This title appears in the Scientific Report :
2005
Please use the identifier:
http://hdl.handle.net/2128/2123 in citations.
Please use the identifier: http://dx.doi.org/10.1021/la051195x in citations.
Scanning Probe Microscopic Studies of the Oriented Attachment and Membrane Reconstitution of Cytochrome c Oxidase to a Gold Electrode
Scanning Probe Microscopic Studies of the Oriented Attachment and Membrane Reconstitution of Cytochrome c Oxidase to a Gold Electrode
Scanning probe microscopy was used to monitor the resulting surface of the oriented incorporation of cytochrome c oxidase into electrode supported lipid bilayer at four crucial stages with molecular resolution. We were able to reveal the formation of a densely packed monolayer of the active ester di...
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Personal Name(s): | Mayer, D. |
---|---|
Ataka, K. / Heberle, J. / Offenhäusser, A. | |
Contributing Institute: |
Center of Nanoelectronic Systems for Information Technology; CNI Biologische Strukturforschung; IBI-2 Institut für Bio- und Chemosensoren; ISG-2 |
Published in: | Langmuir, 21 (2005) S. 8580 - 8583 |
Imprint: |
Washington, DC
ACS Publ.
2005
|
Physical Description: |
8580 - 8583 |
PubMed ID: |
16142929 |
DOI: |
10.1021/la051195x |
Document Type: |
Journal Article |
Research Program: |
Neurowissenschaften Materialien, Prozesse und Bauelemente für die Mikro- und Nanoelektronik |
Series Title: |
Langmuir
21 |
Subject (ZB): | |
Link: |
Get full text OpenAccess |
Publikationsportal JuSER |
Please use the identifier: http://dx.doi.org/10.1021/la051195x in citations.
Scanning probe microscopy was used to monitor the resulting surface of the oriented incorporation of cytochrome c oxidase into electrode supported lipid bilayer at four crucial stages with molecular resolution. We were able to reveal the formation of a densely packed monolayer of the active ester dithio(succiniimidylepropionate) (DTSP) and the covalent linkage of the nitrilotriacetic acid (NTA) to the thiol anchored DTSP by scanning tunneling microscopy. Atomic force microscopy investigations showed that the detergent solubilized oxidase is immobilized as monomers and small aggregates via histidine residues. Finally, the reconstitution of the proteins within the supported membrane was verified. The amount of oxidase immobilized within the solid supported membrane was estimated. |