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 |
2014-03-01T01:18:45Z |
|
dc.date.available |
2014-03-01T01:18:45Z |
|
dc.date.issued |
2003 |
en |
dc.identifier.issn |
0141-8130 |
en |
dc.identifier.uri |
https://dspace.lib.ntua.gr/xmlui/handle/123456789/15174 |
|
dc.subject |
Catechol dioxygenase |
en |
dc.subject |
EPR |
en |
dc.subject |
Organic solvent |
en |
dc.subject.classification |
Biochemistry & Molecular Biology |
en |
dc.subject.other |
catechol 1,2 dioxygenase |
en |
dc.subject.other |
helium |
en |
dc.subject.other |
hexane |
en |
dc.subject.other |
aqueous solution |
en |
dc.subject.other |
article |
en |
dc.subject.other |
catalysis |
en |
dc.subject.other |
electron spin resonance |
en |
dc.subject.other |
enzyme activity |
en |
dc.subject.other |
freeze drying |
en |
dc.subject.other |
oxidation |
en |
dc.subject.other |
Pseudomonas putida |
en |
dc.subject.other |
temperature sensitivity |
en |
dc.subject.other |
Catechol 1,2-Dioxygenase |
en |
dc.subject.other |
Dioxygenases |
en |
dc.subject.other |
Electron Spin Resonance Spectroscopy |
en |
dc.subject.other |
Freeze Drying |
en |
dc.subject.other |
Hexanes |
en |
dc.subject.other |
Iron |
en |
dc.subject.other |
Oxygenases |
en |
dc.subject.other |
Pseudomonas putida |
en |
dc.subject.other |
Solutions |
en |
dc.subject.other |
Pseudomonas |
en |
dc.subject.other |
Pseudomonas putida |
en |
dc.title |
Catechol 1,2-dioxygenase from Pseudomonas putida in organic media - An electron paramagnetic resonance study |
en |
heal.type |
journalArticle |
en |
heal.identifier.primary |
10.1016/S0141-8130(03)00073-4 |
en |
heal.identifier.secondary |
http://dx.doi.org/10.1016/S0141-8130(03)00073-4 |
en |
heal.language |
English |
en |
heal.publicationDate |
2003 |
en |
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.publisher |
ELSEVIER SCIENCE BV |
en |
heal.journalName |
International Journal of Biological Macromolecules |
en |
dc.identifier.doi |
10.1016/S0141-8130(03)00073-4 |
en |
dc.identifier.isi |
ISI:000186835800015 |
en |
dc.identifier.volume |
33 |
en |
dc.identifier.issue |
1-3 |
en |
dc.identifier.spage |
101 |
en |
dc.identifier.epage |
106 |
en |