Electron tunneling in proteins: Coupling through a β strand

Ralf Langen, I. Jy Chang, Juris P. Germanas, John H. Richards, Jay R. Winkler, Harry B. Gray

Research output: Contribution to journalArticle

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Abstract

Electron coupling through a β strand has been investigated by measurement of the intramolecular electron-transfer (ET) rates in ruthenium-modified derivatives of the β barrel blue copper protein Pseudomonas aeruginosa azurin. Surface histidines, introduced on the methionine-121 β strand by mutagenesis, were modified with a Ru(2,2′-bipyridine)2(imidazole)2+ complex. The Cu+ to Ru3+ rate constants yielded a distance-decay constant of 1.1 per angstrom, a value close to the distance-decay constant of 1.0 per angstrom predicted for electron tunneling through an idealized β strand. Activation-less ET rate constants in combination with a tunneling-pathway analysis of the structures of azurin and cytochrome c confirm that there is a generally efficient network for coupling the internal (native) redox center to the surface of both proteins.

Original languageEnglish
Pages (from-to)1733-1735
Number of pages3
JournalScience
Volume268
Issue number5218
DOIs
Publication statusPublished - 1995 Jan 1

ASJC Scopus subject areas

  • General

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    Langen, R., Chang, I. J., Germanas, J. P., Richards, J. H., Winkler, J. R., & Gray, H. B. (1995). Electron tunneling in proteins: Coupling through a β strand. Science, 268(5218), 1733-1735. https://doi.org/10.1126/science.7792598