DESIGN AND SYNTHESIS OF MULTI-HEME PROTEINS

A water-soluble, 62-residue, di-alpha-helical peptide has been synthes ized which accommodates two bis-histidyl haem groups. The peptide asse mbles into a four-helix dimer with 2-fold symmetry and four parallel h aems that closely resemble native haems in their spectral and electro- chemical properties, including haem-haem redox interaction. This prote in is an essential intermediate in the synthesis of molecular 'maquett es', a novel class of simplified versions of the metalloproteins invol ved in redox catalysis and in energy conversion in respiratory and pho tosynthetic electron transfer.