Atmospheric implication of the hydrogen bonding interaction in hydrated clusters of HONO and dimethylamine in the nighttime

2017 ◽  
Vol 19 (1) ◽  
pp. 65-77 ◽  
Author(s):  
Hailiang Zhao ◽  
Lin Du
Keyword(s):  
Hydrogen Bonding ◽  
Hydrogen Bonding Interaction ◽  
Bonding Interaction ◽  
Hydrated Clusters

The role of hydrogen bonding in the hydrated clusters of HONO and dimethylamine has been reported.

The essential role of hydrogen-bonding interaction in the extractive separation of phenolic compounds by ionic liquid

AIChE Journal ◽  
2012 ◽  
Vol 59 (5) ◽  
pp. 1657-1667 ◽  
Author(s):  
Qiwei Yang ◽  
Huabin Xing ◽  
Baogen Su ◽  
Zongbi Bao ◽  
Jun Wang ◽  
...  
Keyword(s):  
Ionic Liquid ◽  
Hydrogen Bonding ◽  
Phenolic Compounds ◽  
Essential Role ◽  
Hydrogen Bonding Interaction ◽  
Bonding Interaction ◽  
Extractive Separation

Radical Enzymes Control the Chemistry of Their Highly Reactive Intermediates Using the Quantum Coulombic Effect

2020 ◽  
Author(s):  
Hossein Khalilian ◽  
Gino A. DiLabio
Keyword(s):  
Hydrogen Bonding ◽  
Molecular Orbital ◽  
Reactive Intermediates ◽  
Hydrogen Bonding Interaction ◽  
Orbital Ordering ◽  
Dynamic Nature ◽  
Radical Intermediate ◽  
Highest Occupied Molecular Orbital ◽  
Bonding Interaction ◽  
Close Proximity

Here, we report an exquisite strategy that the B12 enzymes exploit to manipulate the reactivity of their radical intermediate (Adenosyl radical). Based on the quantum-mechanic calculations, these enzymes utilize a little known long-ranged through space quantum Coulombic effect (QCE). The QCE causes the radical to acquire an electronic structure that contradicts the Aufbau Principle: The singly-occupied molecular orbital (SOMO) is no longer the highest-occupied molecular orbital (HOMO) and the radical is unable to react with neighbouring substrates. The dynamic nature of the enzyme and its structure is expected to be such that the reactivity of the radical is not restored until it is moved into close proximity of the target substrate. We found that the hydrogen bonding interaction between the nearby conserved glutamate residue and the ribose ring of Adenosyl radical plays a crucial role in manipulating the orbital ordering

Radical Enzymes Control the Chemistry of Their Highly Reactive Intermediates Using the Quantum Coulombic Effect

2020 ◽  
Author(s):  
Hossein Khalilian ◽  
Gino A. DiLabio
Keyword(s):  
Hydrogen Bonding ◽  
Molecular Orbital ◽  
Reactive Intermediates ◽  
Hydrogen Bonding Interaction ◽  
Orbital Ordering ◽  
Dynamic Nature ◽  
Radical Intermediate ◽  
Highest Occupied Molecular Orbital ◽  
Bonding Interaction ◽  
Close Proximity

Here, we report an exquisite strategy that the B12 enzymes exploit to manipulate the reactivity of their radical intermediate (Adenosyl radical). Based on the quantum-mechanic calculations, these enzymes utilize a little known long-ranged through space quantum Coulombic effect (QCE). The QCE causes the radical to acquire an electronic structure that contradicts the Aufbau Principle: The singly-occupied molecular orbital (SOMO) is no longer the highest-occupied molecular orbital (HOMO) and the radical is unable to react with neighbouring substrates. The dynamic nature of the enzyme and its structure is expected to be such that the reactivity of the radical is not restored until it is moved into close proximity of the target substrate. We found that the hydrogen bonding interaction between the nearby conserved glutamate residue and the ribose ring of Adenosyl radical plays a crucial role in manipulating the orbital ordering

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