A scanning tunnelling microscopy study of Clostridium pasteurianum rubredoxin.
Scanning tunnelling microscopy (STM), which can provide 'direct' and 'non-averaged' information on molecular structure in three dimensions, has been used to achieve sub-molecular resolution in a 'single molecule' of rubredoxin, an important iron-sulphur protein, at the gold (111)/water interface. The metal-ligand site [Fe(III)-Cys4] appears distinct because of an enhancement of the tunnelling current over this region compared to the surrounding protein structure.
Mukhopadhyay
R
R
Department of Chemistry, University of Oxford, UK.
Davis
J J
JJ
Kyritsis
P
P
Hill
H A
HA
Meyer
J
J
D003013:Clostridium / Q000737:chemistry*; D018360:Crystallography, X-Ray; D016252:Microscopy, Scanning Tunneling; D011487:Protein Conformation; D012416:Rubredoxins / Q000737:chemistry*
D012416:Rubredoxins