Catechol 1,2-dioxygenase from Pseudomonas putida in organic media - An electron paramagnetic resonance study

Sanakis, Y; Mamma, D; Christakopoulos, P; Stamatis, H

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