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Published November 8, 1989 | public
Journal Article

Long-range electron transfer in structurally engineered pentaammineruthenium (histidine-62) cytochrome c


In many biological processes, long-range electron transfer (ET) plays a key role. When the three-dimensional structures of proteins are accurately known, use of modified proteins and protein-protein complexes provides an experimental approach to study ET rates between two metal centers. For Ru(His)- modified proteins, the introduction of histidine residues at any desired surface location by site-directed mutagenesis opens the way for systematic investigations of ET pathways.

Additional Information

© 1989 American Chemical Society. Received July 19, 1989. We thank Professor Judith L. Campbell, Dr. Guy Guillemette, Dr. Alfred Gartner, and Professor A. G. Mauk for helpful discussions and Dr. Adrienne Raphael for assistance with the electrochemical (differential pulse polarography) measurements. Large-scale fermentations were done with the aid of Dr. Tom Sutherland at the UCLA Molecular Biology Institute. B.E.B. acknowledges the Medical Research Council (Canada) for a postdoctoral fellowship. This research was supported by National Science Foundation Grant CHE88-14222

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October 23, 2023