Observation of photoactive yellow protein anchored to a modified Au(111) surface by scanning tunneling microscopy

Rzeznicka II; Wurpel GWH; Bonn M; van der Horst MA; Hellingwerf KJ; Matsunaga S; Yamada T; Kawai M

Chemical Physics Letters, Vol.472, No.1-3, 113-117, 2009

DOI10.1016/j.cplett.2009.02.067 Export Citation

Observation of photoactive yellow protein anchored to a modified Au(111) surface by scanning tunneling microscopy

Rzeznicka II, Wurpel GWH, Bonn M, van der Horst MA, Hellingwerf KJ, Matsunaga S, Yamada T, Kawai M

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. (C) 2009 Elsevier B. V. All rights reserved.