期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 128, 期 5, 页码 1711-1716出版社
AMER CHEMICAL SOC
DOI: 10.1021/ja056972u
关键词
-
资金
- Biotechnology and Biological Sciences Research Council [JF19090] Funding Source: researchfish
- Engineering and Physical Sciences Research Council [EP/C006755/1] Funding Source: researchfish
- Biotechnology and Biological Sciences Research Council [JF19090] Funding Source: Medline
An electrode surface is presented that enables the characterization of redox-active membrane enzymes in a native-like environment. An ubiquinol oxidase from Escherichia coli, cytochrome bo(3) (cbo(3)), has been co-immobilized into tethered bilayer lipid membranes (tBLMs). The tBLM is formed on gold surfaces functionalized with cholesterol tethers which insert into the lower leaflet of the membrane. The planar membrane architecture is formed by self-assembly of proteoliposomes, and its structure is characterized by surface plasmon resonance (SPR), electrochemical impedance spectroscopy (EIS), and tapping-mode atomic force microscopy (TM-AFM). The functionality of cbo(3) is investigated by cyclic voltammetry (CV) and is confirmed by the catalytic reduction of oxygen. Interfacial electron transfer to cbo(3) is mediated by the membrane-localized ubiquinol-8, the physiological electron donor of cbo(3). Enzyme coverages observed with TM-AFM and CV coincide (2-8.5 fmol(.)cm(-2)), indicating that most-if not all-cbo(3) on the surface is catalytically active and thus retains its integrity during immobilization.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据