Abstract
Direct electron transfer to cytochrome c oxidase (CcO) is investigated as a function of packing density of the surface layer. This is varied by the surface concentration of chelator molecules when the enzyme is immobilized on the electrode using the his-tag technology. Chelator molecules with a terminal nitrilotriacetic acid group are synthesized ex situ in contrast to in situ synthesis used in a previous work. Self-assembled monolayers of the chelator mixed at different mole fractions with a dilution molecule are prepared to bind the CcO after complex formation with Ni 2+ ions. The CcO, which is immobilized in the solubilized form, is then reconstituted into a protein-tethered bilayer lipid membrane (ptBLM). Varying the mixing ratio of chelator to dilution molecules enabled us to control the packing density of CcO residing in the ptBLM. Subtle differences in the architecture of the protein/lipid layers revealed by surface-enhanced IR absorption spectroscopy are considered to be essential for an effective electron transfer. Cyclic voltammograms are measured under anaerobic conditions at different scan rates and analyzed by means of a model which describes the transfer of four electrons to CcO in the ptBLM. The rate constants thus obtained show a marked dependence on the packing density.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 105-114 |
| Number of pages | 10 |
| Journal | Journal of Solid State Electrochemistry |
| Volume | 15 |
| Issue number | 1 |
| DOIs | |
| State | Published - Jan 1 2011 |
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ASJC Scopus subject areas
- Materials Science(all)
- Condensed Matter Physics
- Electrochemistry
- Electrical and Electronic Engineering
Cite this
Oriented immobilization and electron transfer to the cytochrome c oxidase. / Nowak, Christoph; Schach, Denise; Gebert, Jens; Grosserueschkamp, Marc; Gennis, Robert B.; Ferguson-Miller, Shelagh; Knoll, Wolfgang; Walz, Dieter; Naumann, Renate L.C.
In: Journal of Solid State Electrochemistry, Vol. 15, No. 1, 01.01.2011, p. 105-114.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Oriented immobilization and electron transfer to the cytochrome c oxidase
AU - Nowak, Christoph
AU - Schach, Denise
AU - Gebert, Jens
AU - Grosserueschkamp, Marc
AU - Gennis, Robert B.
AU - Ferguson-Miller, Shelagh
AU - Knoll, Wolfgang
AU - Walz, Dieter
AU - Naumann, Renate L.C.
PY - 2011/1/1
Y1 - 2011/1/1
N2 - Direct electron transfer to cytochrome c oxidase (CcO) is investigated as a function of packing density of the surface layer. This is varied by the surface concentration of chelator molecules when the enzyme is immobilized on the electrode using the his-tag technology. Chelator molecules with a terminal nitrilotriacetic acid group are synthesized ex situ in contrast to in situ synthesis used in a previous work. Self-assembled monolayers of the chelator mixed at different mole fractions with a dilution molecule are prepared to bind the CcO after complex formation with Ni 2+ ions. The CcO, which is immobilized in the solubilized form, is then reconstituted into a protein-tethered bilayer lipid membrane (ptBLM). Varying the mixing ratio of chelator to dilution molecules enabled us to control the packing density of CcO residing in the ptBLM. Subtle differences in the architecture of the protein/lipid layers revealed by surface-enhanced IR absorption spectroscopy are considered to be essential for an effective electron transfer. Cyclic voltammograms are measured under anaerobic conditions at different scan rates and analyzed by means of a model which describes the transfer of four electrons to CcO in the ptBLM. The rate constants thus obtained show a marked dependence on the packing density.
AB - Direct electron transfer to cytochrome c oxidase (CcO) is investigated as a function of packing density of the surface layer. This is varied by the surface concentration of chelator molecules when the enzyme is immobilized on the electrode using the his-tag technology. Chelator molecules with a terminal nitrilotriacetic acid group are synthesized ex situ in contrast to in situ synthesis used in a previous work. Self-assembled monolayers of the chelator mixed at different mole fractions with a dilution molecule are prepared to bind the CcO after complex formation with Ni 2+ ions. The CcO, which is immobilized in the solubilized form, is then reconstituted into a protein-tethered bilayer lipid membrane (ptBLM). Varying the mixing ratio of chelator to dilution molecules enabled us to control the packing density of CcO residing in the ptBLM. Subtle differences in the architecture of the protein/lipid layers revealed by surface-enhanced IR absorption spectroscopy are considered to be essential for an effective electron transfer. Cyclic voltammograms are measured under anaerobic conditions at different scan rates and analyzed by means of a model which describes the transfer of four electrons to CcO in the ptBLM. The rate constants thus obtained show a marked dependence on the packing density.
UR - http://www.scopus.com/inward/record.url?scp=77958099377&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=77958099377&partnerID=8YFLogxK
U2 - 10.1007/s10008-010-1032-x
DO - 10.1007/s10008-010-1032-x
M3 - Article
AN - SCOPUS:77958099377
VL - 15
SP - 105
EP - 114
JO - Journal of Solid State Electrochemistry
JF - Journal of Solid State Electrochemistry
SN - 1432-8488
IS - 1
ER -