Gray, Harry B. and Winkler, Jay R. (2005) Long-range electron transfer. Proceedings of the National Academy of Sciences of the United States of America, 102 (10). pp. 3534-3539. ISSN 0027-8424. http://resolver.caltech.edu/CaltechAUTHORS:GRApnas05b
See Usage Policy.
Use this Persistent URL to link to this item: http://resolver.caltech.edu/CaltechAUTHORS:GRApnas05b
Recent investigations have shed much light on the nuclear and electronic factors that control the rates of long-range electron tunneling through molecules in aqueous and organic glasses as well as through bonds in donor-bridge-acceptor complexes. Couplings through covalent and hydrogen bonds are much stronger than those across van der Waals gaps, and these differences in coupling between bonded and nonbonded atoms account for the dependence of tunneling rates on the structure of the media between redox sites in Ru-modified proteins and protein-protein complexes.
|Additional Information:||Copyright © 2005 by the National Academy of Sciences. Edited by Jack Halpern, University of Chicago, Chicago, IL and accepted January 28, 2005 (received for review January 5, 2005). Our work is supported by the National Institutes of Health, the National Science Foundation, BP, and the Arnold and Mabel Beckman Foundation. This paper was submitted directly (Track II) to the PNAS office.|
|Subject Keywords:||ELECTRON TUNNELING, HOPPING, GLASS, PROTEIN, CYTOCHROME-C-OXIDASE, CLASSICAL SOLVENT DYNAMICS, METAL HEMOGLOBIN HYBRIDS, INTERACTION DOMAIN, TRANSFER COMPLEX, SURFACE MUTANTS, TRANSFER RATES, PARACOCCUS-DENITRIFICANS, ALKANETHIOL MONOLAYERS, THEORETICAL-ANALYSIS|
|Usage Policy:||No commercial reproduction, distribution, display or performance rights in this work are provided.|
|Deposited By:||Tony Diaz|
|Deposited On:||15 Nov 2005|
|Last Modified:||14 Nov 2014 19:18|
Repository Staff Only: item control page