TY - JOUR
T1 - Metalloprotein Adsorption on Au(111) and Polycrystalline Platinum Investigated by In Situ Scanning Tunnelling Microscopy with Molecular and Sub-Molecular Resolution
AU - Friis, Esben P.
AU - Andersen, Jens Enevold Thaulov
AU - Madsen, Lars Lithen
AU - Møller, Per
AU - Nichols, R.J.
AU - Ulstrup, Jens
PY - 1998
Y1 - 1998
N2 - Redox metalloproteins exhibit interesting features such as long-range electron transfer (ET),
cooperative e€ects etc. of importance in relation to fundamental ET theory, and mapped in considerable
detail. Adsorption and interfacial electrochemical ET of metalloproteins at metallic surfaces is also broadly
important in a range of contexts, and has been addressed by spectroscopic, voltammetric, and thermodyn-
amic methods. In situ scanning tunneling (STM) and atomic force microscopy (AFM) have opened new
perspectives for addressing adsorbed metalloproteins in their natural functional aqueous medium at the
molecular level. In addition to broadly recognized problems of in situ STM/AFM imaging, sample prep-
aration, mobility, and adsorbate stability are, however, particular problems. We illustrate here the perspec-
tives by recent in situ STM imaging of covalently bound horse heart cytochrome c on polycrystalline
platinum, and of chemisorbed Pseudomonas aeruginosa azurin on Au(111). Molecular resolution is
achieved, but azurin gives by far the best images which show, moreover, an interesting submolecular fea-
ture. This is likely to be associated with the disulphide group as a natural unit for gentle linking, facile ET
routes through the protein, and tunnel enhancement by the low-lying redox level of the copper atom. The
particular electronic-vibrational three-level con®guration in in situ STM of metalloproteins, ®nally, o€ers a
new way of distinction between superexchange, coherent, and sequential ET modes in the long-range ET
patterns of metalloproteins.
AB - Redox metalloproteins exhibit interesting features such as long-range electron transfer (ET),
cooperative e€ects etc. of importance in relation to fundamental ET theory, and mapped in considerable
detail. Adsorption and interfacial electrochemical ET of metalloproteins at metallic surfaces is also broadly
important in a range of contexts, and has been addressed by spectroscopic, voltammetric, and thermodyn-
amic methods. In situ scanning tunneling (STM) and atomic force microscopy (AFM) have opened new
perspectives for addressing adsorbed metalloproteins in their natural functional aqueous medium at the
molecular level. In addition to broadly recognized problems of in situ STM/AFM imaging, sample prep-
aration, mobility, and adsorbate stability are, however, particular problems. We illustrate here the perspec-
tives by recent in situ STM imaging of covalently bound horse heart cytochrome c on polycrystalline
platinum, and of chemisorbed Pseudomonas aeruginosa azurin on Au(111). Molecular resolution is
achieved, but azurin gives by far the best images which show, moreover, an interesting submolecular fea-
ture. This is likely to be associated with the disulphide group as a natural unit for gentle linking, facile ET
routes through the protein, and tunnel enhancement by the low-lying redox level of the copper atom. The
particular electronic-vibrational three-level con®guration in in situ STM of metalloproteins, ®nally, o€ers a
new way of distinction between superexchange, coherent, and sequential ET modes in the long-range ET
patterns of metalloproteins.
M3 - Journal article
VL - 43
SP - 2889
EP - 2897
JO - Electrochimica Acta
JF - Electrochimica Acta
SN - 0013-4686
IS - 19-20
ER -