title: A scanning tunnelling microscopy study of Clostridium pasteurianum rubredoxin.
abstract: 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.
authors.affiliation: Department of Chemistry, University of Oxford, UK.
authors.forename: R
authors.initials: R
authors.lastname: Mukhopadhyay
authors.forename: J J
authors.initials: JJ
authors.lastname: Davis
authors.forename: P
authors.initials: P
authors.lastname: Kyritsis
authors.forename: H A
authors.initials: HA
authors.lastname: Hill
authors.forename: J
authors.initials: J
authors.lastname: Meyer
mesh_terms: D003013:Clostridium / Q000737:chemistry*; D018360:Crystallography, X-Ray; D016252:Microscopy, Scanning Tunneling; D011487:Protein Conformation; D012416:Rubredoxins / Q000737:chemistry*
chemical_list: D012416:Rubredoxins