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Title: Cross-linking and modification of cytochrome c with redox-active metal complexes

Technical Report ·
OSTI ID:5923311

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.

Research Organization:
Ames Lab., IA (USA)
Sponsoring Organization:
USDOE; USDOE, Washington, DC (USA)
DOE Contract Number:
W-7405-ENG-82
OSTI ID:
5923311
Report Number(s):
IS-T-1522; ON: DE91012023
Resource Relation:
Other Information: Thesis (M.S.)
Country of Publication:
United States
Language:
English