confocal fluorescence spectroscopy on Rhodamine 6G
| USAGE | Scientific publication |
| CLIENT | Peter Schon, MTP Group, University of Twente |
| YEAR | 2013 |
This figure is shows catalysis oxidation of the dihydrorhodamine 6G into rhodamine 6G by the enzyme horseradish peroxidase. The reaction is monitored by confocal fluorescence spectroscopy. Hence, direct observation of successive single substrate turnovers into product is made possible by means of fluorescence microscopy if a single enzyme molecule is observed. Furthermore an electric potential activates the catalysis process.
