Cytochrome Electron Transfer and Biomolecular Electronics.
Abstract
This research pursues our previous observation that films of cytochrome c3 deposited on a gold substrate undergo a change in resistivity of ten orders of magnitude when this tetraheme protein passes from a fully oxidized to a fully reduced state. This unusual behavior appears to be attributable to the ability of the four hemes to 'communicate' through intramolecular as well as intermolecular electron transfer. To understand this phenomenon in more detail, four cytochromes c3 with differing physical properties have been selected: 1. D. vulgaris (Miyazaki); 2. D. vulgaris (Hildenborough); 3. D. sulfuricans (Norway) and 4. D. gigas. The macroscopic redox potentials for each of the hemes in the four proteins have been determined. Electrostatic field maps based on the x-ray structures of the Norway and Miyazaki proteins have been prepared to assist in the design of homogeneous and heterogeneous electron transfer experiments. In the next year, the electrical properties of cytochrome films will be evaluated through Hall effect measurements in particular to establish whether the conductivity is ionic or electronic. Keywords: Oxidation reduction reactions.
Document Details
- Document Type
- Technical Report
- Publication Date
- Jun 22, 1988
- Accession Number
- ADA195482
Entities
People
- George S. Wilson
- Michael A. Cusanovich
Organizations
- University of Kansas