Bioluminescence of monolayers of firefly luciferase immobilized on graphite

Stefano Palomba, Nikola Berovic, Richard Palmer

Research output: Contribution to journalArticle

4 Citations (Scopus)


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.
Original languageEnglish
Pages (from-to)5451-5454
Number of pages4
Publication statusPublished - 1 Jan 2006


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