Direct Electrochemistry of Proteins and Enzymes

Perspectives in Bioanalysis

Volumn 1, Issue C, 2005, Pages 517-598

  Ferapontova, Elena E ^a,b   Shleev, Sergey ^a,c   Ruzgas, Tautgirdas ^d   Stoica, Leonard ^a   Christenson, Andreas ^a   Tkac, Jan ^a   Yaropolov, Alexander I ^c   Gorton, Lo ^a  

^a LUND UNIVERSITY   (Sweden)

^b Novosibirsk IT Center   (Russian Federation)

^c BACH INSTITUTE OF BIOCHEMISTRY   (Russian Federation)

^d MALMÖ UNIVERSITY   (Sweden)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 77956710810     PISSN: 18710069     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1871-0069(05)01016-5     Document Type: Article

References (469)

1. Adman E.T., Stenkamp R.E., Sieker L.C., and Jensen L.H. A crystallographic model for azurin at 3 Å resolution. J. Mol. Biol. 123 (1978) 35-47
2. Agostinelli E., Cervoni L., Giartosio A., and Morpurgo L. Stability of Japanese-lacquer-tree (Rhus vernicifera) laccase to thermal and chemical denaturation: Comparison with ascorbate oxidase. Biochem. J. 306 (1995) 697-702
3. Aguey-Zinsou K.-F., Bernhardt P.V., Kappler U., and McEwan A.G. Direct electrochemistry of a bacterial sulfite dehydrogenase. J. Am. Chem. Soc. 125 (2003) 530-535
4. Aizawa M. Principles and applications of electrochemical and optical biosensors. Anal. Chim. Acta 250 (1991) 249-256
5. Albery W.J., Eddowes M.J., Hill H.A.O., and Hillman A.R. Mechanism of the reduction and oxidation reaction of cytochrome c at a modified gold electrode. J. Am. Chem. Soc. 103 (1981) 3904-3910
6. Allendorf M.D., Spira D.J., and Solomon E.I. Low-temperature magnetic circular dichroism studies of native laccase: Spectroscopic evidence for exogenous ligand bridging at a trinuclear copper active site. Proc. Natl. Acad. Sci. USA 82 (1985) 3063-3067
7. Ameyama M., Shinagawa E., Matsushita K., and Adachi O. d-Fructose dehydrogenase of Gluconobacter industrius: Purification, characterization, and application to enzymic microdetermination of d-fructose. J. Bacteriol. 145 (1981) 814-823
8. Amine A., Deni J., and Kauffmann J.-M. Amperometric biosensor based on carbon paste mixed with enzyme, lipid and cytochrome c. Bioelectrochem. Bioenerg. 34 (1994) 123-128
9. Amiot, P.L.O., S. Howell, P.D. Lee and H. Rieley, 2001, Apparatus and method for sensing metal ions, UK, WO 2001006235.
10. Ander P. The cellobiose-oxidizing enzymes CBQ and CbO as related to lignin and cellulose degradation - a review. FEMS Microbiol. Rev. 13 (1994) 297-312
11. Andolfi L., Bruce D., Cannistraro S., Canters G.W., Davis J.J., Hill H.A.O., Crozier J., Verbeet M.P., Wrathmell C.L., and Astier Y. The electrochemical characteristics of blue copper protein monolayers on gold. J. Electroanal. Chem. 565 (2004) 21-28
12. Andreescu, D., S. Andreescu and O.A. Sadik, 2005, New materials for biosensors, biochips and molecular bioelectronics. Biosensors and Modern Biospecific Analytical Techniques, Vol. XLIV, Ed. L. Gorton, Elsevier, Amsterdam, pp. 285-327.
13. Angove H.C., Cole J.A., Richardson D.J., and Butt J.N. Protein film voltammetry reveals distinctive fingerprints of nitrite and hydroxylamine reduction by a cytochrome c nitrite reductase. J. Biol. Chem. 277 (2002) 23374-23381
14. Anthony C. Bacterial Energy Transduction (1988), Academic Press, San Diego
15. Antorini M., Herpoel-Gimbert I., Choinowski T., Sigoillot J.-G., Asther M., Winterhalter K., and Piontek K. Purification, crystallisation and X-ray diffraction study of fully functional laccases from two ligninolytic fungi. Biochim. Biophys. Acta 1594 (2002) 109-114
16. Armstrong F.A. Probing metalloproteins by voltammetry. Struct. Bond. 72 (1990) 137-221
17. Armstrong F.A. Protein film voltammetry: Revealing the mechanisms of biological oxidation and reduction. Russ. J. Electrochem. 38 (2002) 49-62
18. Armstrong, F.A., N.L. Barlow, P.L. Burn, K.R. Hoke, L.J.C. Jeuken, C. Shenton and G. R. Webster, 2004, Fast, long-range electron-transfer reactions of a "blue" copper protein coupled non-covalently to an electrode through a stilbenyl thiolate monolayer, Chem. Commun. (UK), 316-317.
19. Armstrong F.A., Hill H.A.O., Oliver B.N., and Walton N.J. Direct electrochemistry of redox proteins at pyrolytic graphite electrodes. J. Am. Chem. Soc. 106 (1984) 921-923
20. Armstrong F.A., Hill H.A.O., and Walton N.J. Direct electrochemistry of redox proteins. Acc. Chem. Res. 21 (1988) 407-413
21. 2 reduction. J. Am. Chem. Soc. 109 (1987) 7211-7212
22. Arnold S., Feng Z.Q., Kakiuchi T., Knoll W., and Niki K. Investigation of the electrode reaction of cytochrome c through mixed self-assembled monolayers of alkanethiols on gold (1 1 1) surfaces. J. Electroanal. Chem. 438 (1997) 91-97
23. Avigliano L., Vecchini P., Sirianni P., Marcozzi G., Marchesini A., and Mondovi B. A reinvestigation on the quaternary structure of ascorbate oxidase from Cucurbita pepo medullosa. Mol. Cell. Biochem. 56 (1983) 107-112
24. Ayers A.R., Ayers S.B., and Eriksson K.-E. Cellobiose oxidase, purification and partial characterizarion of a hemoprotein from Sporotrichum pulverulentum. Eur. J. Biochem. 90 (1978) 171-181
25. Baeumner, A., 2005, Bioanalytical microsystems: Technology and applications. Biosensors and Modern Biospecific Analytical Techniques, Vol. XLIV, Ed. L. Gorton, Elsevier, Amsterdam, pp. 251-284.
26. Baker E.N. Structure of azurin from Alcaligenes denitrificans. Refinement at 1.8 Å resolution and comparison of the two crystallographically independent molecules. J. Mol. Biol. 203 (1988) 1071-1095
27. Balakshin M., Chen C.-L., Gratzl J.S., Kirkman A.G., and Jakob H. Biobleaching of pulp with dioxygen in laccase-mediator system - Effect of variables on the reaction kinetics. J. Mol. Catal. B: Enz. 16 (2001) 205-215
28. Baminger U., Subramaniam S.S., Renganathan V., and Haltrich D. Purification and characterization of cellobiose dehydrogenase from the plant pathogen Sclerotium (Athelia) rolfsii. Appl. Environ. Microbiol. 67 (2001) 1766-1774
29. Barrett F.M. Phenoloxidases from larval cuticle of the sheep blowfly, Lucilia cuprina: Characterization, developmental changes, and inhibition by antiphenoloxidase antibodies. Arch. Insect Biochem. Physiol. 5 (1987) 99-118
30. Barton S.C., Gallaway J., and Atanassov P. Enzymatic biofuel cells for implantable and microscale devices. Chem. Rev. 104 (2004) 4867-4886
31. 2 to water at +0.7 V (NHE) at pH 5. J. Am. Chem. Soc. 123 (2001) 5802-5803
32. 2 to water at 0.6 V (SHE) at pH 7 on the 'wired' Pleurotus ostreatus laccase cathode. Biosens. Bioelectron. 17 (2002) 1071-1074
33. Berenguer J.J., Manjon A., and Iborra J.L. A pH-tyrosinase biosensor for amino acids, catecholamines, and adrenergic drugs determination. Biotechnol. Technol. 3 (1989) 211-216
34. Berezin I.V., Bogdanovskaya V.A., Varfolomeev S.D., Tarasevich M.R., and Yaropolov A.I. Bioelectrocatalysis. Equilibrium oxygen potential in the presence of laccase. Dokl. Akad. Nauk. SSSR 240 (1978) 615-618
35. Bielli P., and Calabrese L. Structure to function relationships in ceruloplasmin: A "moonlighting" protein. Cell. Mol. Life Sci. 59 (2002) 1413-1427
36. Bistolas N., Christenson A., Ruzgas T., Jung C., Scheller F.W., and Wollenberger U. Spectroelectrochemistry of cytochrome P450cam. Biochem. Biophys. Res. Commun. 314 (2004) 810-816
37. Bistolas N., Wollenberger U., Jung C., and Scheller F.W. Cytochrome P450 biosensors - a review. Biosens. Bioelectron. 20 (2005) 2408-2423
38. Bogdanovskaya V.A., Fridman V.A., Tarasevich M.R., and Scheller F. Bioelectrocatalysis by immobilized peroxidase: The reaction mechanism and the possibility of electroanalytical detection of both inhibitors and activators of enzyme. Anal. Lett. 27 (1994) 2823-2847
39. Bogdanovskaya V.A., Gavrilova E.F., and Tarasevich M.R. Influence of the state of carbon sorbents on the activity of immobilized phenol oxidases. Elektrokhimiya 22 (1986) 742-746
40. Bonagura C.A., Bhaskar B., Shimizu H., Li H., Sundaramoorthy M., McRee D.E., Goodin D.B., and Poulos T.L. High-resolution crystal structures and spectroscopy of native and compound I cytochrome c peroxidase. Biochemistry 42 (2003) 5600-5608
