The goal of this project is to study the relationship between structure and function of the F\sub 1\nosub F\sub 2\nosub type H\super +\nosuper-ATPases, a key enzyme for energy supply in almost all organisms. Emphasis will be focused on photosynthetic ATPases, including those of thermostable species, especially useful for biotehcnological applications. These membranes-bound enzymes are molecular machine that transform a transmembrane proton gradient into the chemical energy of ATP. Our group is interested in the mechanisms that modulate the ATP synthesis/hydrolisis and coupled proton transport activities. Because of the complexity of these proteins, one import experimental approach will be the reconstruction of the purified proteins into well-defined liposome systems. Proteoliposomes will be characterized taking into account the influence of several parameters: lipid/ protein ratio, homogeneity in size and protein content, asymmetry of protein incorptration low ionic permeability. With the development of functional proteoliposomes systems we expect to obtain new and better methods to incorporate integral membrane porteins into liposomes. Functional studies will include the influence of the membrane properties on the formation of proton gradients and enzyme activity. Enzyme structure will be studied by means of fluorescence and infrared spectroscopy (FTIR) as well as by microcalorimetry (DSC)
|Effective start/end date||1/09/93 → 30/09/96|
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