On the mechanism of action of thiamin enzymes, crystal structure of 2-(alpha-hydroxyethyl)thiamin pyrophosphate (HETPP). Complexes of HETPP with zinc(II) and cadmium(II)
| dc.contributor.author | Malandrinos, G. | en |
| dc.contributor.author | Louloudi, M. | en |
| dc.contributor.author | Mitsopoulou, C. A. | en |
| dc.contributor.author | Butler, I. S. | en |
| dc.contributor.author | Bau, R. | en |
| dc.contributor.author | Hadjiliadis, N. | en |
| dc.date.accessioned | 2015-11-24T16:43:13Z | |
| dc.date.available | 2015-11-24T16:43:13Z | |
| dc.identifier.issn | 0949-8257 | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/8668 | |
| dc.rights | Default Licence | - |
| dc.subject | thiamin | en |
| dc.subject | thiamin metal complexes | en |
| dc.subject | spectroscopic characterization | en |
| dc.subject | thiamin catalysis | en |
| dc.subject | diphosphate dependent enzyme | en |
| dc.subject | transketolase | en |
| dc.subject | resolution | en |
| dc.subject | hydrochloride | en |
| dc.subject | spectroscopy | en |
| dc.subject | vitamin-b-1 | en |
| dc.subject | derivatives | en |
| dc.subject | chloride | en |
| dc.subject | zn2+ | en |
| dc.subject | cd2+ | en |
| dc.title | On the mechanism of action of thiamin enzymes, crystal structure of 2-(alpha-hydroxyethyl)thiamin pyrophosphate (HETPP). Complexes of HETPP with zinc(II) and cadmium(II) | en |
| heal.abstract | The crystal structure of the 2-(alpha-hydroxethyl) thiamin pyrophosphate (LH2) was solved by X-ray diffraction. Crystallographic data: space group F2dd, a = 7.922(4) Angstrom, b = 33.11(2) Angstrom, c = 36.232(10) Angstrom, V = 9503(9) Angstrom(3), z = 16. Metal complexes of the general formula K-2{[M(LH)Cl-2](2)} (M = Zn2+, Cd2+) were isolated from methanolic solutions and characterized by elemental analysis, IR, Raman, and C-13 CP MAS NMR spectra. They were also characterized by C-13 NMR, P-31 NMR, Cd-113 NMR, ES-MS, and H-1 NMR ROESY spectra in D2O solutions. The data provide evidence for the bonding of the metals to the N(1') atom of the pyrimidine ring and to the pyrophosphate group. The free ligand and the metal-coordinated ligand adopt the S conformation. Since thiamin cofactor, substrate, and metal ions are present in our system, the extracted results directly refer to thiamin catalysis and possible functional implications are correlated and discussed. | en |
| heal.access | campus | - |
| heal.fullTextAvailability | TRUE | - |
| heal.identifier.primary | DOI 10.1007/s007750050253 | - |
| heal.identifier.secondary | <Go to ISI>://000076617900001 | - |
| heal.identifier.secondary | http://download.springer.com/static/pdf/41/art%253A10.1007%252Fs007750050253.pdf?auth66=1382078775_06f477b5d7e7fa4b84148895f51c5be6&ext=.pdf | - |
| heal.journalName | Journal of Biological Inorganic Chemistry | en |
| heal.journalType | peer reviewed | - |
| heal.language | en | - |
| heal.publicationDate | 1998 | - |
| heal.publisher | Springer Verlag (Germany) | en |
| heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας | el |
| heal.type | journalArticle | - |
| heal.type.el | Άρθρο Περιοδικού | el |
| heal.type.en | Journal article | en |
Αρχεία
Φάκελος/Πακέτο αδειών
1 - 1 of 1
Φόρτωση...
- Ονομα:
- license.txt
- Μέγεθος:
- 1.74 KB
- Μορφότυπο:
- Item-specific license agreed upon to submission
- Περιγραφή: