Graphene oxide-facilitated electron transfer of metalloproteins at electrode surfaces.
Graphene is a particularly useful nanomaterial that has shown great promise in nanoelectronics. Because of the ultrahigh electron mobility of graphene and its unique surface properties such as one-atom thickness and irreversible protein adsorption at surfaces, graphene-based materials might serve as an ideal platform for accommodating proteins and facilitating protein electron transfer. In this work, we demonstrate that graphene oxide (GO) supports the efficient electrical wiring the redox centers of several heme-containing metalloproteins (cytochrome c, myoglobin, and horseradish peroxidase) to the electrode. Importantly, proteins retain their structural intactness and biological activity upon forming mixtures with GO. These important features imply the promising applications of GO/protein complexes in the development of biosensors and biofuel cells.
Zuo
Xiaolei
X
Laboratory of Physical Biology, Shanghai Institute of Applied Physics, Chinese Academy of Sciences, Shanghai 201800, China.
He
Shijiang
S
Li
Di
D
Peng
Cheng
C
Huang
Qing
Q
Song
Shiping
S
Fan
Chunhai
C
D000818:Animals; D045304:Cytochromes c / Q000737:chemistry / Q000378:metabolism; D004563:Electrochemistry; D004566:Electrodes; D004579:Electron Transport; D006108:Graphite / Q000737:chemistry*; D006418:Heme; D006735:Horseradish Peroxidase / Q000737:chemistry / Q000378:metabolism; D008667:Metalloproteins / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D009211:Myoglobin / Q000737:chemistry / Q000378:metabolism; D010087:Oxides / Q000737:chemistry*; D011487:Protein Conformation; D013499:Surface Properties
D008667:Metalloproteins; D009211:Myoglobin; D010087:Oxides; D006418:Heme; D006108:Graphite; D045304:Cytochromes c; D006735:Horseradish Peroxidase