Abstract
Density functional theory calculations have been employed to study the interaction between the Zn2+ ion and some standard amino acid models. The highest affinities towards the Zn2+ ion are predicted for serine, cysteine, and histidine. Relatively high affinities are reported also for proline and glutamate/aspartate residues. It was found that the zinc complexes with cysteine adopt a tetrahedral conformation. Conversely, complexes with one or two histidine moieties remain in an octahedral geometry, while those with three or more histidine groups adopt a square-planar geometry.
Original language | English (US) |
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Pages (from-to) | 133-137 |
Number of pages | 5 |
Journal | Journal of Biological Inorganic Chemistry |
Volume | 13 |
Issue number | 1 |
DOIs | |
State | Published - 2008 |
Keywords
- Amino acids
- Density functional theory
- Enzymes
- Metallization
- Zinc
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry