. Morgan ◽  
Ahmet S. Vakkasoglu ◽  
Johan Lugtenburg ◽  
Robert B. Gennis ◽  
Akio Maeda
Keyword(s):  
Ftir Spectroscopy ◽  
Structural Changes ◽  
Proton Release ◽  
Time Resolved ◽  
Release Group

scholarly journals Glutamic Acid 204 is the Terminal Proton Release Group at the Extracellular Surface of Bacteriorhodopsin

1995 ◽  
Vol 270 (45) ◽  
pp. 27122-27126 ◽  
Author(s):  
Leonid S. Brown ◽  
Jun Sasaki ◽  
Hideki Kandori ◽  
Akio Maeda ◽  
Richard Needleman ◽  
...  
Keyword(s):  
Glutamic Acid ◽  
Proton Release ◽  
Release Group

Effect of salt on the tyrosine and protonated Schiff base deprotonation kinetics in bacteriorhodopsin

1985 ◽  
Vol 63 (7) ◽  
pp. 1699-1704 ◽  
Author(s):  
Paul Dupuis ◽  
M. A. El-Sayed
Keyword(s):  
Schiff Base ◽  
Quantum Yield ◽  
Salt Concentration ◽  
Slow Component ◽  
High Salt ◽  
Proton Release ◽  
High Ph ◽  
Bacteriorhodopsin Photocycle

It is observed that the number of protons pumped per M412 formed in the bacteriorhodopsin photocycle almost doubles at high salt concentrations. In this paper, we studied the rates of deprotonation of tyrosine and of the two components of the protonated Schiff base at high salt concentrations, and at different pHs and temperatures. It is found that at pH = 7, increasing the salt concentration decreases the rates of deprotonation of the protonated Schiff base and tyrosine. This strongly suggests that the observed gain in the quantum yield of proton release per M412 formed when the salt concentration is increased is not a result of an increase in these rates. However, at high pH, e.g. 9.6, increasing the salt concentration increases the rate of deprotonation of the Schiff base by about 50%. Under all conditions, the slow component of the Schiff base is found to lose its proton prior to tyrosine.

Pathways of proton release in the bacteriorhodopsin photocycle

Biochemistry ◽  
1992 ◽  
Vol 31 (36) ◽  
pp. 8535-8543 ◽  
Author(s):  
Laszlo Zimanyi ◽  
Gyorgy Varo ◽  
Man Chang ◽  
Baofu Ni ◽  
Richard Needleman ◽  
...  
Keyword(s):  
Proton Release ◽  
Bacteriorhodopsin Photocycle

scholarly journals Relationship of proton release at the extracellular surface to deprotonation of the schiff base in the bacteriorhodopsin photocycle

1995 ◽  
Vol 68 (4) ◽  
pp. 1518-1530 ◽  
Author(s):  
Y. Cao ◽  
L.S. Brown ◽  
J. Sasaki ◽  
A. Maeda ◽  
R. Needleman ◽  
...  
Keyword(s):  
Schiff Base ◽  
Proton Release ◽  
Relationship Of ◽  
Bacteriorhodopsin Photocycle
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