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Science 31 May 1991:
Vol. 252. no. 5010, pp. 1285 - 1288
DOI: 10.1126/science.1656523
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Articles

Science, Vol 252, Issue 5010, 1285-1288
Copyright © 1991 by American Association for the Advancement of Science

articles

Protein electron transfer rates set by the bridging secondary and tertiary structure

DN Beratan, JN Betts, and JN Onuchic

Beratan, Jet Propulsion Laboratory, California Institute of Technology, Pasadena 91109.

The rate of long-distance electron transfer in proteins rapidly decreases with distance, which is indicative of an electron tunneling process. Calculations predict that the distance dependence of electron transfer in native proteins is controlled by the protein's structural motif. The helix and sheet content of a protein and the tertiary arrangement of these secondary structural units define the distance dependence of electronic coupling in that protein. The calculations use a tunneling pathway model applied previously with success to ruthenated proteins. The analysis ranks the average distance decay constant for electronic coupling in electron transfer proteins and identifies the amino acids that are coupled to the charge localization site more strongly or weakly than average for their distance.


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