Photo-modulation of horseradish peroxidase activity via covalent attachment of carboxylated-spiropyran dyes.
The photo-modulation of the enzyme horseradish peroxidase modified with photochromic spiropyran dyes is reported. The degree of photo-modulation, greater than 90% reduction in enzyme activity under visible compared to UV illumination, matches the greatest degree of photo-modulation previously reported in the literature. The observation that only a small fraction of the conjugated photochromic molecules are photo-switched suggests that the dyes influence the enzyme activity via local interaction with the enzyme active site.
Weston
D G
DG
Cranfield Biotechnology Centre, Institute of BioScience and Technology, Cranfield University, Cranfield, Bedfordshire MK43 0AL, UK.
Kirkham
J
J
Cullen
D C
DC
D001578:Benzopyrans / Q000737:chemistry*; D001665:Binding Sites; D004396:Coloring Agents / Q000737:chemistry*; D006735:Horseradish Peroxidase / Q000737:chemistry* / Q000528:radiation effects; D007211:Indoles; D009574:Nitro Compounds; D014466:Ultraviolet Rays
D001578:Benzopyrans; D004396:Coloring Agents; D007211:Indoles; D009574:Nitro Compounds; C088184:spiropyran; D006735:Horseradish Peroxidase