tailieunhanh - Báo cáo khoa học: Fluorescence and FTIR study of pressure-induced structural modifications of horse liver alcohol dehydrogenase (HLADH)

The process of pressure-induced modification of horse liver alcohol dehydrogenase (HLADH) was followed by measuringin situ catalytic activity (up to 250 MPa), intrinsic fluorescence (–600 MPa) and modifications of FTIR spectra (up to 1000 MPa). The tryptophan fluor-escence measurements and the kinetic data indicated that the pressure-induced denaturation of HLADH was a process involving several transitions and that the observed transient states have characteristic properties of molten globules. . | Eur. J. Biochem. 270 119-128 2003 FEBS 2003 doi Fluorescence and FTIR study of pressure-induced structural modifications of horse liver alcohol dehydrogenase HLADH Marie Trovaslet1 Sandrine Dallet-Choisy1 Filip Meersman2 Karel Heremans2 Claude Balny3 and Marie Dominique Legoy1 1 Laboratoire de Genie Proteique et Cellulaire Universite de La Rochelle France department of Chemistry Katholieke Universiteit Leuven Belgium 3INSERM U 128 Montpellier Cedex 5 France The process of pressure-induced modification of horse liver alcohol dehydrogenase HLADH was followed by measuring in situ catalytic activity up to 250 MPa intrinsic fluorescence MPa and modifications of FTIR spectra up to 1000 MPa . The tryptophan fluorescence measurements and the kinetic data indicated that the pressure-induced denaturation of HLADH was a process involving several transitions and that the observed transient states have characteristic properties of molten globules. Low pressure 100 MPa induced no important modification in the catalytic efficiency of the enzyme and slight conformational changes characterized by a small decrease in the centre of spectral mass of the enzyme s intrinsic fluorescence a native-like state was assumed. Higher pressures 100-400 MPa induced a strong decrease of HLADH catalytic efficiency and further conformational changes. At 400 MPa a dimeric molten globule-like state was proposed. Further increase of pressure 400-600 MPa seemed to induce the dissociation of the dimer leading to a transition from the first dimeric molten globule state to a second monomeric molten globule. The existence of two independent structural domains in HLADH was assumed to explain this transition these domains were supposed to have different stabilities against high pressure-induced denaturation. FTIR spectroscopy was used to follow the changes in HLADH secondary structures. This technique confirmed that the intermediate states have a lowdegree of unfolding

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