Breaking the barrier to fast electron transfer

Bioelectrochemistry

Volumn 76, Issue 1-2, 2009, Pages 19-27

  Demin, Soren ^a   Hall, Elizabeth A H ^a  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

Author keywords

Enzyme electrochemistry; FAD; Fast electron transfer; Glycosylation

Indexed keywords

ACTIVE SITE; ANAEROBIC CONDITIONS; DIRECT ELECTRON TRANSFER; ELECTROCHEMICAL ELECTRON; ELECTRON TRANSFER; ELECTRON TRANSFER RATES; FAD; FAST ELECTRON TRANSFER; FLAVIN ADENINE DINUCLEOTIDE; GLYCOSYLATED; ORDERS OF MAGNITUDE; OXYGEN INTERACTION; POLYHISTIDINE; PROTON-TRANSFER MECHANISM;

CHARGE TRANSFER; ELECTROCHEMICAL ELECTRODES; ELECTROCHEMISTRY; ELECTRON TRANSITIONS; ENZYMES; ESTERIFICATION; GLYCOSYLATION; ION EXCHANGE; NEUTRON EMISSION; OXYGEN; RATE CONSTANTS;

PROTON TRANSFER;

FLAVINE ADENINE NUCLEOTIDE; GLUCOSE OXIDASE; HISTIDINE; OXYGEN; POLYHISTIDINE TAG;

ANAEROBIC CAPACITY; ARTICLE; CONFORMATIONAL TRANSITION; ELECTRICITY; ELECTROCHEMISTRY; ELECTRODE; ELECTRON TRANSPORT; ENZYME ACTIVE SITE; IMMOBILIZATION; MOLECULAR INTERACTION; OXIDATION REDUCTION REACTION; PROTON TRANSPORT; REACTION TIME;

AMINO ACID SEQUENCE; CATALYTIC DOMAIN; ELECTROCHEMISTRY; ELECTRODES; ELECTRON TRANSPORT; ENZYMES, IMMOBILIZED; FLAVIN-ADENINE DINUCLEOTIDE; GLUCOSE; GLUCOSE OXIDASE; GLYCOSYLATION; HISTIDINE; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; OXYGEN; PROTEIN STRUCTURE, QUATERNARY;

EID: 68549123501     PISSN: 15675394     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bioelechem.2009.03.006     Document Type: Article

References (42)

