Use this URL to cite or link to this record in EThOS: http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.603796
Title: Electron transfer proteins in the cyanobacterium Phormidium laminosum
Author: Hart, S. E.
Awarding Body: University of Cambridge
Current Institution: University of Cambridge
Date of Award: 2006
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Abstract:
This study continues the characterisation of redox proteins of the cyanobacterium Phormidium laminosum and their interactions. So far, research has focussed on the interaction between P. laminosum Cyt f and Pc. In order to create a more complete picture of the interactions taking place in P. laminosum, this study has begun the characterisation of P. laminosum COX and four luminal subunits of P. laminosum PSI. A long-term aim of this work is to be able to compare how Pc/Cyt c6 interact with Cyt f, PSI and COX in P. laminosum. The genes of the COX complex and the luminal subunits of PSI have been cloned and their sequences analysed at the nucleotide and amino acid level. It was possible to identify residues likely to be involved in the function of the proteins. P. laminosum was also found to contain the genes for an alternative respiratory terminal oxidase (ARTO), the genes of which have been cloned. In addition, the gene for Cyt cm, which may interact with COX, has been cloned. Attempts have been made to develop expression systems for truncated versions of subunit II of COX (CtaC) and ARTO (CtaCII). Expression of an untagged- and a tagged-version of CtaC in the cytosol of E. coli have been demonstrated. In addition, comparative models for regions of CtaC and Cyt cM have been generated. From these, it has been possible to identify potential docking sites and charge-clusters, which could play a role in the interactions of both proteins. This study expands the understanding of the interaction between Cyt f and Pc of P. laminosum, by determining the role of charged residues of Cyt f in its interaction with Pc.
Supervisor: Not available Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID: uk.bl.ethos.603796  DOI: Not available
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