41. Bond A.M. Chemical and electrochemical approaches to the investigations of redox reactions of simple electron transfer metaloproteins. Inorg. Chim. Acta 226 (1994) 293-340
42. Bond D.R., and Lovley D.R. Electricity production by Geobacter sulfurreducens attached to electrodes. Appl. Environ. Microbiol. 69 (2003) 1548-1555
43. Borsari M., and Azab H.A. Voltammetric behavior of bovine erythrocyte superoxide dismutase. Bioelectrochem. Bioenerg. 27 (1992) 229-233
44. Brown A.P., and Anson F.C. Electron transfer with both reactant and product attached to the electrode surface. J. Electroanal. Chem. 92 (1978) 133-145
45. Burestedt E., Navarez A., Ruzgas T., Gorton L., Emnéus J., and Marko-Varga G. Rate limiting steps of tyrosinase-modified electrodes for the detection of catechol. Anal. Chem. 68 (1996) 1605-1611
46. Burgess J.D., Rhoten M.C., and Hawkridge F.M. Observation of the resting and pulsed states of cytochrome c oxidase in electrode-supported lipid bilayer membranes. J. Am. Chem. Soc. 120 (1998) 4488-4491
47. Burrows A.L., Hill H.A.O., Leese T.A., McIntire W.S., Nakayama H., and Sanghera G.S. Direct electrochemistry of the enzyme, methylamine dehydrogenase, from bacterium W3A1. Eur. J. Biochem. 199 (1991) 73-78
48. ®-process). J. Biotechnol. 53 (1997) 163-202
49. Cameron M.D., and Aust S.D. Kinetics and reactivity of the flavin and heme cofactors of cellobiose dehydrogenase from Phanerochaete chrysosporium. Biochemistry 39 (2000) 13595-13601
50. Cameron M.D., and Aust S.D. Cellobiose dehydrogenase - An extracellular fungal flavocytochrome. Enzyme Microb. Technol. 28 (2001) 129-138
51. Campanella L., Bonanni A., Finotti E., and Tomassetti M. Biosensors for determination of total and natural antioxidant capacity of red and white wines: Comparison with other spectrophotometric and fluorimetric methods. Biosens. Bioelectron. 19 (2004) 641-651
52. Campanella L., Favero G., Persi L., Sammartino M.P., Tomassetti M., and Visco G. Organic phase enzyme electrodes: Applications and theoretical studies. Anal. Chim. Acta 426 (2001) 235-247
53. Carrico R.J., Malmström B.G., and Vänngård T. Reduction and oxidation of human ceruloplasmin. Evidence that a diamagnetic chromophore in the enzyme participates in the oxidase mechanism. Eur. J. Biochem. 22 (1971) 127-133
54. Cha M.-K., and Kim I.-H. Ceruloplasmin has a distinct active site for the catalyzing glutathione-dependent reduction of alkyl hydroperoxide. Biochemistry 38 (1999) 12104-12110
55. Chaudhuri S.K., and Lovley D.R. Electricity generation by direct oxidation of glucose in mediatorless microbial fuel cells. Nat. Biotechnol. 21 (2003) 1229-1232
56. Chen X., Xie H., Kong J., and Deng J. Characterization for didodecyldimethylammonium bromide crystal film entrapping catalase with enhanced direct electron transfer rate. Biosens. Bioelectron. 16 (2001) 115-120
57. Christenson A., Dimcheva N., Ferapontova E.E., Gorton L., Ruzgas T., Stoica L., Shleev S., Yaropolov A.I., Haltrich D., Thorneley R.N.F., and Aust S.D. Direct electron transfer between ligninolytic redox enzymes and electrodes. Electroanalysis 16 (2004) 1074-1092
58. Christenson A., Dock E., Gorton L., and Ruzgas T. Direct heterogeneous electron transfer of theophylline oxidase. Biosens. Bioelectron. 20 (2004) 176-183
59. Clark J.L.C., and Lyons C. Electrode systems for continuous monitoring in cardiovascular surgery. Ann. NY Acad. Sci. 102 (1962) 29-45
60. Cooper J.M., Greenough K.R., and McNeil C.J. Direct electron transfer between immobilized cytochrome c and modified gold electrodes. J. Electroanal. Chem. 347 (1993) 267-275
61. Correia dos Santos M.M., Paes de Sousa P.M., Simoes Goncalves M.L., Krippahl L., Moura J.J.G., Lojou E., and Bianco P. Electrochemical studies on small electron transfer proteins using membrane electrodes. J. Electroanal. Chem. 541 (2003) 153-162
62. Correia dos Santos M.M., Sousa P.M.P., Goncalves M.L.S., Romao M.J., Moura I., and Moura J.J.G. Direct electrochemistry of the Desulfovibrio gigas aldehyde oxidoreductase. Eur. J. Biochem. 271 (2004) 1329-1338
63. Cosnier S., and Innocent C. A new strategy for the construction of a tyrosinase-based amperometric phenol and o-diphenol sensor. Bioelectrochem. Bioenerg. 31 (1993) 147-160
64. Csöregi E., Gorton L., and Marko-Varga G. Carbon fibre as electrode materials for the construction of peroxidase modified amperometric biosensors. Anal. Chim. Acta 273 (1993) 59-70
65. Csöregi E., Jönsson-Pettersson G., and Gorton L. Mediatorless electrocatalytic reduction of hydrogen peroxide at graphite electrodes chemically modified with peroxidases. J. Biotechnol. 30 (1993) 315-337
66. Csöregi E., Gorton L., and Marko-Varga G. Amperometric microbiosensors for detection of hydrogen peroxide and glucose based on peroxidase modified carbon fibres. Electroanalysis 6 (1994) 925-933
67. Csöregi E., Gorton L., Marko-Varga G., Tüdös A., and Kok T.W. Peroxidase modified carbon fiber microelectrodes in flow system for detection of hydrogen peroxide and organic peroxides. Anal. Chem. 66 (1994) 3604-3610
68. Cusanovich M.A., and Tollin G. Kinetics of electron transfer of c-type cytochromes with small reagents. In: Scott R.A., and Mauk A.G. (Eds). Cytochrome c: A Multidisciplinary Approach (1996), University Science Books, Sausalito 489-513
69. Daigle F., Trudeau F., Robinson G., Smyth M.R., and Leech D. Mediated reagentless enzyme inhibition electrodes. Biosens. Bioelectron. 13 (1998) 417-425
70. Davidson, V.L., Ed., 1993, Principles and Applications of Quinoproteins, Marcel Dekker, New York.
71. Davidson V.L. Electron transfer in quinoproteins. Arch. Biochem. Biophys. 428 (2004) 32-40
72. Davidson V.L., and Jones L.H. Intermolecular electron transfer from quinoproteins and its relevance to biosensor technology. Anal. Chim. Acta 249 (1991) 235-240
73. de Castro, A.F., S.K. Gupta and A.K. Agarwal, 1989, Enzymic determination of theophylline, WO 8907653 A1 19890824.
74. De Ley M., and Osaki S. Intramolecular electron transport in human ferroxidase (ceruloplasmin). Biochem. J. 151 (1975) 561-566
75. Degani Y., and Heller A. Direct electrical communication between chemically modified enzymes and metal electrodes. I. Electron transfer from glucose oxidase to metal electrodes via electron relays, bound covalently to the enzyme. J. Phys. Chem. 91 (1987) 1285-1289
76. Deinum J., and Vänngård T. The stoichiometry of the paramagnetic copper and the oxidation-reduction potentials of type I copper in human ceruloplasmin. Biochim. Biophys. Acta 310 (1973) 321-330
77. Deverall B.J. Phenolase and pectic enzyme activity in chocolate spot disease of beans. Nature 189 (1961) 311
78. Dryhurst, G., K.M. Kadish, F. Scheller and R. Renneberg, Eds., 1982, Biological Electrochemistry, Academic Press, New York.
79. Ducros V., Brzozowski A.M., Wilson K.S., Brown S.H., Østergaard P., Schneider P., Yaver D.S., Pedersen A.H., and Davies G.J. Crystal structure of the type-2 Cu depleted laccase from Coprinus cinereus at 2.2 Å resolution. Nat. Struct. Biol. 5 (1998) 310-316
80. Duine J.A. Quinoproteins: Enzymes containing the quinoid cofactor pyrroloquinoline quinone, topaquinone or tryptophan-tryptophan quinone. Eur. J. Biochem. 200 (1991) 271-284
81. Duine J.A. The importance of natural diversity in redox proteins for achieving cofactor-directed electron transfer. Biosens. Bioelectron. 10 (1995) 17-23
82. Duine J.A. Cofactor diversity in biological oxidations: Implications and applications. Chem. Record 1 (2001) 74-83
83. Duine J.A., Frank J., and Jongjan J.A. Enzymology of quinoproteins. Adv. Enzymol. Relat. Areas Mol. Biol. 59 (1987) 165-212
84. Dunford H.B. Heme Peroxidases (1999), Wiley, New York
85. Duran N., Rosa M.A., D'Annibale A., and Gianfreda L. Applications of laccases and tyrosinases (phenoloxidases) immobilized on different supports: A review. Enz. Microb. Technol. 31 (2002) 907-931
86. Eddowes, M.J. and H.A.O. Hill, 1977, Novel method for the investigation of the electrochemistry of metalloproteins: cytochrome c, J. Chem. Soc., Chem. Commun. 771-772.
