Abstract
Interactions between charged porphyrins and complimentary or similarly charged proteins provide important models systems for studies of electron transfer processes, artificial photosynthesis, and control of protein-protein interactions. Typically, the experimental results are analyzed and discussed assuming that the proteins exist in a monodisperse state. However, combined small- and wide-angle X-ray scattering experiments revealed the formation of multimers with a wide range of complex sizes. Binding interactions were explored using wild-type and 12 mutants of PpcA, a 3-heme c-type cytochrome from Geobacter sulfurreducens, with several anionic water-soluble derivatives of tetraphenylporphyrin.
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