Active site structure and redox processes of cytochrome c oxidase immobilised in a novel biomimetic lipid membrane on an electrode

文献情報

出版日 2004-09-28

DOI 10.1039/B410998H

インパクトファクター 6.222

著者

Marcel G. Friedrich, Frank Gieβ, Renate Naumann, Wolfgang Knoll, Kenichi Ataka, Joachim Heberle, Jana Hrabakova, Daniel H. Murgida, Peter Hildebrandt

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要旨

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.

掲載誌

Chemical Communications

CiteScore: 8.6

自己引用率: 4.7%

年間論文数: 2458

ChemComm publishes urgent research which is of outstanding significance and interest to experts in the field, while also appealing to the journal’s broad chemistry readership. Our communication format is ideally suited to short, urgent studies that are of such importance that they require accelerated publication. Our scope covers all topics in chemistry, and research at the interface of chemistry and other disciplines (such as materials science, nanoscience, physics, engineering and biology) where there is a significant novelty in the chemistry aspects. Major topic areas covered include: Analytical Chemistry Catalysis Chemical Biology and medicinal chemistry Computational Chemistry and Machine Learning Energy and sustainable chemistry Environmental Chemistry Green Chemistry Inorganic Chemistry Materials Chemistry Nanoscience Organic Chemistry Physical Chemistry Polymer Chemistry Supramolecular Chemistry

Active site structure and redox processes of cytochrome c oxidase immobilised in a novel biomimetic lipid membrane on an electrode

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