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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.
Publication status:
Published

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Authors


Mukhopadhyay, R More by this author
More by this author
Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Inorganic Chemistry
Kyritsis, P More by this author
Journal:
Journal of inorganic biochemistry
Volume:
78
Issue:
3
Pages:
251-254
Publication date:
2000-02-05
DOI:
EISSN:
1873-3344
ISSN:
0162-0134
URN:
uuid:2a3dcbd3-1bd9-424c-9d8f-8338af49ee65
Source identifiers:
31672
Local pid:
pubs:31672

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