DocumentCode :
1826639
Title :
Cytochrome c3, an oriented iron wire
Author :
Cusanovich, Michael A. ; Akutsu, Hideo ; Hazzard, Jo H.
Author_Institution :
Dept. of Biochem., Arizona Univ., Tucson, AZ, USA
fYear :
1989
fDate :
9-12 Nov 1989
Firstpage :
1339
Abstract :
The kinetics of reduction and ligand binding by the cytochromes c 3 are reported on as part of an ongoing effort to understand the unique electrical properties of this unusual heme protein family. When absorbed as films on electrode surfaces they show conductivity changes of ten orders of magnitude when the iron redox state is changed. The studies presented establish that both carbon monoxide binding and deazariboflavin semiquinone reduction enable the hemes of cytochrome c 3 to be discriminated and offer the opportunity of characterizing the interaction domains and immediate heme environment of each of the hemes. This may provide the means for investigating the interactions between the hemes. The approaches described here, coupled with the use of cytochrome c3 from other species (natural chemical modification) and site-directed mutagenesis, should allow one to understand in molecular terms those properties of cytochrome c3 that result in its unique behavior in dry films
Keywords :
bioelectric phenomena; molecular biophysics; proteins; conductivity changes; deazariboflavin semiquinone reduction; dry films; heme environment; protein electrical properties; site-directed mutagenesis; Biomedical electrodes; Bonding; Conducting materials; Conductive films; Conductivity; Electrons; Iron; Kinetic theory; Temperature dependence; Wire;
fLanguage :
English
Publisher :
ieee
Conference_Titel :
Engineering in Medicine and Biology Society, 1989. Images of the Twenty-First Century., Proceedings of the Annual International Conference of the IEEE Engineering in
Conference_Location :
Seattle, WA
Type :
conf
DOI :
10.1109/IEMBS.1989.96227
Filename :
96227
Link To Document :
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