Accession Number : ADA195482
Title : Cytochrome Electron Transfer and Biomolecular Electronics.
Descriptive Note : Annual rept. Nov 87-Jun 88,
Corporate Author : KANSAS UNIV LAWRENCE DEPT OF CHEMISTRY
Personal Author(s) : Wilson, George S ; Cusanovich, Michael A
PDF Url : ADA195482
Report Date : 22 Jun 1988
Pagination or Media Count : 6
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.
Descriptors : *BLOOD PROTEINS, *ELECTRON TRANSFER, *BIOELECTRICITY, *ELECTROCHEMISTRY, ELECTRICAL PROPERTIES, ELECTROSTATIC FIELDS, FIELD EQUIPMENT, FILMS, GOLD, HALL EFFECT, HETEROGENEITY, HOMOGENEITY, MEASUREMENT, MOLECULE MOLECULE INTERACTIONS, OXIDATION REDUCTION REACTIONS, PHYSICAL PROPERTIES, REDUCTION, RESISTANCE, STRUCTURES, SUBSTRATES, X RAYS, ELECTRICAL RESISTANCE, BIOMOLECULES
Subject Categories : Biochemistry
Distribution Statement : APPROVED FOR PUBLIC RELEASE