Please use this identifier to cite or link to this item: http://ktisis.cut.ac.cy/handle/10488/9378
Title: Detection of functional hydrogen-bonded water molecules with protonated/deprotonated key carboxyl side chains in the respiratory enzyme ba3-oxidoreductase
Authors: Nicolaides, Antonis 
Soulimane, Tewfik 
Varotsis, Constantinos 
Keywords: Water;Copper;Heme;Hydrogen Bonding;Kinetics
Category: Earth and Related Environmental Sciences
Field: Natural Sciences
Issue Date: 28-Mar-2015
Publisher: Royal Society of Chemistry
Source: Physical Chemistry Chemical Physics Volume 17, Issue 12, 28 March 2015, Pages 8113-8119
metadata.dc.doi: 10.1039/c5cp00043b
Abstract: The protonation/deprotonation of active carboxyl side chains by water networks forming the proton loading and exit sites in proteins are important steps in protein catalysis. An excellent system to study such basic principles is the heme-copper ba3 from T. thermophilus because it utilizes one proton input channel and it delivers protons to the active site for both O2 chemistry and proton pumping. We report the interaction of the heme a3 Fe propionate-A and the Asp372-His376 pair which forms the valve for the exit pathway for the protons with internal water molecules in ba3 oxidoreductase by light minus dark FTIR spectroscopy in conjunction with H2O/H218O/D2O exchange. The proton loading site consists of several water molecules including w941/w946 which are H-bonded to propionate-A-H+, acting as the Zundel cation. The detection of two H218O sensitive bands at 3640 and 3634 cm-1 shows the existence of weakly H-bonded water molecules. This journal is
URI: http://ktisis.cut.ac.cy/handle/10488/9378
ISSN: 14639076
Rights: © the Owner Societies.
Type: Article
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