Objective
PROTEINS CONTAINING METAL IONS DO CATALYSE MANY IMPORTANT BIOLOGICAL REACTIONS, NAMELY THOSE INVOLVING TRANSFER OF ELECTRONS. IT IS ANTICIPATED THAT MODIFICATIONS OF THE METAL CLUSTERS OF THESE PROTEINS WILL OPEN NEW CATALYTIC POSSIBILITIES THAT CAN BE USED IN MULTIPHASE BIOCATALYSIS AND THE DEVELOPMENT OF NOVEL BIOREACTORS. THE DESIGN OF SUCH CATALYSTS OBTAINED BY A BIOSYNTHETIC ROUTE MAY TURN OUT TO BE ADVANTAGEOUS IN COMPARISON WITH CHEMICAL SYNTHETIC ONES AND CAN THUS SUBSTANTIALLY EXPAND THE FIELD OF BIOINORGANIC CHEMISTRY.
Iron sulfur proteins are involved as main catalysts in bioconversion processes (hydrogen evolution, nitrogen and carbon monoxide fixation, photosynthesis, respiration, etc). The metal active centres of different iron sulfur proteins, simple and complex, (eg, rubredoxin, ferredoxins and hydrogenase) were characterized and chemically modified, in order to produce new active structures with novel, and/or enhanced catalytic properties. A new concept of assisted inorganic synthesis by a protein template was developed for the synthesis of mixed metal clusters. The reactivity and stability of the newly formed catalysts and hydrogenase (free and immobilized) were tested by measuring hydrogen evolution and production, deuterium protium exchange (mass spectroscopy) and hydrogenation activity.
The following results were obtained (from research into the structure, reactivity and immobilization of metalloproteins:
isomorphous substitutions (cobalt and nickel) of the iron centre in rubredoxins:
chemical and spectroscopic characterization;
testing biocatalytic performance and mimicking of bacterial hydrogenase activity (model design);
assisted inorganic synthesis of novel mixed metal clusters of the type M, 3 iron-4 sulphur (M = cobalt, nickel, zinc, cadmium, calcium);
spectroscopic studies involving electron paramagnetic resonance (EPR), nuclear magnetic resonance (NMR) and Moessbauer methods;
characterization of the metal sites involved in bacterial hydrogen production and consumption;
differentiation of hydrogenase types by their spectroscopic, catalytic and inhibition parameters;
biocatalysis in organic media using hydrogenase encapsulated in micellar systems;
kinetics of both free and immobilized hydrogenases;
stability of the hydrogen evolving system in reversed micellar systems (multiphase system) using purified hydrogenase and whole cells.
IN ORDER TO PROVIDE THE OTHER PARTNERS IN THE PROJECT WITH SUFFICIENT (PURE) STARTING MATERIAL THE SULFATE REDUCING AS WELL AS METHANOGENIC BACTERIA WILL BE GROWN AT BIG QUANTITIES. AT THE SAME TIMES ENRICHED CAN BE PERFORMED WITH EITHER 61NI, 57FE OR 77SE. THE IRON-SULFUR CONTAINING PROTEINS WILL BE EXTRACTED FROM THE CELLS AND FURTHER PURIFIED. AFTER BOTH MODIFICATION OF THE ENZYMES CHEMICALLY AS WELL AS INTRODUCING DIFFERENT METALS IN ORDER TO OBTAIN MIXED METAL CLUSTERS, BOTH THE NATIVE AND MODIFIED ENZYMES WILL BE ASSAYED FOR THEIR ACTIVITY BY MEASURING H/D-EXCHANGE USING MASS SPECTROMETRY. IN THE FINAL PHASE OF THE PROJECT THESE ENZYMES WILL BE IMMOBILISED AND ASSAYED IN THE SAME WAY FOR EXAMPLE IN MULTIPHASIC REACTORS AND USING FOR EXAMPLE ACETYLENE AS SUBSTRATE.
Fields of science (EuroSciVoc)
CORDIS classifies projects with EuroSciVoc, a multilingual taxonomy of fields of science, through a semi-automatic process based on NLP techniques. See: The European Science Vocabulary.
CORDIS classifies projects with EuroSciVoc, a multilingual taxonomy of fields of science, through a semi-automatic process based on NLP techniques. See: The European Science Vocabulary.
- natural sciences chemical sciences inorganic chemistry bioinorganic chemistry
- natural sciences chemical sciences inorganic chemistry inorganic compounds
- natural sciences chemical sciences inorganic chemistry transition metals
- natural sciences chemical sciences catalysis biocatalysis
- natural sciences biological sciences biochemistry biomolecules proteins enzymes
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Coordinator
13108 Saint-Paul-lez-Durance
France
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