Covalently immobilised cytochrome c imaged by in situ scanning tunnelling microscopy

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Publication Details

Author list: Andersen JET, Olesen KG, Danilov AI, Foverskov CE, Moller P, Ulstrup J

Place: LAUSANNE

Publication year: 1997

Journal: BIOELECTROCHEMISTRY AND BIOENERGETICS (0302-4598)

Journal acronym: BIOELECTROCH BIOENER

Volume number: 44

Issue number: 1

Start page: 57

End page: 63

Number of pages: 7

ISSN: 0302-4598

Languages: English-Great Britain (EN-GB)

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Abstract

In situ scanning tunnelling microscopy (STM) imaging of cytochrome c (cyt c) on polycrystalline Pt surfaces and on Au(lll) was achieved first by covalent immobilisation of 3-aminopropyltriethoxysilane (3-APTS) brought to react with oxide present on the Pt surfaces. Covalently bound 3-APTS forms a further link to glutaric dialdehyde which immobilises the protein molecules. Cyt c is immobilised on Au(ll!) by reaction with N-acetylcystein and 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide. Imaging by in situ STM in a 20 mM phosphate buffer electrolyte with a Au/AuOx reference electrode could then be achieved, Protein was identified as hemispherical features on the surface with close to molecular resolution and with a quite different character compared both to the bare metal surfaces and to metal surfaces with only linker molecules attached. No subunits or side chains were visible, but the protein exhibited a grained surface appearance, possibly caused by mobile subunits or immobilising agent. (C) 1997 Elsevier Science S.A.

Keywords

immobilised cytochrome c, ST microscopy

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