Citation:

Fonseca, BM, Paquete CM, Salgueiro CA, Louro RO.  2012.  The role of intramolecular interactions in the functional control of multiheme cytochromes c. FEBS Lett. 586(5):504-509.

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.

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