Objective
As a key enzyme of the biological nitrogen cycle, bacterial nitrite reductase (cytochrome cd1) reduces nitrite but it also catalyses the reduction of oxygen to water. Cytochrome cd1 serves as an ideal model in elucidating three fundamental questions in biology:
- How do electrons move between haem groups?
- How is nitrite reduced to nitric oxide?
- How is oxygen reduced to water?
Based on the first crystal structure of cytochrome cd1, isolated from t soil bacterium T. pantotropha, the structural/ functional properties of this enzyme will be studied via various spectroscopic and electro- chemical methods.
Visible spectroscopy, especially stopped-flow experiments, will elucida the kinetics and catalytic mechanisms of this enzyme with respect to its nitrite and oxygen reducing capabilities. The effect of various substrates and inhibitors will be studied using the wild-type, specifically designed mutants and metal-substituted species.
In addition, redox-titrations and cyclovoltammetry will be used to stud the thermodynamics of inter- and intra electron-transfer processes between haem groups.
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.
- engineering and technology materials engineering crystals
- natural sciences biological sciences microbiology bacteriology
- natural sciences physical sciences thermodynamics
- natural sciences biological sciences biochemistry biomolecules proteins enzymes
- natural sciences physical sciences optics spectroscopy
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Coordinator
OX1 3QU OXFORD
United Kingdom
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