The role of intramolecular interactions in the functional control of multiheme cytochromes c
Copyright policy )The role of intramolecular interactions in the functional control of multiheme cytochromes c
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.
Models, Molecular, Protein Conformation, Cooperativity, Static Electricity, Cytochromes c, Heme, Hydrogen-Ion Concentration, Heme–heme interaction, Electron transfer, Electron Transport, Bacterial Proteins, Thermodynamics, Oxidation-Reduction, Multiheme cytochrome c
Models, Molecular, Protein Conformation, Cooperativity, Static Electricity, Cytochromes c, Heme, Hydrogen-Ion Concentration, Heme–heme interaction, Electron transfer, Electron Transport, Bacterial Proteins, Thermodynamics, Oxidation-Reduction, Multiheme cytochrome c
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