Reconstitution of apo-glucose oxidase with a nitrospiropyran-modified FAD cofactor yields a photoswitchable biocatalyst for amperometric transduction of recorded optical signals

Itamar Willner, Ron Blonder, Eugenii Katz, Achim Stocker, Andreas F. Bückmann

Research output: Contribution to journalArticlepeer-review

54 Scopus citations

Abstract

Here we wish to report on a novel method to tailor photoswitchable redox biocatalysts by reconstitution of apo-flavoenzymes with a nitrospiropyran modified flavin adenine dinucleotide, FAD, cofactor. We demonstrate a novel method a organize photoswitchable redox proteins for amperometric transduction of optical signals. The method consists of reconstitution of a flavo-apoenzyme, apo-GOD, with a synthetic FAD analog modified by a nitrospiropyran photosiomerizable unit. The protein implanted photoisomerizable group delicately controls the protein structure in the FAD cofactor surrounding. The site-specific modification of the enzyme by the photoisomerizable units through the application of the reconstitution methodology reconstitution methodology represents a major advance in designing photoswitchable enzymes. It enables further structural characterization of the biocatalyst and elucidation of the steric perturbations of the protein stimulated by photoisomerizable components.

Original languageEnglish
Pages (from-to)5310-5311
Number of pages2
JournalJournal of the American Chemical Society
Volume118
Issue number22
DOIs
StatePublished - 5 Jun 1996

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