Construction of Unsymmetrical Bis‐Urea Macrocyclic Host for Neutral Molecule and Chloride Ion Binding

Author(s):  
Biprajit Paul ◽  
Ayan Mukherjee ◽  
Deepak Bhuyan ◽  
Samit Guha
2020 ◽  
Vol 10 (20) ◽  
pp. 7027-7033
Author(s):  
Surbhi Grewal ◽  
Saonli Roy ◽  
Himanshu Kumar ◽  
Mayank Saraswat ◽  
Naimat K. Bari ◽  
...  

A proof-of-concept on temporal control in the tritylation reactions has been demonstrated using a designed tripodal triazole-linked azo(hetero)arene-based photoswitchable catalyst.


2018 ◽  
Vol 20 (5) ◽  
pp. 3381-3387 ◽  
Author(s):  
Kota Katayama ◽  
Yuji Furutani ◽  
Masayo Iwaki ◽  
Tetsuya Fukuda ◽  
Hiroo Imai ◽  
...  

ATR-FTIR spectroscopic study elucidates the novel role of Cl−-binding in primate long-wavelength-sensitive (LWS) visual pigment.


2013 ◽  
Vol 67 (1) ◽  
pp. 137-143 ◽  
Author(s):  
Kiyofumi KURUMISAWA ◽  
Yuto MURAKAMI ◽  
Kunihiko ISHIGAKI ◽  
Toyoharu NAWA

1999 ◽  
Vol 76 (4) ◽  
pp. 1951-1958 ◽  
Author(s):  
Lóránd Kelemen ◽  
Péter Galajda ◽  
Sándor Száraz ◽  
Pál Ormos

2009 ◽  
Vol 392 (1) ◽  
pp. 48-62 ◽  
Author(s):  
Daisuke Suzuki ◽  
Yuji Furutani ◽  
Keiichi Inoue ◽  
Takashi Kikukawa ◽  
Makoto Sakai ◽  
...  

2017 ◽  
Author(s):  
Asghar M. Razavi ◽  
Lucie Delemotte ◽  
Joshua R. Berlin ◽  
Vincenzo Carnevale ◽  
Vincent A. Voelz

AbstractNa+/K+-ATPase transports Na+and K+ions across the cell membrane via an ion binding site made alternatively accessible to the intra- and extracellular milieu by conformational transitions that confer marked changes in ion binding stoichiometry and selectivity. To probe the mechanism of these changes, we used molecular simulation approaches to identify the protonation state of Na+and K+coordinating residues in E1P and E2P conformations. Further analysis of these simulations revealed a novel molecular mechanism responsible for the change in protonation state: the conformation-dependent binding of an anion (a chloride ion in our simulations) to a previously unrecognized cytoplasmic site in the loop between transmembrane helices 8 and 9, which influences the electrostatic potential of the crucial Na+-coordinating residue D926. This mechanistic model is consistent with experimental observations and provides a molecular-level picture of how E1P to E2P enzyme conformational transitions are coupled to changes in ion binding stoichiometry and selectivity.


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