Designing light-activated charge-separating proteins with a naphthoquinone amino acid

Bruce R. Lichtenstein, Chris Bialas, José F. Cerda, Bryan A. Fry, P. Leslie Dutton, Christopher C. Moser

Research output: Contribution to journalArticlepeer-review

Abstract

The first principles design of manmade redox-protein maquettes is used to clarify the physical/chemical engineering supporting the mechanisms of natural enzymes with a view to recapitulate and surpass natural performance. Herein, we use intein-based protein semisynthesis to pair a synthetic naphthoquinone amino acid (Naq) with histidine-ligated photoactive metal-tetrapyrrole cofactors, creating a 100 μs photochemical charge separation unit akin to photosynthetic reaction centers. By using propargyl groups to protect the redox-active para-quinone during synthesis and assembly while permitting selective activation, we gain the ability to employ the quinone amino acid redox cofactor with the full set of natural amino acids in protein design. Direct anchoring of quinone to the protein backbone permits secure and adaptable control of intraprotein electron-tunneling distances and rates.

Original languageEnglish
Pages (from-to)13626-13629
Number of pages4
JournalAngewandte Chemie - International Edition
Volume54
Issue number46
Early online date14 Sep 2015
DOIs
Publication statusPublished - 9 Nov 2015

Keywords

  • amino acids
  • electron transfer
  • photosynthesis
  • protein engineering
  • quinones

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