pH Dependence of Anabaena Sensory Rhodopsin: Retinal Isomer Composition, Rate of Dark Adaptation, and Photochemistry

2014 ◽  
Vol 118 (30) ◽  
pp. 8995-9006 ◽  
Author(s):  
Rinat Rozin ◽  
Amir Wand ◽  
Kwang-Hwan Jung ◽  
Sanford Ruhman ◽  
Mordechai Sheves
Keyword(s):  
Dark Adaptation ◽  
Ph Dependence ◽  
Sensory Rhodopsin ◽  
Isomer Composition

Retinal Isomer Composition in Some Bacteriorhodopsin Mutants under Light and Dark Adaptation Conditions

1995 ◽  
Vol 99 (24) ◽  
pp. 10052-10055 ◽  
Author(s):  
Li Song ◽  
Difei Yang ◽  
M. A. El-Sayed ◽  
J. K. Lanyi
Keyword(s):  
Dark Adaptation ◽  
Isomer Composition

Dark-adaptation recovery after pulsed light.

1972 ◽  
Author(s):  
David J. Florip ◽  
Robert W. Bayer
Keyword(s):  
Dark Adaptation ◽  
Pulsed Light

Perceived brightness as a function of time of dark-adaptation

1966 ◽  
Author(s):  
Gosta Ekman ◽  
Jan Hosman ◽  
Ulf Berglund
Keyword(s):  
Dark Adaptation

Illumination Accelerates the Decay of the O-intermediate of pharaonis Phoborhodopsin (Sensory Rhodopsin II)¶

2002 ◽  
Vol 76 (4) ◽  
pp. 462 ◽  
Author(s):  
Masayuki Iwamoto ◽  
Yuki Sudo ◽  
Kazumi Shimono ◽  
Naoki Kamo
Keyword(s):  
Sensory Rhodopsin

Self-association of insulin. Its pH dependence and effect of plasma

Diabetes ◽  
1987 ◽  
Vol 36 (3) ◽  
pp. 261-264 ◽  
Author(s):  
E. Helmerhorst ◽  
G. B. Stokes
Keyword(s):  
Ph Dependence ◽  
Self Association

Rationalizing the pH-Activity Response for Escherichia Coli’s Glycinamide Ribonucleotidetransformylase Through Computational Methods

2019 ◽  
Author(s):  
Adrian Roitberg ◽  
Pancham Lal Gupta
Keyword(s):  
Transfer Reaction ◽  
Catalytic Mechanism ◽  
Ph Dependence ◽  
Ph Effects ◽  
Dependent Manner ◽  
E Coli ◽  
Gar Tfase ◽  
Activity Curve ◽  
Ph Dependent ◽  
Formyl Transfer

<div>Human Glycinamide ribonucleotide transformylase (GAR Tfase), a regulatory enzyme in the de novo purine biosynthesis pathway, has been established as an anti-cancer target. GAR Tfase catalyzes the formyl transfer reaction from the folate cofactor to the GAR ligand. In the present work, we study E. coli GAR Tfase, which has high sequence similarity with the human GAR Tfase with most functional residues conserved. E. coli GAR Tfase exhibits structural changes and the binding of ligands that varies with pH which leads to change the rate of the formyl transfer reaction in a pH-dependent manner. Thus, the inclusion of pH becomes essential for the study of its catalytic mechanism. Experimentally, the pH-dependence of the kinetic parameter kcat is measured to evaluate the pH-range of enzymatic activity. However, insufficient information about residues governing the pH-effects on the catalytic activity leads to ambiguous assignments of the general acid and base catalysts and consequently its catalytic mechanism. In the present work, we use pH-replica exchange molecular dynamics (pH-REMD) simulations to study the effects of pH on E. coli GAR Tfase enzyme. We identify the titratable residues governing the pH-dependent conformational changes in the system. Furthermore, we filter out the protonation states which are essential in maintaining the structural integrity, keeping the ligands bound and assisting the catalysis. We reproduce the experimental pH-activity curve by computing the population of key protonation states. Moreover, we provide a detailed description of residues governing the acidic and basic limbs of the pH-activity curve.</div>

A Study of the Normal Value of Dark Adaptation Time for Healthy Chinese Pilots

1989 ◽  
Author(s):  
Shihong Gao ◽  
Jialong Wu ◽  
Dongxian Hao ◽  
Changming Kang
Keyword(s):  
Dark Adaptation ◽  
Normal Value ◽  
Adaptation Time ◽  
Healthy Chinese

pH Dependence of the polarographic limiting currents of α-keto acids

1961 ◽  
Vol 26 (1) ◽  
pp. 141-155 ◽  
Author(s):  
S. Ono ◽  
M. Takagi ◽  
T. Wasa
Keyword(s):  
Ph Dependence ◽  
Keto Acids
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