Chemistry of the iron-molybdendum-cofactor of nitrogenase

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Project objective

Research objectives and content The aim of the project is to define chemistry of FeMoco, the isolable cluster which is at the heart of enzymic nitrogen fixation. Defining how and where dinitrogen or other small molecules interact with FeMoco, the redox levels at which their binding and reduction takes place, and how supramolecular or intramolecular hydrogen-bonding or coulombic interactions modify the properties of the cofactor, will contribute to a better understanding of the mechanism of the biological process and to the design of artificial fixation systems. Training content (objective, benefit and expected impact) Dr Schollhammer will gain direct experience in the application of advanced fast reaction kinetic and electrochemical techniques, in a multi-disciplinary environment, by addressing an important problem in bioinorganic chemistry. Expertise and facilities in EPR/ENDOR, multinuclear NMR, X-ray crystallography and Moessbauer spectroscopy can be called upon within NFL as and where appropriate. He will be working on the chemistry of a natural system against a background of considerable 'in house' knowledge of model inoganic systems and he will benefit the project by bringing in his own expertise in metal-sulphur chemistry. Links with industry / industrial relevance (22) Industrial relevance: new abiological nitrogen fixation systems may evolve from an understanding of FeMoco chemistry

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Participants

• JOHN INNES CENTRE · NORWICHCoordinatorUnited Kingdom

Links

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