87. Eddowes M.J., Hill H.A.O., and Uosaki K. Electrochemistry of cytochrome c. Comparison of the electron-transfer at a surface-modified gold electrode with that to cytochrome-oxidase. J. Am. Chem. Soc. 101 (1979) 7113-7114
88. Eddowes M.J., Hill H.A.O., and Uosaki K. The electrochemistry of cytochrome c. Investigation of the mechanism of the 4,4′-bipyridyl surface modified gold electrode. Bioelectrochem. Bioenerg. 7 (1980) 527-537
89. El Kasmi A., Wallace J.M., Bowden E.F., Binet S.M., and Linderman R.J. Controlling interfacial electron-transfer kinetics of cytochrome c with mixed self-assembled monolayers. J. Am. Chem. Soc. 120 (1998) 225-226
90. Elliott S.J., Hoke K.R., Heffron K., Palak M., Rothery R.A., Weiner J.H., and Armstrong F.A. Voltammetric studies of the catalytic mechanism of the respiratory nitrate reductase from Escherichia coli: How nitrate reduction and inhibition depend on the oxidation state of the active site. Biochemistry 43 (2004) 799-807
91. Elliott S.J., McElhaney A.E., Feng C., Enemark J.H., and Armstrong F.A. A voltammetric study of interdomain electron transfer within sulfite oxidase. J. Am. Chem. Soc. 124 (2002) 11612-11613
92. Enemark J.H., Cooney J.J.A., Wang J.-J., and Holm R.H. Synthetic analogues and reaction systems relevant to the molybdenum and tungsten oxotransferases. Chem. Rev. 104 (2004) 1175-1200
93. Enguita F.J., Martins L.O., Henriques A.O., and Carrondo M.A. Crystal structure of a bacterial endospore coat component: A laccase with enhanced thermostability properties. J. Biol. Chem. 278 (2003) 19416-19425
94. Esaka M., Fujisawa K., Goto M., and Kisu Y. Regulation of ascorbate oxidase expression in pumpkin by auxin and copper. Plant Physiol. 100 (1992) 231-237
95. Fantuzzi A., Fairhead M., and Gilardi G. Direct electrochemistry of immobilized human cytochrome P450 2E1. J. Am. Chem. Soc. 126 (2004) 5040-5041
96. Farhangrazi Z.S., Fossett M.E., Powers L.S., and Ellis Jr. W.R. Variable-temperature spectroelectrochemical study of horseradish peroxidase. Biochemistry 34 (1995) 2866-2871
97. Farrar J.A., Thomson A.J., Cheesman M.R., Dooley D.M., and Zumft W.G. A model of the copper centers of nitrous oxide reductase (Pseudomonas stutzeri). Evidence from optical, EPR and MCD spectroscopy. FEBS Lett. 294 (1991) 11-15
98. Feng C., Kedia R.V., Hazzard J.T., Hurley J.K., Tollin G., and Enemark J.H. Effect of solution viscosity on intramolecular electron transfer in sulfite oxidase. Biochemistry 41 (2002) 5816-5821
99. Feng C.J., Wilson H.L., Hurley J.K., Hazzard J.T., Tollin G., Rajagopalan K.V., and Enemark J.H. Essential role of conserved arginine 160 in intramolecular electron transfer in human sulfite oxidase. Biochemistry 42 (2003) 12235-12242
100. Feng Z.Q., Imabayashi S., Kakiuchi T., and Niki K. Long-range electron-transfer reaction rates to cytochrome c across long- and short-chain alkanethiol self-assembled monolayers: Electroreflectance studies. J. Chem. Soc., Farad. Trans. 93 (1997) 1367-1370
101. Feng Z.Q., Sagara T., and Niki K. Application of potential-modulated UV-visible reflectance spectroscopy to electron transfer rate measurements for adsorbed species on electrode surfaces. Anal. Chem. 67 (1995) 3564-3570
102. Ferapontova E.E. Direct peroxidase bioelectrocatalysis on a variety of electrode materials. Electroanalysis 16 (2004) 1101-1112
103. Ferapontova E.E., Christenson A., Hellmark A., and Ruzgas T. Spectroelectrochemical study of heme- and molybdopterin cofactor-containing chicken liver sulphite oxidase. Bioelectrochemistry 63 (2004) 49-53
104. Ferapontova E.E., and Fedorovich N.V. Effect of cation adsorption on the kinetics of anion electroreduction Part I. Effect of the adsorption of inorganic cations in small concentrations on the kinetics of anion electroreduction with different elementary steps of discharge. J. Electroanal. Chem. 476 (1999) 26-36
105. Ferapontova E.E., and Gorton L. Effect of proton donors on direct electron transfer in the system gold electrode-horseradish peroxidase. Electrochem. Commun. 3 (2001) 767-774
106. Ferapontova E., and Gorton L. Effect of pH on direct electron transfer in the system gold electrode-recombinant horseradish peroxidase. Bioelectrochemistry 55 (2002) 83-87
107. Ferapontova E.E., and Gorton L. Direct electrochemistry of heme multicofactor-containing enzymes on alkanethiol-modified gold electrodes. Bioelectrochemistry 66 (2005) 55-63
108. Ferapontova E.E., Grigorenko V.G., Egorov A.M., Börchers T., Ruzgas T., and Gorton L. Direct electron transfer in the system gold electrode-recombinant horseradish peroxidases. J. Electroanal. Chem. 509 (2001) 19-26
109. 2 based on recombinant forms of horseradish peroxidase directly adsorbed on polycrystalline gold. Biosens. Bioelectron. 16 (2001) 147-157
110. Ferapontova E., and Puganova E. Effect of pH on direct electron transfer between graphite and horseradish peroxidase. J. Electroanal. Chem. 518 (2002) 20-26
111. Ferapontova E., Schmengler K., Börchers T., Ruzgas T., and Gorton L. Effect of cysteine mutations on direct electron transfer of horseradish peroxidase on gold. Biosens. Bioelectron. 17 (2002) 953-963
112. Ferapontova E.E., Reading N.S., Aust S.D., Ruzgas T., and Gorton L. Direct electron transfer between graphite electrodes and ligninolytic peroxidases from Phanerochaete chrysosporium. Electroanalysis 14 (2002) 1411-1418
113. Ferapontova E.E., Ruzgas T., and Gorton L. Direct electron transfer of heme- and molybdopterin cofactor-containing chicken liver sulfite oxidase on alkanethiol-modified gold electrodes. Anal. Chem. 75 (2003) 4841-4850
114. Finklea, H.O., 1996, Electrochemistry of organized monolayers of thiols and related molecules on electrodes. Electroanalytical Chemistry, Vol. 19, Ed. A.J. Bard, Marcel Dekker, New York, pp. 114-335.
