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The membrane associated form of methane monooxygenase
Reference
B13749
Principal Investigator / Supervisor
Professor H Dalton
Co-Investigators /
Co-Supervisors
Institution
University of Warwick
Department
Biological Sciences
Funding type
Research
Value (£)
189,468
Status
Completed
Type
Research Grant
Start date
12/02/2001
End date
12/02/2004
Duration
36 months
Abstract
We have recently perfected a protocol for the routine production of high specific activity proteins of this enigmatic enzyme system. We now wish to dissect the structure of the component proteins with a view to understanding the mechanism of action of the particulate methane monooxygenase (pMMO). A combination of these two proteins require duroquinol as reductant for methane oxidation and will be analysed for their prosthetic groups, substrate interactions and component interactions by spectroscopic and kinetic techniques. The as isolated form of the system uses NADH as electron donor which is lost on further purification. We will search for the protein(s) that couple NADH to methane oxidation activity using both a proteomic and direct biochemical analysis.
Summary
unavailable
Committee
Closed Committee - Biomolecular Sciences (BMS)
Research Topics
X – not assigned to a current Research Topic
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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