Catechol 1,2-dioxygenase from Pseudomonas putida in organic media--an electron paramagnetic resonance study.
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.
Biotechnology Laboratory, Biological Applications and Technologies Department, University of Ioannina, 45110 Ioannina, Greece.
Y
Y
Sanakis
D
D
Mamma
P
P
Christakopoulos
H
H
Stamatis
D050548:Catechol 1,2-Dioxygenase; D049308:Dioxygenases; D004578:Electron Spin Resonance Spectroscopy / Q000379:methods*; D005612:Freeze Drying; D006586:Hexanes / Q000737:chemistry; D007501:Iron / Q000737:chemistry / Q000378:metabolism; D010105:Oxygenases / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*; D016958:Pseudomonas putida / Q000201:enzymology*; D012996:Solutions
D006586:Hexanes; D012996:Solutions; D007501:Iron; D010105:Oxygenases; D049308:Dioxygenases; D050548:Catechol 1,2-Dioxygenase