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Nature 368, 425-432 (31 March 1994) | doi:10.1038/368425a0; Received 18 October 1993; Accepted 27 January 1994

Design and synthesis of multi-haem proteins

Dan E. Robertson*, Ramy S. Farid*, Christopher C. Moser*, Jeffrey L. Urbauer†, Stephen E. Mulholland*, Ravindernath Pidikiti*, James D. Lear‡, A. Joshua Wand†, William F. DeGrado*‡ & P. Leslie Dutton*

  1. *Johnson Research Foundation, Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA
  2. †Department of Biochemistry, School of Chemical Sciences, University of Illinois at Urbana-Champaign, 600 S. Matthews Street, Urbana, Illinois 61801, USA
  3. ‡E. I. du Pont de Nemours Co., Central Research and Development Department, PO Box 80328, Wilmington, Delaware 19880, USA
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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.