Activation/Inactivation Role of Ionic Liquids on Formate Dehydrogenase from Pseudomonas sp. 101 and Its Mutated Thermostable Form

Ionic liquids (ILs) are used in numerous research areas including biocatalysis. The effect of ILs/water mixture on the activity of wild type and a more thermally and chemically stable mutant (SM4) of a specific formate dehydrogenases (PseFDH, EC 1.2.1.2) were studied experimentally and by molecular...

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Published in:ChemCatChem Vol. 10; no. 15; pp. 3247 - 3259
Main Authors: D'Oronzo, Erica, Secundo, Francesco, Minofar, Babak, Kulik, Natallia, Pometun, Anastasia A., Tishkov, Vladimir I.
Format: Journal Article
Language:English
Published: Weinheim Wiley Subscription Services, Inc 13-08-2018
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Summary:Ionic liquids (ILs) are used in numerous research areas including biocatalysis. The effect of ILs/water mixture on the activity of wild type and a more thermally and chemically stable mutant (SM4) of a specific formate dehydrogenases (PseFDH, EC 1.2.1.2) were studied experimentally and by molecular dynamics (MD) simulations. The ILs investigated were [Mmim][Me2PO4], [Bmim][Br], [Bmim][CH3SO3], [Bmim][BF4], [Bmim][AcO], and it was found that low concentrations (optimally 2.5 %) of some ILs increased (up to 42 %) the activity of the SM4 FDH but not of the WT FDH. Using intrinsic fluorescence to calculate Stern–Volmer constants and thermodynamic parameters, we have studied protein conformational changes caused by ILs for both enzymes. Kinetic analyses allowed us to shed light on the mechanism of activation by 2.5 % [Bmim][BF4] on the mutant enzyme. MD simulation provided evidences of a molecular basis of different enzyme activities in ILs that well correlated with the experimental data. Salty environment: The effects of ionic liquid–water mixtures on the activity of wild‐type and SM4 mutant of formate dehydrogenase are studied experimentally and by molecular dynamics simulations. Low concentrations of some ionic liquids increase the enzyme activity. A molecular basis to the action of ionic liquids on protein conformational changes and activity is pointed out.
ISSN:1867-3880
1867-3899
DOI:10.1002/cctc.201800145