Design and synthesis of multi-haem proteins. Academic Article uri icon


  • A water-soluble, 62-residue, di-alpha-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.

published proceedings

  • Nature

altmetric score

  • 3

author list (cited authors)

  • Robertson, D. E., Farid, R. S., Moser, C. C., Urbauer, J. L., Mulholland, S. E., Pidikiti, R., ... Dutton, P. L.

citation count

  • 538

complete list of authors

  • Robertson, DE||Farid, RS||Moser, CC||Urbauer, JL||Mulholland, SE||Pidikiti, R||Lear, JD||Wand, AJ||DeGrado, WF||Dutton, PL

publication date

  • March 1994

published in