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Designing Light‐Activated Charge‐Separating Proteins with a Naphthoquinone Amino Acid
Author(s) -
Lichtenstein Bruce R.,
Bialas Chris,
Cerda José F.,
Fry Bryan A.,
Dutton P. Leslie,
Moser Christopher C.
Publication year - 2015
Publication title -
angewandte chemie
Language(s) - English
Resource type - Journals
eISSN - 1521-3757
pISSN - 0044-8249
DOI - 10.1002/ange.201507094
Subject(s) - quinone , chemistry , semisynthesis , naphthoquinone , histidine , amino acid , tetrapyrrole , redox , cofactor , combinatorial chemistry , stereochemistry , biochemistry , organic chemistry , enzyme
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.