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https://olympias.lib.uoi.gr/jspui/handle/123456789/8667Full metadata record
| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Malandrinos, G. | en |
| dc.contributor.author | Dodi, K. | en |
| dc.contributor.author | Louloudi, M. | en |
| dc.contributor.author | Hadjiliadis, N. | en |
| dc.date.accessioned | 2015-11-24T16:43:12Z | - |
| dc.date.available | 2015-11-24T16:43:12Z | - |
| dc.identifier.issn | 0162-0134 | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/8667 | - |
| dc.rights | Default Licence | - |
| dc.subject | thiamin enzymes | en |
| dc.subject | bivalent metal ions | en |
| dc.subject | diphosphate dependent enzyme | en |
| dc.subject | crystal-structure | en |
| dc.subject | chloride hydrochloride | en |
| dc.subject | aldehyde derivatives | en |
| dc.subject | angstrom resolution | en |
| dc.subject | complexes | en |
| dc.subject | catalysis | en |
| dc.subject | 2-(alpha-hydroxybenzyl)thiamine | en |
| dc.subject | stereochemistry | en |
| dc.subject | decarboxylase | en |
| dc.title | On the mechanism of action of thiamin enzymes in the presence of bivalent metal ions | en |
| heal.type | journalArticle | - |
| heal.type.en | Journal article | en |
| heal.type.el | Άρθρο Περιοδικού | el |
| heal.identifier.primary | Doi 10.1016/S0162-0134(99)00178-6 | - |
| heal.identifier.secondary | <Go to ISI>://000086988500005 | - |
| heal.identifier.secondary | http://ac.els-cdn.com/S0162013499001786/1-s2.0-S0162013499001786-main.pdf?_tid=846052ae7bff31621e18400b587fad19&acdnat=1333034404_2dfc9e9c0c1e9995369c7fdf1de4bd91 | - |
| heal.language | en | - |
| heal.access | campus | - |
| heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας | el |
| heal.publicationDate | 2000 | - |
| heal.abstract | Results on the interactions between the bivalent metal ions Zn2+, Cd2+, Hg2+, Co2+, Ni-2 and 'active aldehyde' thiamin derivatives are reviewed. The techniques used in these studies include spectroscopic methods, i.e., IR-Raman, UV-Vis, multidimensional and multinuclear NMR in solution and in solid state, and X-ray crystal structure determinations. More recently, potentiometric studies on thiamin pyrophosphate and 2-(alpha-hydroxyethyl)thiamin in combination with NMR and EPR techniques were also undertaken. All these studies lead to useful conclusions on the mechanism of action of thiamin enzymes in the presence of bivalent metal ions. (C) 2000 EIsevier Science Inc. All rights reserved. | en |
| heal.publisher | Elsevier | en |
| heal.journalName | J Inorg Biochem | en |
| heal.journalType | peer reviewed | - |
| heal.fullTextAvailability | TRUE | - |
| Appears in Collections: | Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά). ΧΗΜ | |
Files in This Item:
| File | Description | Size | Format | |
|---|---|---|---|---|
| Malandrinos-2000-On the mechanism of.pdf | 141.92 kB | Adobe PDF | View/Open Request a copy |
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