TY  - JOUR
AU  - Mayer, D.
AU  - Ataka, K.
AU  - Heberle, J.
AU  - Offenhäusser, A.
TI  - Scanning Probe Microscopic Studies of the Oriented Attachment and Membrane Reconstitution of Cytochrome c Oxidase to a Gold Electrode
JO  - Langmuir
VL  - 21
SN  - 0743-7463
CY  - Washington, DC
PB  - ACS Publ.
M1  - PreJuSER-47540
SP  - 8580 - 8583
PY  - 2005
N1  - Record converted from VDB: 12.11.2012
AB  - 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.
KW  - Electrodes
KW  - Electron Transport Complex IV: chemistry
KW  - Gold: chemistry
KW  - Membranes, Artificial
KW  - Microscopy, Scanning Probe: methods
KW  - Particle Size
KW  - Sensitivity and Specificity
KW  - Surface Properties
KW  - Membranes, Artificial (NLM Chemicals)
KW  - Gold (NLM Chemicals)
KW  - Electron Transport Complex IV (NLM Chemicals)
KW  - J (WoSType)
LB  - PUB:(DE-HGF)16
C6  - pmid:16142929
UR  - <Go to ISI:>//WOS:000231789800004
DO  - DOI:10.1021/la051195x
UR  - https://juser.fz-juelich.de/record/47540
ER  -