The adsorption of photoactive yellow protein (PYP) on a Au(111) surface and its fluorescence activity have been studied by electrochemical scanning tunneling microscopy (EC-STM) and. uorescence photometry. A stable, densely packed protein layer was observed after protein immobilization onto a Au(111) surface modified with a mixture of 3-mercaptopropanoic acid (3-MPA) and 11-mercaptoundecanoic acid (11-MUA) and subsequent formation of the amide bond with the use of N-hydroxysuccinimide and carbodiimide. Fluorescence photometry data indicate that covalent binding of PYP to the functionalized Au(111) surface does not interfere with the. uorescence properties of the native protein.

Additional Metadata
Persistent URL dx.doi.org/10.1016/j.cplett.2009.02.067
Journal Chem. Phys. Lett.
Citation
Rzeznicka, I. I, Wurpel, G. W. H, Bonn, M, van der Horst, M. A, Hellingwerf, K. J, Matsunaga, S, … Kawai, M. (2009). Observation of photoactive yellow protein anchored to a modified Au(111) surface by scanning tunneling microscopy. Chem. Phys. Lett., 472, 113–117. doi:10.1016/j.cplett.2009.02.067