1. Hecht H.J., Kalisz H.M., and Hendle J. Crystal structure of glucose oxidase from Aspergillus niger refined at 2·3 Å resolution. Journal of Molecular Biology 229 (1993) 153-172
2. Marcus R.A., and Sutin N. Electron transfers in chemistry and biology. Biochimica et Biophysica Acta 811 (1985) 265-322
3. Alvarez-Icaza M., Kalisz H.M., Hecht H.J., Aumann K.D., Schomburg D., and Schmid R.D. The design of enzyme sensors based on the enzyme structure. Biosensors and Bioelectronics 10 (1995) 735-742
4. Liu G., Paddon-Rowand M.N., and Justin Gooding J. A molecular wire modified glassy carbon electrode for achieving direct electron transfer to native glucose oxidase. Electrochemistry Communications 9 (2007) 2218-2223
5. Gorton L., Lindgren A., Larsson T., Munteanu F.D., Ruzgas T., and Gazaryan I. Direct electron transfer between heme-containing enzymes and electrodes as basis for third generation biosensors. Analytica Chimica Acta 400 (1999) 91-108
6. Liu G.Z., and Gooding J.J. An interface comprising molecular wires and poly(ethylene glycol) spacer units self-assembled on carbon electrodes for studies of protein electrochemistry. Langmuir 22 (2006) 7421-7430
7. Lötzbeyer T., Schuhmann W., Katz E., Falter J., and Schmidt H. Direct electron transfer between the covalently immobilized enzyme microperoxidase MP-11 and a cystamine-modified gold electrode. Journal of Electroanalytical Chemistry 377 (1994) 291-294
8. Loechel C., Basran A., Basran J., Scrutton N., and Hall E.A.H. Using trimethylamine dehydrogenase in an enzyme linked amperometric electrode Part 2. Rational design engineering of a 'wired' mutant. The Analyst 128 7 (2003) 889-898
9. Jianjun Wei J.H. Electron-transfer dynamics of cytochrome C: a change in the reaction mechanism with Distance13. Angewandte Chemie International Edition 41 (2002) 4700-4703
10. Cai C., and Chen J. Direct electron transfer of glucose oxidase promoted by carbon nanotubes. Analytical Biochemistry 332 (2004) 75-83
11. Guiseppi-Elie A., Lei C., and Baughman R.H. Direct electron transfer of glucose oxidase on carbon nanotubes. Nanotechnology 13 (2002) 559-564
12. Zhao Y., Zhang W.D., Chen H., Hong L., and Qing-Ming. Direct electron transfer of glucose oxidase molecules adsorbed onto carbon nanotube powder microelectrode. Analytical Sciences 18 (2002) 939-941
13. Cui X.D., Primak A., Zarate X., Tomfohr J., Sankey O.F., Moore A.L., Moore T.A., Gust D., Harris G., and Lindsay S.M. Reproducible measurement of single-molecule conductivity. Science 294 (2001) 571-574
14. Frederick K.R., Tung J., Emerick R.S., Masiarz F.R., Chamberlain S.H., Vasavada S., Rosenberg S., Chakraborty S., Schopter L.M., and Massey V. Glucose oxidase from Aspergillus niger. Cloning, gene sequence, secretion from Saccharomyces cerevisiae and kinetic analysis of a yeast- derived enzyme [published erratum appears in J Biol Chem 265(19),1990 11405]. Journal of Biological Chemistry 265 (1990) 3793-3802
15. Dean N. Asparagine-linked glycosylation in the yeast Golgi. Biochimica et Biophysica Acta 1426 (1999) 309-322
16. Wohlfahrt G., Witt S., Hendle J., Schomburg D., Kalisz D., Hecht H., and Hans-Jurgen H. 1.8 and 1.9 A resolution structures of the Penicillium amagasakiense and Aspergillus niger glucose oxidases as a basis for modelling substrate complexes. Acta Crystallographica Section D 55 (1999) 969-977
17. Fraser D.M., Zakeeruddin S.M., and Grätzel M. Mediation of glycoslated and partially-deglycosylated glucose oxidase of Aspergillus niger by a ferrocene-derivatised detergent. Biochimica et Biophysica Acta 1099 1 (1992) 91-101
18. Kalisz H.M., Hendle J., and Schmid R.D. Structural and biochemical properties of glycosylated and deglycosylated glucose oxidase from Penicillium amagasakiense. Applied Microbiology and Biotechnology 47 5 (1997) 502-507
19. Kohen A.T., Jonsson T., and Klinman J.P. Effects of protein glycosylation on catalysis: changes in hydrogen tunneling and enthalpy of activation in the glucose oxidase reaction. Biochemistry 36 9 (1997) 2603-2611
20. Nakamura S., and Hayashi S. A role of the carbohydrate moiety of glucose oxidase: kinetic evidence for protection of the enzyme from thermal inactivation in the presence of sodium dodecyl sulfate. FEBS Letters 41 2 (1974) 327-330
21. Nakamura S., Hayashi S., and Koga K. Effect of periodate oxidation on the structure and properties of glucose oxidase. Biochimica et Biophysica Acta (BBA) - Enzymology 445 2 (1976) 294-308
