- P-ISSN 2233-4203
- E-ISSN 2093-8950
- P-ISSN2233-4203
- E-ISSN2093-8950
- ESCI, SCOPUS, KCI
Article Detail
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Structural Analysis of the Cu-binding Site in the [Cu·dCMP·dCMP-H]1− Complex
Mass Spectrometry Letters / Mass Spectrometry Letters, (P)2233-4203; (E)2093-8950
2013, v.4 no.4, pp.67-70
https://doi.org/10.5478/MSL.2013.4.4.67
(Kumoh National Institute of Technology)
(Kumoh National Institute of Technology)
(Kumoh National Institute of Technology)
Sang-Mi,
J., &
Ho-Tae,
K.
(2013). Structural Analysis of the Cu-binding Site in the [Cu·dCMP·dCMP-H]1− Complex. Mass Spectrometry Letters, 4(4), 67-70, https://doi.org/10.5478/MSL.2013.4.4.67
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Abstract
The Cu-binding site in the [Cu·dCMP·dCMP-H]1− complex was investigated. The tandem mass (MS/MS) spectra ofthe [Cu·dCMP·dCMP-H]1− parent ion showed [dCMP·Cu·H2PO4 + CONH]1− fragment ions. Therefore, we propose that the Cucation is simultaneously coordinated to the phosphate site and cytosine moiety in the stable geometry of the [Cu·dCMP·dCMPH]1− complex. Three geometries for the complex were considered in an attempt to optimize the structure of the[Cu·dCMP·dCMP-H]1− complex. The ab initio calculations were performed at the B3LYP/6-311G** level.
- keywords
- Dcmp, [Cu· dCMP·dCMP-H]1− complex, Mass spectrometry (MS), Tandem Mass Spectrometry (MS/MS)
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- Submission Date
- 2013-11-18
- Revised Date
- 2013-12-03
- Accepted Date
- 2013-12-04
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