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Thesis

Structure-function relationship studies in the disulfide-bond reductase DsbD and a c-type apocytochrome

Abstract:

The efficient covalent attachment of heme to c-type apocytochromes in the periplasm of Gram-negative bacteria requires the provision of reductant. Heme attachment is facilitated by a system of eight proteins, the Cytochrome c maturation (Ccm) system. The disulfide bond oxidoreductase DsbD, a member of the Disulfide bond formation system (Dsb), transfers reductant to the Ccm system via interaction with one of its proteins, CcmG. This study is focused on two key proteins of these systems, the p...

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Institution:
University of Oxford
Division:
MSD
Department:
Biochemistry
Oxford college:
Merton College
Role:
Depositor, Author

Contributors

Division:
MSD
Department:
Biochemistry
Role:
Supervisor
Division:
MSD
Department:
Biochemistry
Role:
Supervisor
Publication date:
2011
Type of award:
MSc by Research
Level of award:
Masters
Awarding institution:
University of Oxford
UUID:
uuid:756c13fd-1e72-49a0-8205-8158b717c0d0
Local pid:
ora:6624

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