Add time:08/23/2019         Source:sciencedirect.com

Many biological functions involve the formation of protein-protein complexes. In the present study, we investigated the interaction of two proteins involved in electron transfer, Adrenodoxin (cas 12687-22-8) (Adx) and adrenodoxin reductase (AdR) by using Raman and infrared spectroscopies. Different shifts and splittings of the FeSb/t stretching vibrational modes upon interaction of the two proteins can be reported pointing towards major structural changes in the [2Fe2S] cluster. These changes may be necessary for optimizing electron transfer. The assignment of the shifted modes to the [2Fe2S] cluster was confirmed by 54Fe labeling of the truncated Adx (4–108) as well as the investigation of mutants close to the interaction site and in the vicinity of the [2Fe2S] cluster. Electrochemically induced FTIR difference spectra revealed that the flavin cofactor in AdR also changes due to the interaction with [2Fe2S] cluster in the Adx/AdR electron transfer complex.

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