115. Freire R.S., Duran N., and Kubota L.T. Effects of fungal laccase immobilization procedures for the development of a biosensor for phenol compounds. Talanta 54 (2001) 681-686
116. Freire R.S., Pessoa C.A., Mello L.D., and Kubota L.T. Direct electron transfer: An approach for electrochemical biosensors with higher selectivity and sensitivity. J. Braz. Chem. Soc. 14 (2003) 230-243
117. Fridman V.A., Bogdanovskaya V.A., and Tarasevich M.R. Kinetics and mechanism of peroxidase redox transformations on a carbon material. Elektrokhimiya 30 (1994) 807-811
118. Fridman V., Wollenberger U., Bogdanovskaya V., Lisdat F., Ruzgas T., Lindgren A., Gorton L., and Scheller F.W. Electrochemical investigation of cellobiose oxidation by cellobiose dehydrogenase in the presence of cytochrome c as mediator. Biochem. Soc. Trans. 28 (2000) 63-70
119. Fridovich I. The biology of oxygen radicals. Science 201 (1978) 875-880
120. Frieden E., and Hsieh H.S. Ceruloplasmin: The copper transport protein with essential oxidase activity. Adv. Enzymol. Relat. Areas Mol. Biol. 44 (1976) 187-236
121. Fujieda N., Mori M., Kano K., and Ikeda T. Spectroelectrochemical evaluation of redox potentials of cysteine tryptophylquinone and two hemes c in quinohemoprotein amine dehydrogenase from Paracoccus denitrificans. Biochemistry 41 (2002) 13736-13743
122. Gajhede M., Schuller D.J., Henriksen A., Smith A.T., and Poulos T.L. Crystal structure of horseradish peroxidase C at 2.5 Å resolution. Nat. Struct. Biol. 4 (1997) 1032-1038
123. Gaspar S., Zimmermann H., Gazaryan I., Csöregi E., and Schuhmann W. Hydrogen peroxide biosensors based on direct electron transfer from plant peroxidases immobilized on self-assembled thiol-monolayer modified gold electrodes. Electroanalysis 13 (2001) 284-288
124. Gazarian I.G., Lagrimini L.M., George S.J., and Thorneley R.N.F. Anionic tobacco peroxidase is active at extremely low pH: Veratryl alcohol oxidation with a pH optimum of 1.8. Biochem. J. 320 (1996) 369-372
125. Gazaryan I.G., Lagrimini L.M., Ashby G.A., and Thorneley R.N.F. Mechanism of indole-3-acetic acid oxidation by plant peroxidases: Anaerobic stopped-flow spectrophotometric studies on horseradish and tobacco peroxidases. Biochem. J. 313 (1996) 841-847
126. Ge B., and Lisdat F. Superoxide sensor based on cytochrome c immobilized on mixed-thiol SAM with a new calibration method. Anal. Chim. Acta 454 (2002) 53-64
127. Ge B., Scheller F.W., and Lisdat F. Electrochemistry of immobilized CuZnSOD and FeSOD and their interaction with superoxide radicals. Biosens. Bioelectron. 18 (2003) 295-302
128. Gelo-Pujic M., Kim H.H., Butlin N.G., and Palmore G.T. Electrochemical studies of a truncated laccase produced in Pichia pastoris. Appl. Environ. Microbiol. 65 (1999) 5515-5521
129. Ghindilis A. Direct electron transfer catalyzed by enzymes: Application for biosensor development. Biochem. Soc. Trans. 28 (2000) 84-89
130. Ghindilis A.L., Atanasov P., and Wilkins E. Enzyme-catalyzed direct electron transfer: Fundamentals and analytical applications. Electroanalysis 9 (1997) 661-674
131. Gilardi G., den Blaauwen T., and Canters G.W. Molecular recognition - design of a biosensor with genetically engineered azurin as redox mediator. J. Control. Release 29 (1994) 231-238
132. Givaudan A., Effosse A., Faure D., Potier P., Bouillant M.L., and Bally R. Polyphenol oxidase in Azospirillum lipoferum isolated from rice rhizosphere: Evidence for laccase activity in nonmotile strains of Azospirillum lipoferum. FEMS Microbiol. Lett. 108 (1993) 205-210
133. Gorton L. Carbon paste electrodes chemically modified with enzymes, tissues and cells. A review. Electroanalysis 7 (1995) 23-45
134. Gorton L., Bremle G., Csöregi E., Jönsson-Pettersson G., and Persson B. Amperometric glucose sensors based on immobilised glucose oxidising enzymes and chemically modified electrodes. Anal. Chim. Acta 249 (1991) 43-54
135. Gorton L., Csöregi E., Domínguez E., Emnéus J., Jönsson-Pettersson G., Marko-Varga G., and Persson B. Selective detection in flow analysis based on the combination of immobilised enzymes and chemically modified electrodes. Anal. Chim. Acta 250 (1991) 203-248
136. Gorton L., Domínguez E., Marko-Varga G., Persson B., Jönsson-Pettersson G., Csöregi E., Johansson K., Narasaiah D., Ghobadi S., Kacaniklic V., Skotheim T., Hale P., Okamoto Y., and Lan H.-L. Amperometric biosensors based on immobilized redox-enzymes in carbon paste electrodes. In: Pungor E. (Ed). Bioelectroanalysis (1992), Akadémiai Kiadó, Budapest, Hungary 33-52
137. 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. Anal. Chim. Acta 400 (1999) 91-108
138. Grass G., and Rensing C. CueO is a multi-copper oxidase that confers copper tolerance in Escherichia coli. Biochem. Biophys. Res. Commun. 286 (2001) 902-908
139. Gray H.B., and Winkler J.R. Electron tunneling through proteins. Quart. Rev. Biophys. 36 (2003) 341-372
140. Grigorenko V., Chubar T., Kapeliuch Y., Börchers T., Spener F., and Egorov A. New approaches for functional expression of recombinant horseradish peroxidase C in Escherichia coli. Biocatal. Biotransform. 17 (1999) 359-379
141. Gunnarsson P.O., Nylen U., and Pettersson G. Kinetics of the interaction between ceruloplasmin and reducing substrates. Eur. J. Biochem. 37 (1973) 41-46
142. Guo L.-H., and Hill H.A.O. Direct electrochemistry of proteins and enzymes. Adv. Inorg. Chem. 36 (1991) 341-375
143. 552). J. Biol. Chem. 265 (1990) 1958-1963
144. Guo L.H., Hill H.A.O., Lawrance G.A., Sanghera G.S., and Hopper D.J. Direct unmediated electrochemistry of the enzyme p-cresolmethylhydroxylase. J. Electroanal. Chem. 266 (1989) 379-396
145. Guo J., Liang X.X., Mo P.S., and Li G.X. Purification and properties of bilirubin oxidase from Myrothecium verrucaria. Appl. Biochem. Biotechnol. 31 (1991) 135-143
146. Gupta S.K., Agarwal A.K., and deCastro A.F. A novel enzymatic approach for serum theophylline measurement. Clin. Chem. 34 (1988) 1267
147. Gupta G., Rajendran V., and Atanassov P. Bioelectrocatalysis of oxygen reduction reaction by laccase on gold electrode. Electroanalysis 16 (2004) 1182-1185
148. Haas A.S., Pilloud D.L., Reddy K.S., Babcock G.T., Moser C.C., Blasie J.K., and Dutton P.L. Cytochrome c and cytochrome c oxidase: Monolayer assemblies and catalysis. J. Phys. Chem. B 105 (2001) 11351-11362
149. Haghighi B., Gorton L., Ruzgas T., and Jönsson L.J. Characterization of graphite electrodes modified with laccase from Trametes versicolor and their use for bioelectrochemical monitoring of phenolic compounds in flow injection analysis. Anal. Chim. Acta 487 (2003) 3-14
150. Hakulinen N., Kiiskinen L.-L., Kruus K., Saloheimo M., Paananen A., Koivula A., and Rouvinen J. Crystal structure of a laccase from Melanocarpus albomyces with an intact trinuclear copper site. Nat. Struct. Biol. 9 (2002) 601-605
151. 552 from Thiobacillus ferrooxidans. Anal. Chim. Acta 289 (1994) 15-20
152. Hale P.D., and Skotheim T.A. Cyclic voltammetry at TCNQ and TTF-TCNQ modified platinum electrodes: A study of the glucose oxidase/glucose and galactose oxidase/galactose system. Synth. Met. 28 (1989) C853-C858
153. Hällberg, B.M., 2002. Structural studies on the extracellular flavocytochrome cellobiose dehydrogenase from Phanerochaete chrysosporium, Doctoral thesis, Uppsala University, Uppsala, Sweden.
154. Hallberg B.M., Bergfors T., Backbro K., Pettersson G., Henriksson G., and Divne C. A new scaffold for binding heme in the cytochrome domain of the extracellular flavocytochrome cellobiose dehydrogenase. Structure 8 (2000) 79-88
155. Harbury H.A. Oxidation-reduction potentials of horseradish peroxidase. J. Biol. Chem. 225 (1957) 1009-1024
156. Hayashi Y., and Yamazaki I. The oxidation-reduction potentials of compound I/compound II and compound II/ferric couples of horseradish peroxidases A2 and C. J. Biol. Chem. 254 (1979) 9101-9106
157. He B., Sinclair R., Copeland B.R., Makino R., Powers L.S., and Yamazaki I. The structure-function relationship and reduction potentials of high oxidation states of myoglobin and peroxidase. Biochemistry 35 (1996) 2413-2420
158. Hedenmo M., Narváez A., Domínguez E., and Katakis I. Improved mediated tyrosinase amperometric enzyme electrodes. J. Electroanal. Chem. 425 (1997) 1-11
159. Heering H.A., Weiner J.H., and Armstrong F.A. Direct detection and measurement of electron relays in a multicentered enzyme: Voltammetry of electrode-surface films of E. coli fumarate reductase, an iron-sulfur flavoprotein. J. Am. Chem. Soc. 119 (1997) 11628-11638
160. Heffron K., Leger C., Rothery R.A., Weiner J.H., and Armstrong F.A. Determination of an optimal potential window for catalysis by E. coli dimethyl sulfoxide reductase and hypothesis on the role of Mo(V) in the reaction pathway. Biochemistry 40 (2001) 3117-3126
161. Heller A. Miniature biofuel cells. Phys. Chem. Chem. Phys. 6 (2004) 209-216
162. Heller A., and Degani Y. Direct electrical communication between chemically modified enzymes and metal electrodes. 2. Methods for bonding electron-transfer relays to glucose oxidase and D-amino-acid oxidase. J. Am. Chem. Soc. 110 (1988) 2615-2620
163. Henriksson G., Johansson G., and Pettersson G. A critical review of cellobiose dehydrogenase. J. Biotechnol. 78 (2000) 93-113
164. Henriksson G., Sild V., Szabo I., Pettersson G., and Johansson G. Substrate specificity of cellobiose dehydrogenase from Phanerochaete chrysosporium. Biochim. Biophys. Acta 1383 (1998) 48-54
165. Hill H.A.O., Guo L.H., and McLendon G. Direct electrochemistry of cytochrome c. In: Scott R.A., and Mauk A.G. (Eds). Cytochrome c: A Multidisciplinary Approach (1996), University Science Books, Sausalito 317-333
166. Hill, H.A.O. and N.I. Hunt, 1993, Direct and indirect electrochemical investigations of metalloenzymes. Methods in Enzymology, Vol. 227, Eds. J.F. Riordan, B.L. Vallee, Academic Press, San Diego, pp. 501-522.
