The energetic and
geometric features enabling redox chemistry across
the copper cupredoxin fold contain key components of electron transfer
chains (ETC), which have been extended here by templating the cross-β
bilayer assembly of a synthetic nonapeptide, HHQALVFFA-NH2 (K16A), with copper ions. Similar to ETC cupredoxin plastocyanin,
these assemblies contain copper sites with blue-shifted (λ
max
573 nm) electronic transitions and
strongly oxidizing reduction potentials. Electron spin echo envelope
modulation and X-ray absorption spectroscopies define square planar
Cu(II) sites containing a single His ligand. Restrained molecular
dynamics of the cross-β peptide bilayer architecture support
metal ion coordination stabilizing the leaflet interface and indicate
that the relatively high reduction potential is not simply the result
of distorted coordination geometry (entasis). Cyclic voltammetry (CV)
supports a charge-hopping mechanism across multiple copper centers
placed 10–12 Å apart within the assembled peptide leaflet
interface. This metal-templated scaffold accordingly captures the
electron shuttle and cupredoxin functionality in a peptide membrane-localized
electron transport chain.