title: The role of intramolecular interactions in the functional control of multiheme cytochromes c.
abstract: 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.
authors.affiliation: Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Av. da República, EAN, 2780-157 Oeiras, Portugal.
authors.forename: Bruno M
authors.initials: BM
authors.lastname: Fonseca
authors.forename: Catarina M
authors.initials: CM
authors.lastname: Paquete
authors.forename: Carlos A
authors.initials: CA
authors.lastname: Salgueiro
authors.forename: Ricardo O
authors.initials: RO
authors.lastname: Louro
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism; D045304:Cytochromes c / Q000737:chemistry* / Q000378:metabolism; D004579:Electron Transport; D006418:Heme / Q000737:chemistry* / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D008958:Models, Molecular; D010084:Oxidation-Reduction; D011487:Protein Conformation; D055672:Static Electricity; D013816:Thermodynamics
chemical_list: D001426:Bacterial Proteins; D006418:Heme; D045304:Cytochromes c