167. Hille R. The mononuclear molybdenum enzymes. Chem. Rev. 96 (1996) 2757-2816
168. Hirose J., Inoue K., Sakuragi H., Kikkawa M., Minakami M., Morikawa T., Iwamoto H., and Hiromi K. Anions binding to bilirubin oxidase from Trachyderma tsunodae K-2593. Inorg. Chim. Acta 273 (1998) 204-212
169. Hirst J., Sucheta A., Ackrell B.A.C., and Armstrong F.A. Electrocatalytic voltammetry of succinate dehydrogenase: Direct quantification of the catalytic properties of a complex electron-transport enzyme. J. Am. Chem. Soc. 118 (1996) 5031-5038
170. Ho W.O., Athey D., McNeil C.J., Hager H.J., Evans G.P., and Mullen W.H. Mediatorless horseradish peroxidase enzyme electrodes based on activated carbon: Potential application to specific binding assay. J. Electroanal. Chem. 351 (1993) 185-197
171. Hoke K.R., Cobb N., Armstrong F.A., and Hille R. Electrochemical studies of arsenite oxidase: An unusual example of a highly cooperative two-electron molybdenum center. Biochemistry 43 (2004) 1667-1674
172. Hyde S.M., and Wood P.M. Kinetic and antigenic similarities for cellobiose dehydrogenase from brown rot fungus Coniophora puteana and the white rot fungus Phanerochaete chrysosporium. FEMS Microbiol. Lett. 145 (1996) 439-444
173. Härtl A., Schmich E., Garrido J.A., Hernando J., Catharino S.C.R., Walter S., Feulner P., Kromka A., Steinmüller D., and Stutzmann M. Protein-modified nanocrystalline diamond thin films for biosensor applications. Nat. Mater. 3 (2004) 736-742
174. Igarashi K., Momohara I., Nishino T., and Samejima M. Kinetics of inter-domain electron transfer in flavocytochrome cellobiose dehydrogenase from the white-rot fungus Phanerochaete chrysosporium. Biochem. J. 365 (2002) 521-526
175. Igarashi K., Verhagen M.F.J.M., Samejima M., Schülein M., Eriksson K.-E., and Nishino T. Cellobiose dehydrogenase from the fungi Phanerochaete chrysosporium and Humicola insolens. J. Biol. Chem. 274 (1999) 3338-3344
176. Ikeda T. Electrochemical biosensors based on biocatalyst electrodes. Bull. Electrochem. 8 (1992) 145-159
177. Ikeda T. Direct redox communication between enzymes and electrodes. In: Scheller F.W., Schubert F., and Fedrowitz J. (Eds). Frontiers in Biosensorics Vol. 1 (1997), Birkhäuser, Basel 243-266
178. Ikeda T., Fushimi F., Miki K., and Senda M. Direct bioelectrocatalysis at electrodes modified with d-gluconate dehydrogenase. Agric. Biol. Chem. 52 (1988) 2655-2658
179. Ikeda T., Fushimi F., Miki K., and Senda M. Amperometric biosensors based on quinoprotein-flavoprotein-dehydrogenases: Methods of steady-state current measurements and voltammetric measurements at higher sensitivity. Bunseki Kagaku 38 (1989) 583-588
180. Ikeda T., Kobayashi D., Matsushita F., Sagara T., and Niki K. Bioelectrocatalysis at electrodes coated with alcohol dehydrogenase, a quinohemoprotein with heme c serving as a built-in mediator. J. Electroanal. Chem. 361 (1993) 221-228
181. Ikeda T., Miyaoka S., and Miki K. Enzyme-catalyzed electrochemical oxidation of d-gluconate at electrodes coated with d-gluconate dehydrogenase, a membrane-bound flavohemoprotein. J. Electroanal. Chem. 352 (1993) 267-278
182. Ikeda T., Matsushita F., and Senda M. Amperometric fructose sensor based on direct bioelectrocatalysis. Biosens. Bioelectron. 6 (1991) 299-304
183. Ikeda, T., S. Miyaoka, F. Matsushita, D. Kobayashi and M. Senda, 1992, Direct bioelectrocatalysis at metal and carbon electrodes modified with adsorbed d-gluconate dehydrogenase or adsorbed alcohol dehydrogenase from bacterial membranes, Chem. Lett. 847-850.
184. Itoh H., Hirota A., Hirayama K., Shin T., and Murao S. Properties of ascorbate oxidase produced by Acremonium sp. HI-25. Biosci. Biotechnol. Biochem. 59 (1995) 1052-1056
185. Iwata S., Ostermeier C., Ludwig B., and Michel H. Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans. Nature 376 (1995) 660-669
186. Jarosz-Wilkolazka A., Janusz G., Ruzgas T., Gorton L., Malarczyk E., and Leonowicz A. Development of a laccase modified electrode for amperometric detection of mono- and diphenols: I. Influence of the enzyme storage method. Anal. Lett. 37 (2004) 1497-1513
187. Jarosz-Wilkolazka A., Ruzgas T., and Gorton L. Use of laccase-modified electrode for amperometric detection of plant flavonoids. Enzyme Microb. Technol. 35 (2004) 238-241
188. Jeuken L.J.C. Conformational reorganisation in interfacial protein electron transfer. Biochim. Biophys. Acta 1604 (2003) 67-76
189. Jeuken L.J.C., McEvoy J.P., and Armstrong F.A. Insights into gated electron-transfer kinetics at the electrode-protein interface: A square wave voltammetry study of the blue copper protein azurin. J. Phys. Chem. B 106 (2002) 2304-2313
190. Jeuken L.J.C., van Vliet P., Verbeet M.P., Camba R., McEvoy J.P., Armstrong F.A., and Canters G.W. Role of the surface-exposed and copper-coordinating histidine in blue copper proteins: The electron-transfer and redox-coupled ligand binding properties of His117Gly azurin. J. Am. Chem. Soc. 122 (2000) 12186-12194
191. Jia N.Q., Zhang Z.R., Zhu J.Z., and Zhang G.X. A galactose biosensor based on the microfabricated thin film electrode. Anal. Lett. 36 (2003) 2095-2106
192. Jin L., Liu H., and Fang Y. Ascorbic acid oxidase biosensor based on the glassy carbon electrode modified with Nafion and methyl viologen. Fenxi Huaxue 20 (1992) 515-519
193. Jin W., Wollenberger U., Bier F.F., Makower A., and Scheller F.W. Electron transfer between cytochrome c and copper enzymes. Bioelectrochem. Bioenerg. 39 (1996) 221-225
194. João Romão M., Knäblein J., Huber R., and Moura J.J.G. Structure and function of molybdoptrein containing enzymes. Prog. Biophys. Molec. Biol. 68 (1997) 121-144
195. Johansen, C., 1996, A basic protein composition for killing or inhibiting microbial cells, Wo, Wo 9606532 A1 19960307.
