Coupling Coherence Distinguishes Structure Sensitivity in Protein Electron Transfer
| Autor: | David N. Beratan, Igor V. Kurnikov, Tatiana R. Prytkova |
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| Rok vydání: | 2007 |
| Předmět: |
Models
Molecular Protein Folding Chemical Phenomena Cytochrome Protein Conformation Stereochemistry Ligands Redox Ruthenium Article Electron Transport Electron transfer Protein structure Computer Simulation Histidine Quantum Quantum tunnelling Multidisciplinary biology Chemistry Physical Chemistry Cytochromes c Hydrogen Bonding Cytochrome b Group Electron transport chain Models Chemical Chemical physics biology.protein Protein folding Oxidation-Reduction Mathematics |
| Zdroj: | Science. 315:622-625 |
| ISSN: | 1095-9203 0036-8075 |
| DOI: | 10.1126/science.1134862 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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