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      Design and synthesis of multi-haem proteins.

      Nature

      Amino Acid Sequence, Drug Design, Electrochemistry, Electron Transport Complex III, chemical synthesis, chemistry, Hemeproteins, Models, Molecular, Molecular Sequence Data, Oxidation-Reduction, Protein Conformation, Protein Structure, Secondary, Spectrum Analysis

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          Abstract

          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.

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          Author and article information

          Journal
          8133888
          10.1038/368425a0

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