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DC Field | Value | Language |
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dc.contributor.author | Louloudi, M. | en |
dc.contributor.author | Hadjiliadis, N. | en |
dc.date.accessioned | 2015-11-24T16:48:00Z | - |
dc.date.available | 2015-11-24T16:48:00Z | - |
dc.identifier.issn | 0010-8545 | - |
dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/9268 | - |
dc.rights | Default Licence | - |
dc.subject | nuclear-magnetic-resonance | en |
dc.subject | chloride hydrochloride trihydrate | en |
dc.subject | crystal-structure | en |
dc.subject | molecular-structure | en |
dc.subject | ion interactions | en |
dc.subject | coenzyme interactions | en |
dc.subject | aldehyde derivatives | en |
dc.subject | divalent-cations | en |
dc.subject | monohydrate | en |
dc.subject | pyrophosphate | en |
dc.title | Structural Aspects of Thiamine, Its Derivatives and Their Metal-Complexes in Relation to the Enzymatic Action of Thiamine Enzymes | en |
heal.type | journalArticle | - |
heal.type.en | Journal article | en |
heal.type.el | Άρθρο Περιοδικού | el |
heal.identifier.primary | Doi 10.1016/0010-8545(94)80074-X | - |
heal.identifier.secondary | <Go to ISI>://A1994PU57200012 | - |
heal.identifier.secondary | http://ac.els-cdn.com/001085459480074X/1-s2.0-001085459480074X-main.pdf?_tid=90759e4e-362e-11e3-923b-00000aacb35e&acdnat=1381906117_dd2d15578e29ebbd190246072547aa61 | - |
heal.language | en | - |
heal.access | campus | - |
heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Χημείας | el |
heal.publicationDate | 1994 | - |
heal.abstract | A review is given of the mechanism of the enzymatic action of thiamine (vitamin B-1) enzymes, based mainly on the metal complexes and the crystal structures of the ligand and its derivatives. It consists of three parts. Part 1 is a general introduction. Part 2 emphasizes the role of the pyrimidine and thiazole moities of thiamine and also of the pyrophosphate group and the bivalent metal ions in the enzymatic action, covered in four subsections referred to each of the above labels, the last of which describes the crystal structures of thiamine, its derivatives and their metal complexes. It attempts a correlation of the crystallographic data with the proposed mechanisms of the enzymatic action of thiamine. Part 3 is the conclusion, pointing to the stage of intervention of the metal ions and expanding the importance of the S conformation of the ligand during the enzymatic action of thiamine enzymes. | en |
heal.publisher | Elsevier | en |
heal.journalName | Coordination Chemistry Reviews | en |
heal.journalType | peer reviewed | - |
heal.fullTextAvailability | TRUE | - |
Appears in Collections: | Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά). ΧΗΜ |
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File | Description | Size | Format | |
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Louloudi-1994-Structural Aspects o.pdf | 2.23 MB | Adobe PDF | View/Open Request a copy |
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