Diazonium Functionalisation of Carbon Nanotubes for Specific Orientation of Multicopper Oxidases: Controlling Electron Entry Points and Oxygen Diffusion to the Enzyme

被引：48
作者：
Lalaoui, Noemie [1 ,2 ]
Holzinger, Michael [1 ,2 ]
Le Goff, Alan [1 ,2 ]
Cosnier, Serge [1 ,2 ]
机构：
[1] Univ Grenoble Alpes, DCM UMR 5250, F-38000 Grenoble, France
[2] CNRS, DCM UMR 5250, F-38000 Grenoble, France
来源：
CHEMISTRY-A EUROPEAN JOURNAL | 2016年 / 22卷 / 30期
关键词：
bilirubin oxidases; diazonium; metalloenzymes; nanotubes; oxygen reduction; BILIRUBIN OXIDASE; BIOFUEL CELLS; COPPER CENTERS; REDUCTION; LACCASE; SURFACE; GOLD; IMMOBILIZATION; ASSEMBLIES; GRAPHITE;
D O I：
10.1002/chem.201601377
中图分类号：
O6 [化学];
学科分类号：
0703 ;
摘要：
We report the controlled orientation of bilirubin oxidases (BOD) from Myrothecium verrucaria on multiwalled carbon nanotubes (MWCNTs) functionalised by electrografting of 6-carboxynaphthalenediazonium and 4-(2-aminoethyl)benzenediazonium salts. On negatively charged naphthoate-modified MWCNTs, a high-potential (0.44V vs. SCE) oxygen reduction electrocatalysis is observed, occurring via the T1 copper centre. On positively charged ammonium-modified MWCNTs, a low-potential (0.15V) oxygen reduction electrocatalysis is observed, occurring through a partially oxidised state of the T2/T3 trinuclear copper cluster. Finally, chemically modified naphthoate MWCNTs exhibit high bioelectrocatalytic current densities of 3.9mAcm(-2) under air at gas-diffusion electrode.
引用
收藏
页码：10494 / 10500
页数：7
相关论文
共 45 条
[1]   Improved Performance of Gas-diffusion Biocathode for Oxygen Reduction [J].
Asano, Itaru ;
Hamano, Yasuyuki ;
Tsujimura, Seiya ;
Shirai, Osamu ;
Kano, Kenji .
ELECTROCHEMISTRY, 2012, 80 (05) :324-326
[2]   Highly functionalized carbon nanotubes using in situ generated diazonium compounds [J].
Bahr, JL ;
Tour, JM .
CHEMISTRY OF MATERIALS, 2001, 13 (11) :3823-+
[3]   Enzymatic biofuel cells for Implantable and microscale devices [J].
Barton, SC ;
Gallaway, J ;
Atanassov, P .
CHEMICAL REVIEWS, 2004, 104 (10) :4867-4886
[4]   Efficient electrocatalytic oxygen reduction by the 'blue' copper oxidase, laccase, directly attached to chemically modified carbons [J].
Blanford, Christopher F. ;
Foster, Carina E. ;
Heath, Rachel S. ;
Armstrong, Fraser A. .
FARADAY DISCUSSIONS, 2008, 140 :319-335
[5]   A stable electrode for high-potential, electrocatalytic O2 reduction based on rational attachment of a blue copper oxidase to a graphite surface [J].
Blanford, Christopher F. ;
Heath, Rachel S. ;
Armstrong, Fraser A. .
CHEMICAL COMMUNICATIONS, 2007, (17) :1710-1712
[6]   Supramolecular Immobilization of Laccase on Carbon Nanotube Electrodes Functionalized with (Methylpyrenylaminomethyl)anthraquinone for Direct Electron Reduction of Oxygen [J].
Bourourou, Mariem ;
Elouarzaki, Kamal ;
Lalaoui, Noemie ;
Agnes, Charles ;
Le Goff, Alan ;
Holzinger, Michael ;
Maaref, Abderrazak ;
Cosnier, Serge .
CHEMISTRY-A EUROPEAN JOURNAL, 2013, 19 (28) :9371-9375
[7]   Permselectivity sensitivity, and amperometric pH sensing at thioctic acid monolayer microelectrodes [J].
Cheng, Q ;
BrajterToth, A .
ANALYTICAL CHEMISTRY, 1996, 68 (23) :4180-4185
[8]   Redox potentials of the blue copper sites of bilirubin oxidases [J].
Christenson, Andreas ;
Shleev, Sergey ;
Mano, Nicolas ;
Heller, Adam ;
Gorton, Lo .
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS, 2006, 1757 (12) :1634-1641
[9]   Bilirubin oxidase from Myrothecium verrucaria: X-ray determination of the complete crystal structure and a rational surface modification for enhanced electrocatalytic O2 reduction [J].
Cracknell, James A. ;
McNamara, Thomas P. ;
Lowe, Edward D. ;
Blanford, Christopher F. .
DALTON TRANSACTIONS, 2011, 40 (25) :6668-6675
[10]   Mechanistic studies of the 'blue' Cu enzyme, bilirubin oxidase, as a highly efficient electrocatalyst for the oxygen reduction reaction [J].
dos Santos, Luciano ;
Climent, Victor ;
Blanford, Christopher F. ;
Armstrong, Fraser A. .
PHYSICAL CHEMISTRY CHEMICAL PHYSICS, 2010, 12 (42) :13962-13974
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