The DOI matches its Crossref record; 26 of the 26 references it cites were found in a registry or an index.
The Nature of Aqueous Tunneling Pathways Between Electron-Transfer Proteins
Open accessAbstract
Structured water molecules near redox cofactors were found recently to accelerate electron-transfer (ET) kinetics in several systems. Theoretical study of interprotein electron transfer across an aqueous interface reveals three distinctive electronic coupling mechanisms that we describe here: (i) a protein-mediated regime when the two proteins are in van der Waals contact; (ii) a structured water-mediated regime featuring anomalously weak distance decay at relatively close protein-protein contact distances; and (iii) a bulk water–mediated regime at large distances. Our analysis explains a range of otherwise puzzling biological ET kinetic data and provides a framework for including explicit water-mediated tunneling effects on ET kinetics.
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Self-citationError estimates on averages of correlated data
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Cited by
Water as an active constituent in cell biology
Ball, P. (2008) · Chemical Reviews · doi:10.1021/cr068037a · Cited by 2,177
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Electron-transfer chain in respiratory complex I
Martin, D. R., & Matyushov, D. V. (2017) · Scientific Reports · doi:10.1038/s41598-017-05779-y · Cited by 63
Metadata
- Authors
- Lin, J., Balabin, I. A., & Beratan, D. N.
- Venue
- Science
- Published
- 2005-11-25
- Volume
- 310
- Issue
- 5752
- Pages
- 1311-1313
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1991010290
- Cited by
- 254
- References
- 26
- FWCI
- 11.84
- Type
- journal article
- Language
- en
- Open access
- green
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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.
