Electron-Tunneling Pathways in Ruthenated Proteins


Journal Article

We implement a numerical algorithm to survey proteins for electron-tunneling pathways. Insight is gained into the nature of the mediation process in long-distance electron-transfer reactions. The dominance of covalent and hydrogen bond pathways is shown. The method predicts the relative electronic couplings in ruthenated myoglobin and cytochrome c consistent with measured electron-transfer rates. It also allows the design of long-range electron-transfer systems. Qualitative differences between pathways arise from the protein secondary structure. Effects of this sort are not predicted from simpler models that neglect various details of the protein electronic structure. © 1990, American Chemical Society. All rights reserved.

Full Text

Duke Authors

Cited Authors

  • Beratan, DN; Nelson Onuchic, J; Betts, JN; Bowler, BE; Gray, HB

Published Date

  • January 1, 1990

Published In

Volume / Issue

  • 112 / 22

Start / End Page

  • 7915 - 7921

Electronic International Standard Serial Number (EISSN)

  • 1520-5126

International Standard Serial Number (ISSN)

  • 0002-7863

Digital Object Identifier (DOI)

  • 10.1021/ja00178a011

Citation Source

  • Scopus