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Cited by 191

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Coupling Coherence Distinguishes Structure Sensitivity in Protein Electron Transfer

Open access
Prytkova, Tatiana R., Kurnikov, Igor V., Beratan, David N.·2007·Science

Abstract

Quantum mechanical analysis of electron tunneling in nine thermally fluctuating cytochrome b 562 derivatives reveals two distinct protein-mediated coupling limits. A structure-insensitive regime arises for redox partners coupled through dynamically averaged multiple-coupling pathways (in seven of the nine derivatives) where heme-edge coupling leads to the multiple-pathway regime. A structure-dependent limit governs redox partners coupled through a dominant pathway (in two of the nine derivatives) where axial-ligand coupling generates the single-pathway limit and slower rates. This two-regime paradigm provides a unified description of electron transfer rates in 26 ruthenium-modified heme and blue-copper proteins, as well as in numerous photosynthetic proteins.

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Crossref · 10.1126/science.1134862

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Metadata

Authors
Prytkova, T. R., Kurnikov, I. V., & Beratan, D. N.
Venue
Science
Published
2007-02-02
Volume
315
Issue
5812
Pages
622-625
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2066991715
Cited by
191
References
1
FWCI
13.44
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Coupling Coherence Distinguishes Structure Sensitivity in Protein Electron Transfer. https://app.cochat.ai/papers/10.1126/science.1134862
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Prytkova, T. R., Kurnikov, I. V., & Beratan, D. N. (2007). Coupling Coherence Distinguishes Structure Sensitivity in Protein Electron Transfer. Science. https://doi.org/10.1126/science.1134862

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Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.