| Literature DB >> 21856299 |
Bruno M Fonseca1, Catarina M Paquete, Carlos A Salgueiro, Ricardo O Louro.
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. Copyright ÂMesh:
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Year: 2011 PMID: 21856299 DOI: 10.1016/j.febslet.2011.08.019
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124