The role of intramolecular interactions in the functional control of multiheme cytochromes c
| Autor: | Ricardo O. Louro, Bruno M. Fonseca, Carlos A. Salgueiro, Catarina M. Paquete |
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| Rok vydání: | 2011 |
| Předmět: |
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Molecular Heme-heme interaction Stereochemistry Protein Conformation Cooperativity Static Electricity Biophysics Heme 010402 general chemistry 01 natural sciences Biochemistry Redox Redox Activity Heme–heme interaction Electron transfer Electron Transport 03 medical and health sciences Bacterial Proteins Structural Biology Genetics Molecular Biology 030304 developmental biology 0303 health sciences Chemistry Cytochromes c Cell Biology Hydrogen-Ion Concentration 0104 chemical sciences Intramolecular force Functional significance Thermodynamics Oxidation-Reduction Multiheme cytochrome c |
| Zdroj: | FEBS letters. 586(5) |
| ISSN: | 1873-3468 |
| Popis: | Detailed thermodynamic and structural data measured in soluble monomeric multiheme cytochromes c provided the basis to investigate the functional significance of interactions between redox co-factors. The steep decay of intramolecular interactions with distance means that close proximity of the redox centers is necessary to modulate the intrinsic reduction potentials in a significant way. This ensures selection of specific populations during redox activity in addition to maintaining fast intramolecular electron transfer. Therefore, intramolecular interactions between redox co-factors play an important role in establishing the biological function of the protein by controlling how electrons flow through and are distributed among the co-factors. |
| Databáze: | OpenAIRE |
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