The role of intramolecular interactions in the functional control of multiheme cytochromes c

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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
Original languageUnknown
Pages (from-to)504-509
JournalFEBS Letters
Volume586
Issue number5
DOIs
Publication statusPublished - 1 Jan 2012

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