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Assembly of cytochrome c-dependent electron transfer chains in bacteria: are there chaperones in the periplasm?

ReferenceC07661
Principal Investigator / Supervisor Professor Jeffrey Cole
Co-Investigators /
Co-Supervisors
Institution University of Birmingham
DepartmentSch of Geography, Earth & Env Sciences
Funding typeResearch
Value (£) 149,873
StatusCompleted
TypeResearch Grant
Start date 01/09/1997
End date 01/09/2000
Duration36 months

Abstract

Three anaerobically induced electron transfer chains of enteric bacteria include c-type cytochromes. Their operons are unexpectedly complex, encoding the terminal reductases, other electron transfer proteins, assembly and folding functions. The aims are to determine how c-type cytochromes are assembled in the periplasm of Escherichia coli; the roles of individual cytochrome c maturation proteins and how they interact with disulphide bond formation proteins acting like chaperones in the ordered assembly of multi-haem c-type cytochromes; factors that increase the rate of turnover of the electron transfer components; whether there are two haem transporters (for cytochrome oxidase Cyd and another for haem c) and two haem lyases, one to catalyse attachment of haem to a novel C-W-S-C-K motif of cytochrome c552.

Summary

unavailable
Committee Closed Committee - Biochemistry & Cell Biology (BCB)
Research TopicsX – not assigned to a current Research Topic
Research PriorityX – Research Priority information not available
Research Initiative X - not in an Initiative
Funding SchemeX – not Funded via a specific Funding Scheme
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