22. Binyamin G.T., Chen T., and Heller A. Sources of instability of 'wired' enzyme anodes in serum: urate and transition metal ions. Journal of Electroanalytical Chemistry 500 (2001) 604-611
23. Heller E.J. The many faces of tunneling. J. Phys. Chem. A 103 49 (1999) 10433-10444
24. Fraser D.M., Zakeeruddin S.M., and Gratzel M. Mediation of glycosylated and partially-deglycosylated glucose oxidase of Aspergillus niger by a ferrocene-derivatised detergent. Biochim Biophys Acta 1099 (1992) 91-101
25. Blankespoor R., Limoges B., Schollhorn B., Syssa-Magale J.-L., and Yazidi D. Dense monolayers of metal-chelating ligands covalently attached to carbon electrodes electrochemically and their useful application in affinity binding of histidine-tagged proteins. Langmuir 21 8 (2005) 3362-3375
26. Murata Y., Yano K., Kuroki S., Suzutani T., and Katayama Y. Protein-immobilized electrode for rapid and convenient sensing of thyroid hormone receptor-ligand interaction. Analytical Sciences 19 (2003) 1569
27. Han T., Shibata T., Nakayama M., and Maeda M. A MutS protein-immobilized au electrode for detecting single-base mismatch of DNA. Analytical Sciences 22 5 (2006) 663
28. Ferapontova E.E., Grigorenko V., Egorov V.G., Börchers A.M., Ruzgas T., and Gorton L. Direct electron transfer in the system gold electrode-recombinant horseradish peroxidases. Journal of Electroanalytical Chemistry 509 (2001) 19-26
29. Witt S., Singh M., and Kalisz H.M. Structural and kinetic properties of nonglycosylated recombinant Penicillium amagasakiense glucose oxidase expressed in Escherichia coli. Applied and Environmental Microbiology 64 (1998) 1405-1411
30. Laviron E. Electrochemical reactions with protonations at equilibrium: part VIII. The 2e, 2H+ reaction (nine-member square scheme) for a surface or for a heterogeneous reaction in the absence of disproportionation and dimerization reactions. Journal of Electroanalytical Chemistry 146 (1983) 15-36
31. Trammell S.A., Lowy D., Seferos D., Moore M., Bazan G., and Lebedev N. Heterogeneous electron transfer of quinone-hydroquinone in alkaline solutions at gold electrode surfaces, comparison of saturated and unsaturated bridges. Journal of Electroanalytical Chemistry 606 (2007) 33-38
32. Wohlfahrt G., Trivić S., Zeremski J., Peričin D., and Leskovac V. The chemical mechanism of action of glucose oxidase from Aspergillus niger. Molecular and Cellular Biochemistry 260 (2004) 69-83
33. Haizhen Wei S.O. Interaction of flavin adenine dinucleotide (FAD) with a glassy carbon electrode surface. Chemistry & Biodiversity 5 8 (2008) 1622-1639
34. Laviron E. General expression of the linear potential sweep voltammogram in the case of diffusionless electrochemical systems. Journal of Electroanalytical Chemistry 101 (1979) 19-28
35. Zhihui Wen B.Y. Direct electron transfer reaction of glucose oxidase at bare silver electrodes and its application in analysis. Electroanalysis 9 8 (1997) 641-644
36. Jiang J.C. Elektrochemische Kopplung von Komponenten der Biologischen Elektronentransportkette an Modifizierten Oberflächen: Molekulare Erkennung zwischen cytochrom c-peroxidase und cytochrom c. Angewandte Chemie 107 (1995) 2610
37. Chi Q., Zhang J., Dong S., and Wang E. Direct electrochemistry and surface characterization of glucose oxidase adsorbed on anodized carbon electrodes. Electrochimica Acta 39 (1994) 2431-2438
38. Bhattacharyya S., Stankovich D., and Gao T. Combined quantum mechanical and molecular mechanical simulations of one- and two-electron reduction potentials of flavin cofactor in water, medium-chain acyl-CoA dehydrogenase, and cholesterol oxidase. Journal of Physical Chemistry 111 (2007) 5729-5742
39. Liu J., Paddon-Row M.N., and Gooding J.J. Surface reconstitution of glucose oxidase onto a norbornylogous bridge self-assembled monolayer. Chemical Physics (2007) 216
40. Su Q., and Klinman J.P. Nature of oxygen activation in glucose oxidase from Aspergillus niger: the importance of electrostatic stabilization in superoxide formation. Biochemistry 38 (1999) 8572-8581
41. Nicholson R.S., and Shain I. Theory of stationary electrode polarography. Single scan and cyclic methods applied to reversible, irreversible, and kinetic systems. Analytical Chemistry 36 (1964) 706-723
42. Sandro Ghisla B. On the structure of flavin-oxygen intermediates involved in enzymatic reactions. European Journal of Biochemistry 76 (1977) 139-148