Proton Transport by Proteorhodopsin Requires that the Retinal Schiff Base Counterion Asp-97 Be Anionic†

Biochemistry ◽  
2003 ◽  
Vol 42 (21) ◽  
pp. 6582-6587 ◽  
Author(s):  
Andrei K. Dioumaev ◽  
Jennifer M. Wang ◽  
Zoltán Bálint ◽  
György Váró ◽  
Janos K. Lanyi
Keyword(s):  
Schiff Base ◽  
Proton Transport

scholarly journals 1P248 One-way proton transport in bacteriorhodopsin is modulated by changes in the interaction of the Schiff base with water molecules

2004 ◽  
Vol 44 (supplement) ◽  
pp. S91
Author(s):  
A. Maeda ◽  
Robert B. Gennis ◽  
Sersei P. Balashov ◽  
Thomas G. Ebrey
Keyword(s):  
Schiff Base ◽  
Proton Transport ◽  
Water Molecules

scholarly journals Proton transport by a bacteriorhodopsin mutant, aspartic acid-85-->asparagine, initiated in the unprotonated Schiff base state.

1995 ◽  
Vol 92 (25) ◽  
pp. 11519-11523 ◽  
Author(s):  
S. Dickopf ◽  
U. Alexiev ◽  
M. P. Krebs ◽  
H. Otto ◽  
R. Mollaaghababa ◽  
...  
Keyword(s):  
Schiff Base ◽  
Aspartic Acid ◽  
Proton Transport

Electron crystallographic studies on E.coli - expressed variants of bacteriorhodopsin

1992 ◽  
Vol 50 (1) ◽  
pp. 436-437
Author(s):  
Alok K Mitra ◽  
Larry J. W. Miercke ◽  
Mary C. Betlach ◽  
Richard F. Shand ◽  
Robert M. Stroud
Keyword(s):  
Schiff Base ◽  
Membrane Protein ◽  
Proton Pump ◽  
Proton Transport ◽  
Integral Membrane Protein ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Halobacterium Halobium ◽  
Proton Release ◽  
Extracellular Side

Bacterorhodopsin (BR) is an integral membrane protein present in the purple membrane (PM) of Halobacterium halobium where it is arranged in a highly ordered 2-dimensional hexagonal P3 lattice. BR contains a single retinylidene chromophore bound via a protonated Schiff base to Lys-216 and functions as a light-driven proton pump. Upon absorption of a photon, BR cycles through a series of photointermediates resulting in a vectorial pumping of a proton from the intracellular side to the extracellular side. Site-directed mutagenesis has identified residues whose substitution affects the chromophore environment in BR and those that are involved in the proton transport. Specifically Asp-85, Asp-212, and Arg-82 are involved in the proton release pathway, whereas Asp-96 is involved in Schiff base reprotonation.

Spin-crossover in an iron(iii) complex showing a broad thermal hysteresis

2021 ◽  
Author(s):  
Cyril Rajnák ◽  
Romana Mičová ◽  
Ján Moncoľ ◽  
Ľubor Dlháň ◽  
Christoph Krüger ◽  
...  
Keyword(s):  
Schiff Base ◽  
Schiff Base Ligand ◽  
Spin Crossover ◽  
Thermal Hysteresis ◽  
Mononuclear Complex ◽  
Hysteresis Width ◽  
Thermally Induced

A pentadentate Schiff-base ligand 3,5Cl-L2− and NCSe− form a iron(iii) mononuclear complex [Fe(3,5Cl-L)(NCSe)], which shows a thermally induced spin crossover with a broad hysteresis width of 24 K between 123 K (warming) and 99 K (cooling).

Effects of pH on proton transport by vacuolar pumps from maize roots

1992 ◽  
Vol 86 (1) ◽  
pp. 63-70 ◽  
Author(s):  
David Brauer ◽  
DeNea Conner ◽  
Shu-I Tu
Keyword(s):  
Proton Transport ◽  
Maize Roots ◽  
Effects Of Ph
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