A Simple Method for Determining the Relative Strengths of Normal and Low-Barrier Hydrogen Bonds in Solution: Implications to Enzyme Catalysis

1995 ◽  
Vol 117 (48) ◽  
pp. 11902-11905 ◽  
Author(s):  
Benjamin Schwartz ◽  
Dale G. Drueckhammer
Keyword(s):  
Hydrogen Bonds ◽  
Enzyme Catalysis ◽  
Simple Method ◽  
Low Barrier Hydrogen Bonds

Response : On Low-Barrier Hydrogen Bonds and Enzyme Catalysis

Science ◽  
1995 ◽  
Vol 269 (5220) ◽  
pp. 104-106
Author(s):  
Perry A. Frey
Keyword(s):  
Hydrogen Bonds ◽  
Enzyme Catalysis ◽  
Low Barrier Hydrogen Bonds

scholarly journals On low-barrier hydrogen bonds and enzyme catalysis

Science ◽  
1995 ◽  
Vol 269 (5220) ◽  
pp. 102-106 ◽  
Author(s):  
A Warshel ◽  
A Papazyan ◽  
P. Kollman
Keyword(s):  
Hydrogen Bonds ◽  
Enzyme Catalysis ◽  
Low Barrier Hydrogen Bonds

scholarly journals Short hydrogen bonds in the catalytic mechanism of serine proteases

2008 ◽  
Vol 73 (4) ◽  
pp. 393-403 ◽  
Author(s):  
Vladimir Leskovac ◽  
Svetlana Trivic ◽  
Draginja Pericin ◽  
Mira Popovic ◽  
Julijan Kandrac
Keyword(s):  
Hydrogen Bond ◽  
Hydrogen Bonds ◽  
Active Site ◽  
Serine Proteases ◽  
Active Sites ◽  
Catalytic Mechanism ◽  
Data Bank ◽  
Ground State Structure ◽  
Low Barrier Hydrogen Bonds ◽  
Short Hydrogen Bonds

The survey of crystallographic data from the Protein Data Bank for 37 structures of trypsin and other serine proteases at a resolution of 0.78-1.28 ? revealed the presence of hydrogen bonds in the active site of the enzymes, which are formed between the catalytic histidine and aspartate residues and are on average 2.7 ? long. This is the typical bond length for normal hydrogen bonds. The geometric properties of the hydrogen bonds in the active site indicate that the H atom is not centered between the heteroatoms of the catalytic histidine and aspartate residues in the active site. Taken together, these findings exclude the possibility that short "low-barrier" hydrogen bonds are formed in the ground state structure of the active sites examined in this work. Some time ago, it was suggested by Cleland that the "low-barrier hydrogen bond" hypothesis is operative in the catalytic mechanism of serine proteases, and requires the presence of short hydrogen bonds around 2.4 ? long in the active site, with the H atom centered between the catalytic heteroatoms. The conclusions drawn from this work do not exclude the validity of the "low-barrier hydrogen bond" hypothesis at all, but they merely do not support it in this particular case, with this particular class of enzymes.

Low‐Barrier Hydrogen Bonds in Negative Thermal Expansion Material H 3 [Co(CN) 6 ]

2019 ◽  
Vol 25 (27) ◽  
pp. 6814-6822 ◽  
Author(s):  
Kasper Tolborg ◽  
Mads R. V. Jørgensen ◽  
Mattia Sist ◽  
Aref Mamakhel ◽  
Jacob Overgaard ◽  
...  
Keyword(s):  
Thermal Expansion ◽  
Hydrogen Bonds ◽  
Negative Thermal Expansion ◽  
Low Barrier Hydrogen Bonds

Low-Barrier Hydrogen Bonds

2013 ◽  
pp. 756-759
Author(s):  
P.A. Frey
Keyword(s):  
Hydrogen Bonds ◽  
Low Barrier Hydrogen Bonds

Characterization of Low-Barrier Hydrogen Bonds. 1. Microsolvation Effects. An ab Initio and DFT Investigation

1997 ◽  
Vol 119 (32) ◽  
pp. 7561-7566 ◽  
Author(s):  
Yongping Pan ◽  
Michael A. McAllister
Keyword(s):  
Hydrogen Bonds ◽  
Ab Initio ◽  
Low Barrier Hydrogen Bonds ◽  
Ab Initio And Dft
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