Format:
XVIII, 110 S.
,
Ill., graph. Darst.
Content:
Electron transfer (ET) reactions play a crucial role in the metabolic pathways of all organisms. In biotechnological approaches, the redox properties of the protein cytochrome c (cyt c), which acts as an electron shuttle in the respiratory chain, was utilized to engineer ET chains on electrode surfaces. With the help of the biopolymer DNA, the redox protein assembles into electro active multilayer (ML) systems, providing a biocompatible matrix for the entrapment of proteins. In this study the characteristics of the cyt c and DNA interaction were defined on the molecular level for the first time and the binding sites of DNA on cyt c were identified. Persistent cyt c/DNA complexes were formed in solution under the assembly conditions of ML architectures, i.e. pH 5.0 and low ionic strength. At pH 7.0, no agglomerates were formed, permitting the characterization of the NMR spectroscopy. Using transverse relaxation-optimized spectroscopy (TROSY)-heteronuclear single quantum coherence (HSQC) experiments, DNAs’ binding sites on the protein…
Note:
Potsdam, Univ., Diss., 2015
Additional Edition:
Erscheint auch als Online-Ausgabe Wettstein, Christoph Cytochrome c-DNA and cytochrome c-enzyme interactions for the construction of analytical signal chains 2015
Language:
English
Keywords:
Hochschulschrift
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