We report on a concept that some of us first described a decade ago for pure electron transfer [V. Balland, C. Hureau and J.-M. Savéant, Proc. Natl. Acad. Sci. U. S. A., 2010, 107, 17113]. In the present viewpoint, based on more recent results, we refine and extend this "in-between state" concept to explain the formation of reactive oxygen species by copper ions bound to the amyloid-β (Aβ) peptide involved in Alzheimer's disease. In such intrinsically disordered peptides, the Cu coordination is versatile due to the lack of stable folding and the presence of multiple possible binding anchors. Hence, the Cu(I) and Cu(II) ions do impose their favoured sites, with Cu(I) bound in a linear fashion between two His residues and Cu(II) in a square-based pyramid bound to Asp1 amine and carbonyl groups and two His residues in the equatorial plane. Hence a direct electron transfer is prevented and alternatively an in-between state (IBS) mechanism applies, whose description and analysis with respect to other electron transfer processes is the topic of the present viewpoint.