Direct Electron Transfer to a Metalloenzyme Redox Center Coordinated to a Monolayer-Protected Cluster

被引:57
作者
Abad, Jose M. [1 ]
Gass, Mhairi [2 ]
Bleloch, Andrew [2 ]
Schiffrin, David J. [1 ]
机构
[1] Univ Liverpool, Dept Chem, Liverpool L69 7ZD, Merseyside, England
[2] UK SuperSTEM, Daresbury Lab, Daresbury WA4 4AD, Cheshire, England
关键词
GALACTOSE-OXIDASE; ACTIVE-SITE; GOLD NANOPARTICLES; ORIENTED IMMOBILIZATION; DIRECT ELECTROCHEMISTRY; HYBRID SYSTEMS; PROTEINS; OXIDATION; INTERCONVERSION; TRYPTOPHAN;
D O I
10.1021/ja9026693
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
A strategy for establishing electrical contact to the metal center of a redox metalloenzyme, galactose oxidase (GOase), by coordination of a linker attached to a monolayer-protected gold cluster is presented. The cluster-enzyme hybrid system was first prepared in solution and characterized by high-angle annular dark-field scanning transmission electron microscopy. Electrochemical communication between a gold electrode and GOase was achieved by first modifying the electrode surface with a biphenyl dithiol self-assembled monolayer followed by reaction with gold clusters capped with thioctic acid. GOase was then immobilized by replacement of the H2O Molecule at the Cull exogenous site by coordination of a carboxylate-terminated gold cluster. This chemical attachment ensured electrical contact between the redox center and the electrode, leading to direct mediatorless electron transfer to the protein. Hybrid systems can find applications in biosensors and biofuel cells and for studying electrochemically the catalytic mechanism of reactions for which free radicals and electron-transfer reactions are involved. The present results can be extended to other metalloenzymes.
引用
收藏
页码:10229 / 10236
页数:8
相关论文
共 80 条
[41]   ELECTROCHEMICAL STUDY OF GOLD ELECTRODES WITH ANODIC OXIDE-FILMS .1. FORMATION AND REDUCTION BEHAVIOR OF ANODIC OXIDES ON GOLD [J].
OESCH, U ;
JANATA, J .
ELECTROCHIMICA ACTA, 1983, 28 (09) :1237-1246
[42]   Immobilization of protein molecules onto homogeneous and mixed carboxylate-terminated self-assembled monolayers [J].
Patel, N ;
Davies, MC ;
Hartshorne, M ;
Heaton, RJ ;
Roberts, CJ ;
Tendler, SJB ;
Williams, PM .
LANGMUIR, 1997, 13 (24) :6485-6490
[43]   Direct Electrochemistry of Laccase Immobilized on Au Nanoparticles Encapsulated-Dendrimer Bonded Conducting Polymer: Application for a Catechin Sensor [J].
Rahman, Md. Aminur ;
Noh, Hui-Bog ;
Shim, Yoon-Bo .
ANALYTICAL CHEMISTRY, 2008, 80 (21) :8020-8027
[44]   The stacking tryptophan of galactose oxidase: A second-coordination sphere residue that has profound effects on tyrosyl radical behavior and enzyme catalysis [J].
Rogers, Melanie S. ;
Tyler, Ejan M. ;
Akyumani, Nana ;
Kurtis, Christian R. ;
Spooner, R. Kate ;
Deacon, Sarah E. ;
Tamber, Sarita ;
Firbank, Susan J. ;
Mahmoud, Khaled ;
Knowles, Peter F. ;
Phillips, Simon E. V. ;
McPherson, Michael J. ;
Dooley, David M. .
BIOCHEMISTRY, 2007, 46 (15) :4606-4618
[45]   Copper-tyrosyl radical enzymes [J].
Rogers, MS ;
Dooley, DM .
CURRENT OPINION IN CHEMICAL BIOLOGY, 2003, 7 (02) :189-196
[46]   A comparative study of galactose oxidase and active site analogs based on QM/MM Car Parrinello simulations [J].
Rothlisberger, U ;
Carloni, P ;
Doclo, K ;
Parrinello, M .
JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY, 2000, 5 (02) :236-250
[47]   Oriented immobilization of Desulfovibrio gigas hydrogenase onto carbon electrodes by covalent bonds for nonmediated oxidation of H2 [J].
Rüdiger, O ;
Abad, JM ;
Hatchikian, EC ;
Fernandez, VM ;
De Lacey, AL .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2005, 127 (46) :16008-16009
[48]   The cupric geometry of blue copper proteins is not strained [J].
Ryde, U ;
Olsson, MHM ;
Pierloot, K ;
Roos, BO .
JOURNAL OF MOLECULAR BIOLOGY, 1996, 261 (04) :586-596
[49]   Electrochemical modification of glassy carbon electrode using aromatic diazonium salts .1. Blocking effect of 4-nitrophenyl and 4-carboxyphenyl groups [J].
Saby, C ;
Ortiz, B ;
Champagne, GY ;
Belanger, D .
LANGMUIR, 1997, 13 (25) :6805-6813
[50]   Kinetic studies on the redox interconversion of GOase(semi) and GOase(ox) forms of galactose oxidase with inorganic complexes as redox partners [J].
Saysell, CG ;
Borman, CD ;
Baron, AJ ;
McPherson, MJ ;
Sykes, AG .
INORGANIC CHEMISTRY, 1997, 36 (20) :4520-4525