196. Johnson D.L., Thompson J.L., Brinkmann S.M., Schuller K.A., and Martin L.L. Electrochemical characterization of purified Rhus vernicifera laccase: Voltammetric evidence for a sequential four-electron transfer. Biochemistry 42 (2003) 10229-10237
197. Jönsson G., and Gorton L. An electrochemical sensor for hydrogen peroxide based on peroxidase adsorbed on a spectrographic graphite electrode. Electroanalysis 1 (1989) 465-468
198. Kaim W., and Rall J. Copper - A "modern" bioelement. Angew. Chem. Int. Ed. Engl. 35 (1996) 43-60
199. Karamyshev A.V., Shleev S.V., Koroleva O.V., Yaropolov A.I., and Sakharov I.Y. Laccase-catalyzed synthesis of conducting polyaniline. Enz. Microb. Technol. 33 (2003) 556-564
200. Kassner R.J. Effects of nonpolar environments on the redox potentials of heme complexes. Proc. Nat. Acad. Sci. USA 69 (1972) 2263-2267
201. Katz E., Lioubashevski O., and Willner I. Magnetic field effects on cytochrome c-mediated bioelectrocatalytic transformations. J. Am Chem. Soc. 126 (2004) 11088-11092
202. Katz E., Schlereth D.D., Schmidt H.-L., and Olsthoorn A.J.J. Reconstitution of the quinoprotein glucose dehydrogenase from its apoenzyme on a gold electrode surface modified with a monolayer of pyrroloquinoline quinone. J. Electroanal. Chem. 368 (1994) 165-171
203. Katz E., and Willner I. A biofuel cell with electrochemically switchable and tunable power output. J. Am Chem. Soc. 125 (2003) 6803-6813
204. Kawahara K., Suzuki S., Sakurai T., and Nakahara A. Characterization of cucumber ascorbate oxidase and its reaction with hexacyanoferrate (II). Arch. Biochem. Biophys. 241 (1984) 179-186
205. Khan G.F., Shinohara H., Ikariyama Y., and Aizawa M. Electrochemical behavior of monolayer quinoprotein adsorbed on the electrode surface. J. Electroanal. Chem. 315 (1991) 263-273
206. Kinnear K.T., and Monbouquette H.G. Direct electron transfer to Escherichia coli fumarate reductase in self-assembled alkanethiol monolayers on gold electrodes. Langmuir 9 (1993) 2255-2257
207. Kisker C., Schindelin H., Pacheco A., Wehbi W.A., Garret R.M., Rajagopalan K.V., Enemark J.H., and Rees D.C. Molecular basis of sulfite oxidase deficiency from the structure of sulfite oxidase. Cell 91 (1997) 973-983
208. Kisker C., Schindelin H., and Rees D.C. Molybdenium-cofactor-containing enzymes: Structure and mechanism. Ann. Rev. Biochem. 66 (1997) 233-267
209. Klabunde T., Eicken C., Sacchettini J.C., and Krebs B. Crystal structure of a plant catechol oxidase containing a dicopper center. Nat. Struct. Biol. 5 (1998) 1084-1090
210. Kobayashi D., Qzawa S., Mihara T., and Ikeda T. Flavoenzyme-catalyzed electrochemical oxidation of NADH and NADPH in the absence of external mediators. Denki Kagaku 60 (1992) 1056-1062
211. Kohzuma T., Shidara S., and Suzuki S. Direct electrochemistry of nitrite reductase from Achromobacter cycloclastes IAM 1013. Bull. Chem. Soc. Japan 67 (1994) 138-143
212. Kojima Y., Tsukuda Y., Kawai Y., Tsukamoto A., Sugiura J., Sakaino M., and Kita Y. Cloning, sequence analysis, and expression of ligninolytic phenoloxidase genes of the white-rot basidiomycete Coriolus hirsutus. J. Biol. Chem. 265 (1990) 15224-15230
213. Koroleva O.V., Yavmetdinov I.S., Shleev S.V., Stepanova E.V., and Gavrilova V.P. Isolation and study of some properties of laccase from the basidiomycetes Cerrena maxima. Biochemistry (Moscow) 66 (2001) 618-622
214. Kotte H., Gründig B., Vorlop K.D., Strehlitz B., and Stottmeister U. Methylphenazonium-modified enzyme sensor based on polymer thick-films for subnanomolar detection of phenols. Anal. Chem. 67 (1995) 65-70
215. Kremer S.M., and Wood P.M. Continuous monitoring of cellulose oxidation by cellobiose oxidase from Phanerochaete-chrysosporium. FEMS Microbiol. Lett. 92 (1992) 187-192
216. Kroneck P.M.H., Armstrong F.A., Merkle H., and Marchesini A. Ascorbate oxidase: Molecular properties and catalytic activity. Adv. Chem. Ser. 200 (1982) 223-248
217. Kulys J., and Schmid R.D. Mediatorless peroxidase electrode and preparation of bienzyme sensors. Bioelectrochem. Bioenerg. 24 (1990) 305-311
218. Kulys J.J., and Svirmickas G.J.S. Biochemical cell for the determination of lactate. Anal. Chim. Acta 109 (1979) 55-60
219. Kuznetsov B.A., Shumakovich G.P., Koroleva O.V., and Yaropolov A.I. On applicability of laccase as label in the mediated and mediatorless electroimmunoassay: Effect of distance on the direct electron transfer between laccase and electrode. Biosens. Bioelectron. 16 (2001) 73-84
220. Lai M.E., and Bergel A. Electrochemical reduction of oxygen on glassy carbon: Catalysis by catalase. J. Electroanal. Chem. 494 (2000) 30-40
221. Lai M.E., and Bergel A. Direct electrochemistry of catalase on glassy carbon. Bioelectrochemistry 55 (2002) 157-160
222. Larsson T., Lindgren A., and Ruzgas T. Spectroelectrochemical study of cellobiose dehydrogenase and diaphorase in a thiol-modified gold capillary in the absence of mediators. Bioelectrochemistry 53 (2001) 243-249
223. Larsson T., Lindgren A., Ruzgas T., Lindquist S.E., and Gorton L. Bioelectrochemical characterisation of cellobiose dehydrogenase modified graphite electrodes: Ionic strength and pH dependences. J. Electroanal. Chem. 482 (2000) 1-10
224. Larsson T., Lindquist S.-E., Elmgren M., Tessema M., Gorton L., and Henriksson G. Electron transfer between cellobiose dehydrogenase and graphite electrodes. Anal. Chim. Acta 331 (1996) 207-215
225. 2O at the trinuclear copper cluster active site in native laccase. J. Am. Chem. Soc. 124 (2002) 6180-6193
226. Lee C.W., Gray H.B., Anson F.C., and Malmström B.G. Catalysis of the reduction of dioxygen at graphite electrodes coated with fungal laccase A. J. Electroanal. Chem. 172 (1984) 289-300
227. Leger C., Elliott S.J., Hoke K.R., Jeuken L.J.C., Jones A.K., and Armstrong F.A. Enzyme electrokinetics: Using protein film voltammetry to investigate redox enzymes and their mechanisms. Biochemistry 42 (2003) 8653-8662
228. Leger C., Heffron K., Pershad H.R., Maklashina E., Luna-Chavez C., Cecchini G., Ackrell B.A.C., and Armstrong F.A. Enzyme electrokinetics: Energetics of succinate oxidation by fumarate reductase and succinate dehydrogenase. Biochemistry 40 (2001) 11234-11245
229. Lewis D.F.V. Cytochrome P450: Structure, function and mechanism (1996), Taylor and Francis, London
230. Lewis E.A., and Tolman W.B. Reactivity of dioxygen-copper systems. Chem. Rev. 104 (2004) 1047-1076
231. Li J., Yan J., Deng Q., Cheng G., and Dong S. Viologen-thiol self-assembled monolayers for immobilized horseradish peroxidase at gold electrode surface. Electrochim. Acta 42 (1997) 961-967
232. Lin L.S., and Varner J.E. Expression of ascorbic acid oxidase in zucchini squash (Cucurbita pepo L.). Plant Physiol. 96 (1991) 159-165
233. Lindgren A., Emnéus J., Ruzgas T., Gorton L., and Marko-Varga G. Amperometric detection of phenols using peroxidase-modified graphite electrodes. Anal. Chim. Acta 347 (1997) 51-62
234. Lindgren A., Gorton L., Ruzgas T., Baminger U., Haltrich D., and Schülein M. Direct electron transfer of cellobiose dehydrogenase from various biological origins at gold and graphite electrodes. J. Electroanal. Chem. 496 (2001) 76-81
235. Lindgren A., Ruzgas T., and Gorton L. Direct electron transfer of native and modified peroxidases, research trends. In: Richard R. (Ed). Current Topics in Analytical Chemistry Vol. 2 (2001), Poojapura, Trivandrum 71-94
236. Lindgren A., Larsson T., Ruzgas T., and Gorton L. Direct electron transfer between the heme of cellobiose dehydrogenase and thiol modified gold electrodes. J. Electroanal. Chem. 494 (2000) 105-113
237. Lindgren A., Ruzgas T., Gorton L., Csöregi E., Bautista Ardila G., Sakharov I.Y., and Gazaryan I.G. Biosensors based on novel peroxidases with improved properties in direct and mediated electron transfer. Biosens. Bioelectron. 15 (2000) 491-497
238. Lindgren A., Munteanu F.-D., Gazaryan I.G., Ruzgas T., and Gorton L. Comparison of rotating disk and wall-jet electrode systems for studying the kinetics of direct and mediated electron transfer for horseradish peroxidase on a graphite electrode. J. Electroanal. Chem. 458 (1998) 113-120
239. Lindgren A., Ruzgas T., Emnéus J., Csöregi E., Gorton L., and Marko-Varga G. Flow injection analysis of phenolic compounds with carbon paste electrodes modified with tyrosinase purchased from different companies. Anal. Lett. 29 (1996) 1055-1068
240. Lindgren A., Tanaka M., Ruzgas T., Gorton L., Gazaryan I., Ishimori K., and Morishima I. Direct electron transfer catalysed by recombinant forms of horseradish peroxidase: Insight into the mechanism. Electrochem. Commun. 1 (1999) 171-175
241. Lindley P.F., Card G., Zaitseva I., Zaitsev V., Reinhammar B., Selin-Lindgren E., and Yoshida K. An X-ray structural study of human ceruloplasmin in relation to ferroxidase activity. J. Biol. Inorg. Chem. 2 (1997) 454-463
242. Lisdat F., and Karube I. Copper proteins immobilised on gold electrodes for (bio)analytical studies. Biosens. Bioelectron. 17 (2002) 1051-1057
243. Lojou E., and Bianco P. Membrane electrodes can modulate the electrochemical response of redox proteins - direct electrochemistry of cytochrome c. J. Electroanal. Chem. 485 (2000) 71-80
244. Lopes H., Pettigrew G.W., Moura I., and Moura J.J.G. Electrochemical study on cytochrome c peroxidase from Paracoccus denitrificans: A shifting pattern of structural and thermodynamic properties as the enzyme is activated. J. Biol. Inorg. Chem. 3 (1998) 632-642
245. Lötzbeyer T., Schuhmann W., Katz E., Falter J., and Schmidt H.-L. Direct electron transfer between the covalently immobilized enzyme microperoxidase MP-11 and a cystamine-modified gold electrode. J. Electroanal. Chem. 377 (1994) 291-294
246. 2 reduction with hemin covalently immobilized at a monolayer-modified gold electrode. J. Electroanal. Chem. 395 (1995) 339-343
247. Lötzbeyer T., Schuhmann W., and Schmidt H.-L. Minizymes: A new strategy for the development of reagentless amperometric biosensors based on direct electron-transfer processes. Bioelectrochem. Bioenerg. 42 (1997) 1-6
248. Lu H., Li Z., and Hu N. Direct voltammetry and electrocatalytic properties of catalase incorporated in polyacrylamide hydrogel films. Biophys. Chem. 104 (2003) 623-632
249. Ludwig R., Salamon A., Varga J., Zamocky M., Peterbauer C.K., Kulbe K.D., and Haltrich D. Characterisation of cellobiose dehydrogenases from the white-rot fungi Trametes pubescens and Trametes villosa. Appl. Microbiol. Biotechnol. 64 (2004) 213-222
250. Lutz M., Irth H., Jarskog H., Burestedt E., Ghobadi S., Emnéus J., Gorton L., and Marko-Varga G. Effect of different additives on activity of tyrosinase mixed into carbon paste electrodes. Anal. Chim. Acta 305 (1995) 8-17
251. Macholan L., and Chmelikova B. Plant tissue-based membrane biosensor for l-ascorbic acid. Anal. Chim. Acta 185 (1986) 187-193
252. Machonkin, T.E., 2000, Spectroscopic and biochemical studies of multicopper oxidases involved in iron metabolism, Doctoral thesis, Stanford University, Stanford, CA, USA.
