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Bio-layer Interferometry for Measuring Kinetics of Protein-protein Interactions and Allosteric Ligand Effects
Published on: February 18, 2014
Theoretical study of cooperativity in biotin
Yi Lei1, Haoran Li, Rong Zhang
1Guangdong Institute for Drug Control, Guangzhou 510180, People's Republic of China.
The Journal of Physical Chemistry. B
|December 7, 2007
Summary
Hydrogen bonding cooperativities in biotin's ureido group are key to its catalytic mechanism. These interactions, involving sulfur and the side chain, enhance binding and reactivity.
Area of Science:
- Biochemistry
- Computational Chemistry
- Molecular Biology
Background:
- Biotin's catalytic mechanism is widely discussed but not fully understood.
- Hydrogen bonding (H-bonding) interactions with water are crucial for molecular function.
- Understanding biotin's structure-activity relationship is vital for biochemical applications.
Purpose of the Study:
- To investigate the catalytic mechanism of biotin through computational analysis.
- To explore the role of H-bonding between biotin model molecules and water.
- To elucidate the contributions of biotin's ureido group, sulfur atom, and side chain.
Main Methods:
- Ab initio calculations were performed on four representative biotin model molecules and their water aggregates.
- Molecular dynamics simulations were used for comparative analysis.
- Theoretical investigation of H-bonding cooperativities and electronic properties.
Main Results:
- Significant H-bonding cooperativities were demonstrated in biotin's ureido group.
- Pi-electron delocalization in the ureido group enhances H-bond covalent character and facilitates electrophilic substitution.
- Sulfur atom participates in the pi-electron system via sulfur-nitrogen bonding, reinforcing H-bonding cooperativities.
- Biotin's side chain sterically hinders accessibility but enhances H-bonding cooperativities through folding.
Conclusions:
- H-bonding cooperativities in the ureido group are a significant factor in biotin's catalytic activity.
- The interplay between the ureido group, sulfur, and side chain optimizes biotin's function.
- These cooperative H-bonding effects likely contribute to the strong and specific binding of biotin to streptavidin.
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