| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1310280 | Inorganica Chimica Acta | 2008 | 6 Pages |
Abstract
Type-3 copper proteins like tyrosinase (Ty) and hemocyanin (Hc) contain a dinuclear active Cu site that binds di-oxygen reversibly. The binding can be detected by fluorescence spectroscopy. Immobilization of the proteins (Ty and Hc) in a sol-gel matrix stabilizes them and does not affect their oxygen binding capacity. This finding is an important step towards the realisation of a sensitive and robust oxygen sensor.
Keywords
Related Topics
Physical Sciences and Engineering
Chemistry
Inorganic Chemistry
Authors
Gerhild Zauner, Maria Strianese, Luigi Bubacco, Thijs J. Aartsma, Armand W.J.W. Tepper, Gerard W. Canters,