Ordered assembly and controlled electron transfer of the blue copper protein azurin at gold (111) single-crystal substrates
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Author list: Chi QJ, Zhang JD, Andersen JET, Ulstrup J
Publisher: American Chemical Society
Place: WASHINGTON
Publication year: 2001
Journal: Journal of Physical Chemistry B (Soft Condensed Matter and Biophysical Chemistry) (1520-6106)
Journal acronym: J PHYS CHEM B
Volume number: 105
Issue number: 20
Start page: 4669
End page: 4679
Number of pages: 11
ISSN: 1520-6106
eISSN: 1520-5207
Languages: English-Great Britain (EN-GB)
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Abstract
We have shown that Pseudomonas aeruginosa azurin can be immobilized on alkanethiol monolayers self-assembled on Au(111). Immobilization is achieved through hydrophobic interactions between the hydrophobic area around the copper atom in azurin and methyl heads of alkanethiol to form submonolayers or monolayers. In this orientation mode azurin molecules on Au(111) are oriented with the redox center (copper atom) facing the electrode surface. This is opposite to the orientation of azurin on bare gold which is via a surface disulfide group such as recently reported. Scanning tunneling microscopy (STM) with molecular resolution reveals that both well-ordered alkanethiol and protein adlayers are present. Adsorbed azurin molecules exhibit high stability and retain electron transfer (ET) function. Long-range interfacial ET between azurin and Au(111) across variable-length alkanethiol bridges was systematically investigated by different electrochemical techniques. Distance-dependent ET can be controlled by adjusting the length of the alkanethiol chain. The electrochemical ET rate constant is almost independent of the chain length up to ca. 9 methylene units but follows exponential distance decay with a decay factor (beta) of 1.03 +/- 0.02 per CH2 unit at longer chain lengths. Overvoltage-dependent ET was also examined. The results provide a strategy to ordered molecular assemblies, and controlled orientation and ET of azurin at atomically planar metallic surfaces. This approach can in principle be extended to other redox metalloproteins.
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