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

0493016 - MBÚ 2019 RIV DE eng J - Článek v odborném periodiku
D'Oronzo, E. - Secundo, F. - Minofar, Babak - Kulik, Natalia - Pometun, A.A. - Tishkov, V.I.
Activation/Inactivation Role of Ionic Liquids on Formate Dehydrogenase from Pseudomonas sp 101 and Its Mutated Thermostable Form.
ChemCatChem. Roč. 10, č. 15 (2018), s. 3247-3259. ISSN 1867-3880. E-ISSN 1867-3899
Grant ostatní: GA MŠk(CZ) LM2015042
Institucionální podpora: RVO:61388971
Klíčová slova: enzymes * fluorescence spectroscopy * ionic liquids
Obor OECD: Biochemistry and molecular biology
Impakt faktor: 4.495, rok: 2018

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, EC1.2.1.2) 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.
Trvalý link: http://hdl.handle.net/11104/0286486