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Design and synthesis of multi-haem proteins

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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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Authors and Affiliations

  1. Johnson Research Foundation, Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia, Pennsylvania, 19104, USA

    Dan E. Robertson, Ramy S. Farid, Christopher C. Moser, Stephen E. Mulholland, Ravindernath Pidikiti, William F. DeGrado & P. Leslie Dutton

  2. Department of Biochemistry, School of Chemical Sciences, University of Illinois at Urbana-Champaign, 600 S. Matthews Street, Urbana, Illinois, 61801, USA

    Jeffrey L. Urbauer & A. Joshua Wand

  3. E. I. du Pont de Nemours Co., Central Research and Development Department, PO Box 80328, Wilmington, Delaware, 19880, USA

    James D. Lear & William F. DeGrado

Authors
  1. Dan E. Robertson
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  2. Ramy S. Farid
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  3. Christopher C. Moser
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  4. Jeffrey L. Urbauer
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  5. Stephen E. Mulholland
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  6. Ravindernath Pidikiti
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  7. James D. Lear
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  8. A. Joshua Wand
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  9. William F. DeGrado
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  10. P. Leslie Dutton
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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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  • DOI: https://doi.org/10.1038/368425a0

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