253. Makino N., McMahill P., and Mason H.S. The oxidation state of copper in resting tyrosinase. J. Biol. Chem. 249 (1974) 6062-6066
254. Malkin R., and Malmström B.G. State and function of copper in biological systems. Adv. Enzymol. Ramb. 33 (1970) 177-244
255. Malmström B.G. Cytochrome oxidase: Some unsolved problems and controversial issues. Arch. Biochem. Biophys. 280 (1990) 233-241
256. Mano N., and Heller A. A miniature membraneless biofuel cell operating at 0.36 V under physiological conditions. J. Electrochem. Soc. 150 (2003) A1136-A1138
257. Mano N., Fernandez J.L., Kim Y., Shin W., Bard A.J., and Heller A. Oxygen is electroreduced to water on a "wired" enzyme electrode at a lesser overpotential than on platinum. J. Am. Chem. Soc. 125 (2003) 15290-15291
258. 2 biofuel cell and its operation in a living plant. J. Am. Chem. Soc. 125 (2003) 6588-6594
259. 2 cathodes based on their "wiring". J. Phys. Chem. B. 106 (2002) 8842-8848
260. Marcus R.A. Electron-transfer reactions in chemistry - Theory and experiment (Nobel lecture). Angew. Chem. Int. Ed. Engl. 32 (1993) 1111-1121
261. Marcus R.A., and Sutin N. Electron transfer in chemistry and biology. Biochim. Biophys. Acta 811 (1985) 265-322
262. Marko-Varga G., Burestedt E., Svensson C.J., Emnéus J., Gorton L., Ruzgas T., Lutz M., and Unger K.K. Effect of HY-zeolites on the performance of tyrosinase-modified carbon paste electrodes. Electroanalysis 8 (1996) 1121-1126
263. Marko-Varga G., Emnéus J., Ruzgas T., and Gorton L. Development of enzyme-based amperometric sensors for the determination of phenolic compounds. Trends Anal. Chem. 14 (1995) 319-328
264. Martins L.O., Soares C.M., Pereira M.M., Teixeira M., Costa T., Jones G.H., and Henriques A.O. Molecular and biochemical characterization of a highly stable bacterial laccase that occurs as a structural component of the Bacillus subtilis endospore coat. J. Biol. Chem. 277 (2002) 18849-18859
265. Mason M.G., Nicholls P., Divne C., Hallberg B.M., Henriksson G., and Wilson M.T. The heme domain of cellobiose oxidoreductase: A one-electron reducing system. Biochim. Biophys. Acta 1604 (2003) 47-54
266. Mason M.G., Wilson M.T., Ball A., and Nicholls P. Oxygen reduction by cellobiose oxidoreductase: The role of the haem group. FEBS Lett. 518 (2002) 29-32
267. Matsumoto K., Yamada R., and Osajiama K. Ascorbate electrode for determination of l-ascorbic acid in food. Anal. Chem. 53 (1981) 1974-1979
268. Mayer A.M., and Staples R.C. Laccase: New functions for an old enzyme. Phytochemistry 60 (2002) 551-565
269. McArdle F.A., and Persaud K.C. Development of an enzyme-based biosensor for atrazine detection. Analyst 118 (1993) 419-423
270. McNeil C.J., Athey D., and Ho W.O. Direct electron transfer bioelectronic interfaces: Application to clinical analysis. Biosens. Bioelectron. 10 (1995) 75-83
271. McNeil C.J., Athey D., and Renneberg R. Immunosensors for clinical diagnostics. In: Scheller F.W., Schubert F., and Fedrowitz J. (Eds). Frontiers in Biosensorics Vol. 2 (1997), Birkhäuser, Basel 17-25
272. Messerschmidt A., and Huber R. The blue oxidases, ascorbate oxidase, laccase and ceruloplasmin. Modeling and structural relationships. Eur. J. Biochem. 187 (1990) 341-352
273. Messerschmidt, A., R. Huber, T. Poulos and K. Wieghardt, Eds., 2001, Handbook of Metalloproteins, Wiley, Chichester.
274. Messerschmidt A., Ladenstein R., Huber R., Bolognesi M., Avigliano L., Petruzzelli R., Rossi A., and Finazzi-Agro A. Refined crystal structure of ascorbate oxidase at 1.9 Å resolution. J. Mol. Biol. 224 (1992) 179-205
275. Messerschmidt A., Rossi A., Ladenstein R., Huber R., Bolognesi M., Gatti G., Marchesini A., Petruzzelli R., and Finazzi-Agro A. X-ray crystal structure of the blue oxidase ascorbate oxidase from zucchini. Analysis of the polypeptide fold and a model of the copper sites and ligands. J. Mol. Biol. 206 (1989) 513-529
276. Minussi R.C., Pastore G.M., and Duran N. Potential applications of laccase in the food industry. Trends Food Sci. Technol. 13 (2002) 205-216
277. Mirica L.M., Ottenwaelder X., and Stack T.D.P. Structure and spectroscopy of copper-dioxygen complexes. Chem. Rev. 104 (2004) 1013-1045
278. Miyata K., Fujiwara M., Motonaka J., Moriga T., and Nakabayashi I. Micro enzyme-sensor with an osmium complex and porous carbon for measuring galactose. Bull. Chem. Soc. Jpn. 68 (1995) 1921-1927
279. Mondal M.S., Fuller H.A., and Armstrong F.A. Direct measurement of the reduction potential of catalytically active cytochrome c peroxidase compound I: Voltammetric detection of a reversible, cooperative two-electron transfer reaction. J. Am. Chem. Soc. 118 (1996) 263-264
280. Mondal M.S., Goodin D.B., and Armstrong F.A. Simultaneous voltammetric comparisons of reduction potentials, reactivities, and stabilities of the high-potential catalytic states of wild-type and distal-pocket mutant (W51F) yeast cytochrome c peroxidase. J. Am. Chem. Soc. 120 (1998) 6270-6276
281. Mondovi B., Befani O., and Sabatini S. Recent results on the active site of amine oxidases. Agents Actions 14 (1984) 356-357
282. Munteanu F.-D., Gorton L., Lindgren A., Ruzgas T., Emnéus J., Csöregi E., Gazaryan I.G., Ouporov I.V., Mareeva E.A., and Lagrimini L.M. Direct and mediated electron transfer catalyzed by anionic tobacco peroxidase: Effect of calcium ions. Appl. Biochem. Biotechnol. 88 (2000) 321-333
283. Munteanu F.-D., Lindgren A., Emnéus J., Gorton L., Ruzgas T., Csöregi E., Ciucu A., van Huystee R.B., Gazaryan I.G., and Lagrimini L.M. Bioelectrochemical monitoring of phenols and aromatic amines in flow injection using novel plant peroxidases. Anal. Chem. 70 (1998) 2596-2600
284. 2 to water at pH 7.0. Chem. Lett. 32 (2003) 54-55
285. Nakamura T. Purification and physicochemical properties of laccase. Biochim. Biophys. Acta 30 (1958) 44-52
286. Nar H., Messerschmidt A., Huber R., van de Kamp M., and Canters G.W. X-ray crystal structure of the two site-specific mutants His35Gln and His35Leu of azurin from Pseudomonas aeruginosa. J. Mol. Biol. 218 (1991) 427-447
287. Narvaez A., Dominguez E., Katakis I., Katz E., Ranjit K.T., Ben-Dov I., and Willner I. Microperoxidase-11-mediated reduction of hemoproteins: Electrocatalyzed reduction of cytochrome c, myoglobin and hemoglobin and electrocatalytic reduction of nitrate in the presence of cytochrome-dependent nitrate reductase. J. Electroanal. Chem. 430 (1997) 227-233
288. Newcomb E.H. Effect of auxin on ascorbic acid oxidase activity in tobacco pith cells. P. Soc. Exp. Biol. Med. 76 (1951) 504-509
289. Nicholls D.G., and Ferguson S.J. Bioenergetics 3 (2002), Academic Press, Elsevier, Amsterdam
290. Nistor C., Emnéus J., Gorton L., and Ciucu A. Improved stability and altered selectivity of tyrosinase-based graphite electrodes for detection of phenolic compounds. Anal. Chim. Acta 387 (1999) 309-326
291. 4S], the catalytic site in nitrous oxide reductase, by EPR spectroscopy, Dalton Trans. 996-1002.
