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Nat Chem Biol. 2013 Dec;9(12):826-833. doi: 10.1038/nchembio.1362. Epub 2013 Oct 13.

Elementary tetrahelical protein design for diverse oxidoreductase functions.

Author information

Department of Biochemistry and Biophysics, Johnson Research Foundation, University of Pennsylvania, Philadelphia, Pennsylvania, USA.
Max Planck Institute for Developmental Biology, Tübingen, Germany.
School of Biochemistry, University of Bristol, Bristol, UK.
Contributed equally

Erratum in

  • Nat Chem Biol. 2013 Dec;9(12): following 833.
  • Nat Chem Biol. 2014 Feb;10(2):164.


Emulating functions of natural enzymes in man-made constructs has proven challenging. Here we describe a man-made protein platform that reproduces many of the diverse functions of natural oxidoreductases without importing the complex and obscure interactions common to natural proteins. Our design is founded on an elementary, structurally stable 4-α-helix protein monomer with a minimalist interior malleable enough to accommodate various light- and redox-active cofactors and with an exterior tolerating extensive charge patterning for modulation of redox cofactor potentials and environmental interactions. Despite its modest size, the construct offers several independent domains for functional engineering that targets diverse natural activities, including dioxygen binding and superoxide and peroxide generation, interprotein electron transfer to natural cytochrome c and light-activated intraprotein energy transfer and charge separation approximating the core reactions of photosynthesis, cryptochrome and photolyase. The highly stable, readily expressible and biocompatible characteristics of these open-ended designs promise development of practical in vitro and in vivo applications.

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