Award details

MOTTLE - MCD Spectroscopy with in situ electrochemical control. defining the status of all hemes across a continuous potential window

Reference	BB/C007808/1
Principal Investigator / Supervisor	Professor Julea Butt
Co-Investigators / Co-Supervisors	Dr Myles Cheesman, Professor James Durrant, Dr Sophie Marritt
Institution	University of East Anglia
Department	Chemistry
Funding type	Research
Value (£)	146,297
Status	Completed
Type	Research Grant
Start date	01/08/2005
End date	31/03/2009
Duration	44 months

Abstract

The techniques of MCD spectroscopy and protein voltammetry have contributed significantly to the understanding of metalloproteins. They provide valuable complementary information when applied in parallel but uncertainties always exist in the extent to which information from one method can be directly correlated to observations made with the other. This proposal aims to develop true integration of MCD spectroscopy and voltammetry in a device that will exploit the full capabilities of both, simultaneously, using a single sample. Nanostructured, optically transparent electrode materials will be used as working electrodes to permit MCD spectroscopy (200-8000 nm) of samples held under precisely defined but variable potential control in situ. The optimised technology will be used to address key mechanistic issues in the enzymology of several heme-containing oxidoreductases. We will elucidate redox driven chemistries in the active sites of enzymes involved in the carbon-, nitrogen- and sulfur- cycles (a formate dehydrogenase, nitrate reductase and thiosulfate oxidase), establish the previously elusive nature of the O2 reduction site in a high affinity oxidase (cytochrome bd) and resolve how the state of peripheral hemes affects those in the functional core of a heme-containing copper oxidase (cytochrome cbb3). The result of each study will be integrated with current knowledge of these enzymes to refine the descriptions of their catalytic chemistries and to elucidate mechanisms that may serve to regulate the catalytic rates exhibited by these enzymes in vivo.

Summary

unavailable

Committee	Closed Committee - Biomolecular Sciences (BMS)
Research Topics	Technology and Methods Development
Research Priority	X – Research Priority information not available
Research Initiative	X - not in an Initiative
Funding Scheme	X – not Funded via a specific Funding Scheme

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