TY - JOUR
T1 - Reconstitution of apo-glucose oxidase with a nitrospiropyran-modified FAD cofactor yields a photoswitchable biocatalyst for amperometric transduction of recorded optical signals
AU - Willner, Itamar
AU - Blonder, Ron
AU - Katz, Eugenii
AU - Stocker, Achim
AU - Bückmann, Andreas F.
PY - 1996/6/5
Y1 - 1996/6/5
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0030570259&partnerID=8YFLogxK
U2 - 10.1021/ja960228f
DO - 10.1021/ja960228f
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AN - SCOPUS:0030570259
SN - 0002-7863
VL - 118
SP - 5310
EP - 5311
JO - Journal of the American Chemical Society
JF - Journal of the American Chemical Society
IS - 22
ER -