Active site structure and redox processes of cytochrome c oxidase immobilised in a novel biomimetic lipid membrane on an electrode.
Membrane-bound cytochrome c oxidase was attached to an electrode via a His-tag linker and studied by surface enhanced resonance Raman spectroscopy, demonstrating intact redox site structures and electron transfer between the electrode and the immobilized enzyme.
Friedrich
Marcel G
MG
Max-Planck-Institut für Polymerforschung, Ackermannweg 10, D-55128 Mainz, Germany.
Giebeta
Frank
F
Naumann
Renate
R
Knoll
Wolfgang
W
Ataka
Kenichi
K
Heberle
Joachim
J
Hrabakova
Jana
J
Murgida
Daniel H
DH
Hildebrandt
Peter
P
D001665:Binding Sites; D040761:Biomimetic Materials / Q000737:chemistry*; D004566:Electrodes; D003576:Electron Transport Complex IV / Q000737:chemistry*; D004800:Enzymes, Immobilized / Q000737:chemistry*; D008563:Membrane Lipids / Q000737:chemistry*; D010084:Oxidation-Reduction; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D012242:Rhodobacter sphaeroides / Q000201:enzymology; D012834:Silver / Q000737:chemistry*; D013499:Surface Properties
D004800:Enzymes, Immobilized; D008563:Membrane Lipids; D012834:Silver; D003576:Electron Transport Complex IV