The DOI matches its Crossref record; 60 of the 60 references it cites were found in a registry or an index.
Long-range electron transfer
Open accessAbstract
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.
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Cites
Electron transfers in chemistry and biology
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Zur Quantentheorie des Atomkernes
Gamow, G. (1928) · Zeitschrift f�r Physik · doi:10.1007/bf01343196 · Cited by 2,331
Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans
Iwata, S., Ostermeier, C., Ludwig, B., & Michel, H. (1995) · Nature · doi:10.1038/376660a0 · Cited by 2,006
The atomic structure of protein-protein recognition sites 1 1Edited by A. R. Fersht
Conte, L. L., Chothia, C., & Janin, J. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.2439 · Cited by 1,964
Natural engineering principles of electron tunnelling in biological oxidation–reduction
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Structures of Metal Sites of Oxidized Bovine Heart Cytochrome c Oxidase at 2.8 Å
Tsukihara, T., Aoyama, H., Yamashita, E., Tomizaki, T., Yamaguchi, H., Shinzawa-Itoh, K., Nakashima, R., Yaono, R., & Yoshikawa, S. (1995) · Science · doi:10.1126/science.7652554 · Cited by 1,415
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Self-citationRedox-Coupled Crystal Structural Changes in Bovine Heart Cytochrome c Oxidase
Yoshikawa, S., Shinzawa-Itoh, K., Nakashima, R., Yaono, R., Yamashita, E., Inoue, N., Yao, M., Fei, M. J., Libeu, C. P., Mizushima, T., et al. (1998) · Science · doi:10.1126/science.280.5370.1723 · Cited by 1,039
Intramolecular Charge Transfer in Aromatic Free Radicals
McConnell, H. M. (1961) · The Journal of Chemical Physics · doi:10.1063/1.1731961 · Cited by 985
Dynamical effects in electron transfer reactions
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Krausz, F., & Ivanov, M. (2009) · Reviews of Modern Physics · doi:10.1103/revmodphys.81.163 · Cited by 5,468
Water as an active constituent in cell biology
Ball, P. (2008) · Chemical Reviews · doi:10.1021/cr068037a · Cited by 2,177
Lambert, N., Chen, Y.-N., Cheng, Y.-C., Li, C.-M., Chen, G.-Y., & Nori, F. (2013) · Nature Physics · doi:10.1038/nphys2474 · Cited by 948
Light Harvesting for Organic Photovoltaics
Hedley, G. J., Ruseckas, A., & Samuel, I. D. W. (2017) · Chemical Reviews · doi:10.1021/acs.chemrev.6b00215 · Cited by 580
Tay, N. E. S., Lehnherr, D., & Rovis, T. (2022) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00384 · Cited by 518
Metadata
- Authors
- Gray, H. B., & Winkler, J. R.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2005-02-28
- Volume
- 102
- Issue
- 10
- Pages
- 3534-3539
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2105348198
- Cited by
- 855
- References
- 60
- FWCI
- 20.45
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Gray, H. B., & Winkler, J. R. (2005). Long-range electron transfer. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0408029102
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
