A DFT study of the [Cu2+-(GlyGlyHis-3H(+))](-1) ion complex structure
- Authors
- Kim, Bo-Ra; Kim, Ho-Tae
- Issue Date
- 15-Nov-2008
- Publisher
- ELSEVIER SCIENCE BV
- Keywords
- Tripeptide; GlyGlyHis oligopeptide; Metal-peptide complex; Cu2+ ion; DFT calculation
- Citation
- JOURNAL OF MOLECULAR STRUCTURE-THEOCHEM, v.868, no.1-3, pp 109 - 112
- Pages
- 4
- Journal Title
- JOURNAL OF MOLECULAR STRUCTURE-THEOCHEM
- Volume
- 868
- Number
- 1-3
- Start Page
- 109
- End Page
- 112
- URI
- https://scholarworks.bwise.kr/kumoh/handle/2020.sw.kumoh/22267
- DOI
- 10.1016/j.theochem.2008.08.013
- ISSN
- 0166-1280
- Abstract
- Conformations of Cue(2+) ion binding to GlyGlyHis (GGH) tripeptide, a model compound for human serum albumin where the Cu2+ binding site is the N-terminal AspAlaHis, have been studied by many research groups. The specific interactions between GGH and Cu2+ ion, which is known to form a [Cu2+-(GlyGlyHis - 3H(+))](-1) planar structure in aqueous solution, are studied in terms of optimized structures and energies in B3LYP/6-311+G(d,p) calculations. Five geometries are tried to optimize the [Cu2+-(GlyGlyHis - 3H(+))](-1) planar structures. A Cu2+-NNNN planar structure involved the four coordination of a terminal amino nitrogen, two deprotonated amide nitrogens, and an imidazole-N3 atom at the deprotonated imidazole ring, has been calculated to be the most stable structure among the [Cu2+-(GlyGlyHis - 3H(+))](-1) complexes. The energy and geometry of the Cu2+-NNNO coordination structure involving a C-terminal carboxyl oxygen are also calculated to understand the NNNN-coordination preference of Cu2+ in the [Cu2+-(GlyGlyHis - 3H(+))](-1) complex. (C) 2008 Elsevier B.V. All rights reserved.
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