Bioluminescence of monolayers of firefly luciferase immobilized on graphite
We report on the immobilization of the firefly protein luciferase on the hydrophobic surface of graphite. Observation by liquid-phase atomic force microscopy of islands with a height consistent with the size of a single molecule confirmed that the protein was contained within a monomolecular layer....
| Veröffentlicht in: | Langmuir : the ACS journal of surfaces and colloids. - 1992. - 22(2006), 12 vom: 06. Juni, Seite 5451-4 |
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| Weitere Verfasser: | , |
| Format: | Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2006
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| Zugriff auf das übergeordnete Werk: | Langmuir : the ACS journal of surfaces and colloids |
| Schlagworte: | Journal Article Research Support, Non-U.S. Gov't Enzymes, Immobilized Firefly Luciferin 5TBB02N29K Graphite 7782-42-5 Adenosine Triphosphate 8L70Q75FXE Luciferases, Firefly |
| Zusammenfassung: | We report on the immobilization of the firefly protein luciferase on the hydrophobic surface of graphite. Observation by liquid-phase atomic force microscopy of islands with a height consistent with the size of a single molecule confirmed that the protein was contained within a monomolecular layer. The enzyme activity was assayed by single-photon counting of the bioluminescence, which is the catalytic product of luciferase. Attachment to the surface modified the efficiency of the enzyme, but the introduction of the substrates luciferin and ATP resulted in the reactivation of the enzyme. The functionalized graphite surface was employed as a cathode in a bioelectrochemical cell. This demonstrated that the electric field caused a substantial loss of enzyme catalytic activity |
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| Beschreibung: | Date Completed 24.07.2007 Date Revised 21.11.2013 published: Print Citation Status MEDLINE |
| ISSN: | 1520-5827 |