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https://olympias.lib.uoi.gr/jspui/handle/123456789/7620Full metadata record
| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Sanakis, Y. | en |
| dc.contributor.author | Mamma, D. | en |
| dc.contributor.author | Christakopoulos, P. | en |
| dc.contributor.author | Stamatis, H. | en |
| dc.date.accessioned | 2015-11-24T16:33:08Z | - |
| dc.date.available | 2015-11-24T16:33:08Z | - |
| dc.identifier.issn | 0141-8130 | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/7620 | - |
| dc.rights | Default Licence | - |
| dc.subject | catechol dioxygenase | en |
| dc.subject | epr | en |
| dc.subject | organic solvent | en |
| dc.subject | nonheme iron enzymes | en |
| dc.subject | secondary structure | en |
| dc.subject | arvilla c-1 | en |
| dc.subject | purification | en |
| dc.subject | dioxygenases | en |
| dc.subject | pyrocatechase | en |
| dc.subject | activation | en |
| dc.subject | oxygenases | en |
| dc.subject | proteins | en |
| dc.title | Catechol 1,2-dioxygenase from Pseudomonas putida in organic media-an electron paramagnetic resonance study | en |
| heal.type | journalArticle | - |
| heal.type.en | Journal article | en |
| heal.type.el | Άρθρο Περιοδικού | el |
| heal.identifier.primary | Doi 10.1016/S0141-8130(03)00073-4 | - |
| heal.identifier.secondary | <Go to ISI>://000186835800015 | - |
| heal.identifier.secondary | http://ac.els-cdn.com/S0141813003000734/1-s2.0-S0141813003000734-main.pdf?_tid=a2edf05bb698c0ca56497d7a3fe67761&acdnat=1335510356_ca5729f65196293dfbb5edcb3a729074 | - |
| heal.language | en | - |
| heal.access | campus | - |
| heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών και Τεχνολογιών. Τμήμα Βιολογικών Εφαρμογών και Τεχνολογιών | el |
| heal.publicationDate | 2003 | - |
| heal.abstract | The ability of an isolated isozyme of catechol 1,2-dioxygenase from Pseudomonas putida DSM 437 to function in a non-aqueous environment was investigated. The lyophilized enzyme is able to keep its catalytic function catalyzing the oxidation of catechol in n-hexane. Electron paramagnetic resonance (EPR) spectroscopy at liquid helium temperatures was applied to compare the properties of the non-heme iron of the enzyme in the organic solvent and in the aqueous solution. The catalytic performance of the enzyme in the organic solvent is correlated with the spectroscopic properties of the non-heme iron. (C) 2003 Elsevier B.V. All rights reserved. | en |
| heal.journalName | Int J Biol Macromol | en |
| heal.journalType | peer reviewed | - |
| heal.fullTextAvailability | TRUE | - |
| Appears in Collections: | Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά) | |
Files in This Item:
| File | Description | Size | Format | |
|---|---|---|---|---|
| Sanakis-2003-Catechol 1,2-dioxyge.pdf | 163.45 kB | Adobe PDF | View/Open Request a copy |
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