Perspectives for in situ scanning tunnel microscopic imaging of metalloproteins at HOPG surfaces

Jens E.T. Andersen, Marianne Hallberg Jensen, Per Møller, Jens Ulstrup

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

We have investigated the behaviour of the four-copper fungal metalloenzyme laccase (MW ≈ 68 kDa) at highly oriented pyrolytic graphite (HOPG) surfaces by ex situ and in situ STM. The four copper atoms are suited to stimulate long-range inelastic tunnel modes through the protein. The protein forms crystalline or amorphous structures of μm lateral extension during evaporation of aqueous laccase solution at low ionic strength. Individual molecular-size structures distinct from the HOPG background, and possibly arising from tip dislodging can also be imaged. The HOPG surface cracks at certain potentials on in situ potentiostatic control and releases nm size HOPG scrap bits. These are clearly different in shape from the ex situ imaged molecular-size structures. Laccase could not, however, be imaged by in situ STM, most likely due to structural incompatibility between the hydrophobic HOPG surface and the strongly negatively charged protein, and to high protein surface mobility.

Original languageEnglish
Pages (from-to)2005-2010
Number of pages6
JournalElectrochimica Acta
Volume41
Issue number13
DOIs
Publication statusPublished - Jan 1 1996

Fingerprint

Metalloproteins
Graphite
Tunnels
Laccase
Scanning
Imaging techniques
Proteins
Copper
Ionic strength
Membrane Proteins
Evaporation
Crystalline materials
Cracks
Atoms

All Science Journal Classification (ASJC) codes

  • Chemical Engineering(all)
  • Electrochemistry

Cite this

Andersen, Jens E.T. ; Jensen, Marianne Hallberg ; Møller, Per ; Ulstrup, Jens. / Perspectives for in situ scanning tunnel microscopic imaging of metalloproteins at HOPG surfaces. In: Electrochimica Acta. 1996 ; Vol. 41, No. 13. pp. 2005-2010.
@article{e8deb7832dbc4d179a1bd61a1b7fa80a,
title = "Perspectives for in situ scanning tunnel microscopic imaging of metalloproteins at HOPG surfaces",
abstract = "We have investigated the behaviour of the four-copper fungal metalloenzyme laccase (MW ≈ 68 kDa) at highly oriented pyrolytic graphite (HOPG) surfaces by ex situ and in situ STM. The four copper atoms are suited to stimulate long-range inelastic tunnel modes through the protein. The protein forms crystalline or amorphous structures of μm lateral extension during evaporation of aqueous laccase solution at low ionic strength. Individual molecular-size structures distinct from the HOPG background, and possibly arising from tip dislodging can also be imaged. The HOPG surface cracks at certain potentials on in situ potentiostatic control and releases nm size HOPG scrap bits. These are clearly different in shape from the ex situ imaged molecular-size structures. Laccase could not, however, be imaged by in situ STM, most likely due to structural incompatibility between the hydrophobic HOPG surface and the strongly negatively charged protein, and to high protein surface mobility.",
author = "Andersen, {Jens E.T.} and Jensen, {Marianne Hallberg} and Per M{\o}ller and Jens Ulstrup",
year = "1996",
month = "1",
day = "1",
doi = "10.1016/0013-4686(96)00005-9",
language = "English",
volume = "41",
pages = "2005--2010",
journal = "Electrochimica Acta",
issn = "0013-4686",
publisher = "Elsevier Limited",
number = "13",

}

Perspectives for in situ scanning tunnel microscopic imaging of metalloproteins at HOPG surfaces. / Andersen, Jens E.T.; Jensen, Marianne Hallberg; Møller, Per; Ulstrup, Jens.

In: Electrochimica Acta, Vol. 41, No. 13, 01.01.1996, p. 2005-2010.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Perspectives for in situ scanning tunnel microscopic imaging of metalloproteins at HOPG surfaces

AU - Andersen, Jens E.T.

AU - Jensen, Marianne Hallberg

AU - Møller, Per

AU - Ulstrup, Jens

PY - 1996/1/1

Y1 - 1996/1/1

N2 - We have investigated the behaviour of the four-copper fungal metalloenzyme laccase (MW ≈ 68 kDa) at highly oriented pyrolytic graphite (HOPG) surfaces by ex situ and in situ STM. The four copper atoms are suited to stimulate long-range inelastic tunnel modes through the protein. The protein forms crystalline or amorphous structures of μm lateral extension during evaporation of aqueous laccase solution at low ionic strength. Individual molecular-size structures distinct from the HOPG background, and possibly arising from tip dislodging can also be imaged. The HOPG surface cracks at certain potentials on in situ potentiostatic control and releases nm size HOPG scrap bits. These are clearly different in shape from the ex situ imaged molecular-size structures. Laccase could not, however, be imaged by in situ STM, most likely due to structural incompatibility between the hydrophobic HOPG surface and the strongly negatively charged protein, and to high protein surface mobility.

AB - We have investigated the behaviour of the four-copper fungal metalloenzyme laccase (MW ≈ 68 kDa) at highly oriented pyrolytic graphite (HOPG) surfaces by ex situ and in situ STM. The four copper atoms are suited to stimulate long-range inelastic tunnel modes through the protein. The protein forms crystalline or amorphous structures of μm lateral extension during evaporation of aqueous laccase solution at low ionic strength. Individual molecular-size structures distinct from the HOPG background, and possibly arising from tip dislodging can also be imaged. The HOPG surface cracks at certain potentials on in situ potentiostatic control and releases nm size HOPG scrap bits. These are clearly different in shape from the ex situ imaged molecular-size structures. Laccase could not, however, be imaged by in situ STM, most likely due to structural incompatibility between the hydrophobic HOPG surface and the strongly negatively charged protein, and to high protein surface mobility.

UR - http://www.scopus.com/inward/record.url?scp=0030212308&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0030212308&partnerID=8YFLogxK

U2 - 10.1016/0013-4686(96)00005-9

DO - 10.1016/0013-4686(96)00005-9

M3 - Article

VL - 41

SP - 2005

EP - 2010

JO - Electrochimica Acta

JF - Electrochimica Acta

SN - 0013-4686

IS - 13

ER -