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Electron Tunneling in Proteins: Coupling Through a β Strand

Langen, Ralf and Chang, I-Jy and Germanas, Juris P. and Richards, John H. and Winkler, Jay R. and Gray, Harry B. (1995) Electron Tunneling in Proteins: Coupling Through a β Strand. Science, 268 (5218). pp. 1733-1735. ISSN 0036-8075. doi:10.1126/science.7792598.

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Electron coupling through a beta strand has been investigated by measurement of the intramolecular electron-transfer (ET) rates in ruthenium-modified derivatives of the beta barrel blue copper protein Pseudomonas aeruginosa azurin. Surface histidines, introduced on the methionine-121 beta strand by mutagenesis, were modified with a Ru(2,2'-bipyridine)2(imidazole)^2+ complex. The Cu+ to Ru^3+ 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 beta strand. Activationless 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.

Item Type:Article
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URLURL TypeDescription DOIArticle
Winkler, Jay R.0000-0002-4453-9716
Gray, Harry B.0000-0002-7937-7876
Additional Information:© 1995 American Association for the Advancement of Science. 17 January 1995; accepted 23 March 1995. We thank D. R. Casimiro, K. Warncke, J. J. Regan, and J. N. Onuchic for helpful comments. Supported by NIH and NSF.
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Issue or Number:5218
Record Number:CaltechAUTHORS:20150116-145929070
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Official Citation:Langen, R., Chang, I., Germanas, J., Richards, J., Winkler, & Gray, H. (1995). Electron tunneling in proteins: coupling through a beta strand. Science, 268(5218), 1733-1735. doi: 10.1126/science.7792598
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:53841
Deposited On:17 Jan 2015 03:10
Last Modified:10 Nov 2021 20:07

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