Design and synthesis of multi-haem proteins

Abstract

A water-soluble, 62-residue, di-α-helical peptide has been synthesized which accommodates two bis-histidyl haem groups. The peptide assembles into a four-helix dimer with 2-fold symmetry and four parallel haems that closely resemble native haems in their spectral and electrochemical properties, including haem–haem redox interaction. This protein is an essential intermediate in the synthesis of molecular 'maquettes', a novel class of simplified versions of the metalloproteins involved in redox catalysis and in energy conversion in respiratory and photosynthetic electron transfer.

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Robertson, D., Farid, R., Moser, C. et al. Design and synthesis of multi-haem proteins. Nature 368, 425–432 (1994). https://doi.org/10.1038/368425a0

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