Characterization of the Electron Transfer of a Ferrocene Redox Probe and a Histidine-Tagged Hemoprotein Specifically Bound to a Nitrilotriacetic-Terminated Self-Assembled Monolayer-Reference-Cited by-同舟云学术

Characterization of the Electron Transfer of a Ferrocene Redox Probe and a Histidine-Tagged Hemoprotein Specifically Bound to a Nitrilotriacetic-Terminated Self-Assembled Monolayer

Published:2009-05-06 Issue:11 Volume:25 Page:6532-6542
ISSN:0743-7463
Container-title:Langmuir
language:en
Short-container-title:Langmuir

Author:

Balland Véronique¹,Lecomte Sophie²,Limoges Benoît¹

Affiliation:

1. Laboratoire d’Electrochimie Moléculaire, Université Paris Diderot, UMR CNRS 7591, 15 rue Jean-Antoine de Baïf, 75205 Paris Cedex 13, France

2. Chimie Biologie des Membranes et Nano-objets, Université Bordeaux 1, UMR CNRS 5248, 2 rue Robert d’Escarpit, 33607 Pessac, France

Publisher

American Chemical Society (ACS)

Subject

Electrochemistry,Spectroscopy,Surfaces and Interfaces,Condensed Matter Physics,General Materials Science

Link

https://pubs.acs.org/doi/pdf/10.1021/la900062y

Reference75 articles.

1. Direct Electrochemistry of Redox Enzymes as a Tool for Mechanistic Studies

2. Integration of Layered Redox Proteins and Conductive Supports for Bioelectronic Applications

3. Electron-transfer kinetics in organized thiol monolayers with attached pentaammine(pyridine)ruthenium redox centers

4. Ferrocene-mediated enzyme electrode for amperometric determination of glucose

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