Cross-linking and Modification of Cytochrome c with Redox-Activ Metal Complexes [Thesis]

This thesis consists of two parts. The first part shows that a redox-active trinuclear metal cluster may be used as a cross-linking reagent for proteins. Electron transfer is observed in the protein oligomers. The second part involves labelling the cysteine residue of baker's yeast cytochrome c with chloromercuriferrocene. Chloromercuriferrocene reacts with cytochrome c in two interesting ways. Symmetrization produces two products; two proteins cross-linked with mercury and diferrocenylmercury. Simple substitution of FeHgCl onto the protein followed by the addition of a proton by electrophilic substitution affords ferrocene and the mercuric chloride modified protein. 16 refs., 3 figs.