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Modulation of proton and electron transfer to the active site of nitrogenase: time-resolved EPR, ENDOR and FTIR studies
Reference
BBS/E/J/0000A104
Principal Investigator / Supervisor
Professor David John Lowe
Co-Investigators /
Co-Supervisors
Institution
John Innes Centre
Department
John Innes Centre Department
Funding type
Research
Value (£)
18,494
Status
Completed
Type
Institute Project
Start date
03/03/2003
End date
02/03/2006
Duration
36 months
Abstract
To test mechanistic hypotheses, informed by the high-resolution X-ray structures of nitrogenase, that certain totally-conserved amino-acid residues modulate interactions within protein:protein complexes and control the coupling of the electron and proton transfers that effect dinitrogen reduction by: 1) determining the effect of directed mutations on the reduction of substrates requiring different numbers of electrons and protons; 2) detecting bound, partially-reduced, intermediates in the reduction of these substrates by time-resolved EPR, ENDOR, and FTIR spectroscopies; 3) use the inhibitors CO and NO to interrogate transient odd- and even-electron redox states of nitrogenase; 4) examining MgATP-hydrolysis induced conformational changes.
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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