Nickel electrodes as a cheap and versatile platform for studying structure and function of immobilized redox proteins.
Practical use of many bioelectronic and bioanalytical devices is limited by the need of expensive materials and time consuming fabrication. Here we demonstrate the use of nickel electrodes as a simple and cheap solid support material for bioelectronic applications. The naturally nanostructured electrodes showed a surprisingly high electromagnetic surface enhancement upon light illumination such that immobilization and electron transfer reactions of the model redox proteins cytochrome b5(Cyt b5) and cytochrome c (Cyt c) could be followed via surface enhanced resonance Raman spectroscopy. It could be shown that the nickel surface, when used as received, promotes a very efficient binding of the proteins upon preservation of their native structure. The immobilized redox proteins could efficiently exchange electrons with the electrode and could even act as an electron relay between the electrode and solubilized myoglobin. Our results open up new possibility for nickel electrodes as an exceptional good support for bioelectronic devices and biosensors on the one hand and for surface enhanced spectroscopic investigations on the other hand.
State Key Laboratory of Supramolecular Structure and Materials, Jilin University, 2699 Qianjin Street, Changchun 130012, PR China; Institut für Chemie, Technische Universität Berlin, Sekr. PC14, Strasse des 17. Juni 135, D-10623 Berlin, Germany.
Xiao Xia
XX
Han
State Key Laboratory of Supramolecular Structure and Materials, Jilin University, 2699 Qianjin Street, Changchun 130012, PR China.
Junbo
J
Li
Institut für Chemie, Technische Universität Berlin, Sekr. PC14, Strasse des 17. Juni 135, D-10623 Berlin, Germany.
Ibrahim Halil
IH
Öner
State Key Laboratory of Supramolecular Structure and Materials, Jilin University, 2699 Qianjin Street, Changchun 130012, PR China.
Bing
B
Zhao
Institut für Biochemie und Biologie, Universität Potsdam, Karl-Liebknecht Straße 24-25, H. 25, Golm D-14476, Germany.
Silke
S
Leimkühler
Institut für Chemie, Technische Universität Berlin, Sekr. PC14, Strasse des 17. Juni 135, D-10623 Berlin, Germany.
Peter
P
Hildebrandt
Institut für Chemie, Technische Universität Berlin, Sekr. PC14, Strasse des 17. Juni 135, D-10623 Berlin, Germany. Electronic address: i.weidinger@mailbox.tu-berlin.de.
Inez M
IM
Weidinger
D000818:Animals; D003365:Costs and Cost Analysis; D015786:Cytochromes b5 / Q000737:chemistry / Q000378:metabolism; D004566:Electrodes; D006801:Humans; D055767:Immobilized Proteins / Q000737:chemistry* / Q000378:metabolism*; D008958:Models, Molecular; D009211:Myoglobin / Q000737:chemistry / Q000378:metabolism; D009532:Nickel / Q000737:chemistry*; D010084:Oxidation-Reduction; D011487:Protein Conformation; D013059:Spectrum Analysis, Raman / Q000295:instrumentation*; D013499:Surface Properties
D055767:Immobilized Proteins; D009211:Myoglobin; D009532:Nickel; D015786:Cytochromes b5
Biocompatibility; Electron relay; Electron transfer; Ni electrodes; Redox proteins; Surface enhanced Raman spectroscopy