292. Ohsaka, T., M. Shioda, F. Matsumoto, T. Okajima, F. Kitamura, and K. Tokuda, 1996, Electrode reaction of superoxide dismutase at cysteine-modified gold electrodes, Electron Transfer in Proteins and Supramolecular Assemblies at Interfaces, March 17-20, Yokohama National University, Kanagawa, P-33.
293. Ohsaka, T., Y. Tian, M. Shioda, S. Kasahara and T. Okajima, 2002, A superoxide dismutase-modified electrode that detects superoxide ion, Chem. Commun. 990-991.
294. Önnerfjord P., Emnéus J., Marko-Varga G., Gorton L., Ortega F., and Domínguez E. Tyrosinase graphite-epoxy-based composite electrodes for detection of phenols. Biosens. Bioelectron. 10 (1995) 607-619
295. Ortega F., Domínguez E., Johansson E., Emnéus J., Gorton L., and Marko-Varga G. Phenol oxidase based biosensors as selective detection units in column liquid chromatography for the determination of phenolic compounds. J. Chromatogr. 675 (1994) 65-78
296. Ortega F., Domínguez E., Jönsson-Pettersson G., and Gorton L. An amperometric determination of phenolic compounds using a tyrosinase graphite electrode in a FIA system. J. Biotechnol. 31 (1993) 289-300
297. Ortel T.L., Takahashi N., and Putnam F.W. Structural model of human ceruloplasmin based on internal triplication, hydrophilic/hydrophobic character, and secondary structure of domains. Proc. Natl. Acad. Sci. USA 81 (1984) 4761-4765
298. Pacheco A., Hazzard J.T., Tollin G., and Enemark J.H. The pH effect of intramolecular electron transfer rates in sulfite oxidase at high and low anion concentrations. J. Biol. Inorg. Chem. 4 (1999) 390-401
299. Paddock R.M., and Bowden E.F. Electrocatalytic reduction of hydrogen peroxide via direct electron transfer from pyrolytic graphite electrodes to irreversibly adsorbed cytochrome c peroxidase. J. Electroanal. Chem. 260 (1989) 487-494
300. Page C.C., Moser C.C., Chen X., and Dutton P.L. Natural engineering principles of electron tunneling in biological oxidation-reduction. Nature 402 (1999) 47-52
301. Paice M., Bourbonnais R., Renaud S., Labonte S., Sacciadis G., Berry R., Amann M., Candussio A., and Mueller R. Pilot plant bleaching trials with laccase and mediator. Prog. Biotechnol. 21 (2002) 203-211
302. Palmer A.E., Szilagyi R.K., Cherry J.R., Jones A., Xu F., and Solomon E.I. Spectroscopic characterization of the Leu513His variant of fungal laccase: Effect of increased axial ligand interaction on the geometric and electronic structure of the type 1 Cu site. Inorg. Chem. 42 (2003) 4006-4017
303. Palmore G.T.R., and Kim H.-H. Electro-enzymic reduction of dioxygen to water in the cathode compartment of a biofuel cell. J. Electroanal. Chem. 464 (1999) 110-117
304. Pappa H., Li H., Sundaramoorthy M., Arciero D., Hooper A., and Poulos T.L. Crystallization and preliminary crystallographic analysis of cytochrome c553 peroxidase from Nitrosomonas europaea. J. Struct. Biol. 116 (1996) 429-431
305. Pappa H., Tajbaksh S., Saunders A., Pielak G., and Poulos T. Probing the cytochrome c peroxidase - cytochrome c electron transfer reaction using site specific cross-linking. Biochemistry 35 (1996) 4837-4845
306. Pardo-Yissar V., Katz E., Willner I., Kotlyar A.B., Sanders C., and Lill H. Biomaterial engineered electrodes for bioelectronics. Faraday Discuss 116 (2000) 119-134
307. Parellada J., Domínguez E., and Fernández V.M. Amperometric flow injection determination of fructose in honey with a carbon paste sensor based on fructose dehydrogenase. Anal. Chim. Acta 330 (1996) 71-77
308. Pershad H.R., Hirst J., Cochran B., Ackrell B.A.C., and Armstrong F.A. Voltammetric studies of bidirectional catalytic electron transport in Escherichia coli succinate dehydrogenase: Comparison with the enzyme from beef heart mitochondria. Biochim. Biophys. Acta 1412 (1999) 262-272
309. Peter, M.G. and U. Wollenberger, 1997, Phenol-oxidizing enzymes: Mechanisms and applications in biosensors. Frontiers in Biosensorics,Vol. 1, Eds. F.W. Scheller, F. Schubert and J. Fedrowitz, Birkhäuser, Basel, pp. 63-82.
310. Petersen A., and Steckhan E. Continuous indirect electrochemical regeneration of galactose oxidase. Bioorgan. Med. Chem. 7 (1999) 2203-2208
311. Petersen L.C., and Degn H. Steady-state kinetics of laccase from Rhus vernicifera. Biochim. Biophys. Acta 526 (1978) 85-92
312. Pinho D., Besson S., Brondino C.D., Pereira E., de Castro B., and Moura I. Two azurins with unusual redox and spectroscopic properties isolated from the Pseudomonas chlororaphis strains DSM 50083T and DSM 50135. J. Inorg. Biochem. 98 (2004) 276-286
313. Piontek K., Antorini M., and Choinowski T. Crystal structure of a laccase from the fungus Trametes versicolor at 1.90 Å resolution containing a full complement of coppers. J. Biol. Chem. 277 (2002) 37663-37669
314. Poulos T.L., Patterson W.R., and Sundaramoorthy M. The crystal structure of ascorbate and manganese peroxidases: The role of non-heme metal in the catalytic mechanism. Biochem. Soc. Trans. 23 (1995) 228-232
315. Presnova G., Grigorenko V., Egorov A., Ruzgas T., Lindgren A., Gorton L., and Börchers T. Direct heterogeneous electron transfer of recombinant horseradish peroxidases on gold. Farad. Discuss. 116 (2000) 281-289
316. Puig D., Ruzgas T., Emnéus J., Gorton L., Marko-Varga G., and Barceló D. Characterization of tyrosinase-Teflon/graphite composite electrodes for determination of catechol in environmental matrix. Electroanalysis 8 (1996) 885-890
317. Rajesh, Takashima W., and Kaneto K. Amperometric phenol biosensor based on covalent immobilization of tyrosinase onto an electrochemically prepared novel copolymer poly (N-3-aminopropyl pyrrole-co-pyrrole) film. Sens. Actuat. B: Chem. 102 (2004) 271-277
318. Ramanavicius A., Habermüller K., Csöregi E., Laurinavicius V., and Schuhmann W. Polypyrrole-entrapped quinohemoprotein alcohol dehydrogenase. Evidence for direct electron transfer via conducting-polymer chains. Anal. Chem. 71 (1999) 3581-3586
319. Ramos, E., Johnson, T., Martin, M., Gannon, A. and Dorman, S., 2003, Formal reduction potentials of oxygen-binding proteins, 55th Southeast Regional Meeting of the American Chemical Society, Atlanta, GA, USA, 988.
320. Razumas V., Gudavicius A., and Kulys J. Redox conversion of peroxidase on surface-modified gold electrode. J. Electroanal. Chem. 151 (1983) 311-315
321. Razumas V., Gudavicius A., and Kulys J. Kinetics of peroxidase redox conversion of viologen-modified gold electrodes. J. Electroanal. Chem. 198 (1986) 81-87
322. Razumas V., Kazlauskaite J., Ruzgas T., and Kulys J. Bioelectrochemistry of microperoxidases. Bioelectrochem. Bioenerg. 28 (1992) 159-176
323. Razumiene J., Niculescu M., Ramanavicius A., Laurinavicius V., and Csöregi E. Direct bioelectrocatalysis at carbon electrodes modified with quinohemoprotein alcohol dehydrogenase from Gluconobacter sp. 33. Electroanalysis 14 (2002) 43-49
324. Reid M.E. Relation of vitamin C to cell size in the growing region of the primary root of cowpea seedlings. Am. J. Bot. 28 (1941) 410-415
325. Reinhammar, B., 1984, Laccase. Copper Proteins Copper Enzymes, Vol. 3, Ed. R. Lonti, CRC, Boca Raton, pp. 1-35.
326. Reinhammar B., and Vänngård T.I. Electron-accepting sites in Rhus vernicifera laccase as studied by anaerobic oxidation-reduction titrations. Eur. J. Biochem. 18 (1971) 463-468
327. Reinhammar B.R.M. Oxidation-reduction potentials of the electron acceptors in laccases and stellacyanin. Biochim. Biophys. Acta 275 (1972) 245-259
328. Reiss P., and Vellinger E. The potential of the arrest of multiplication of the sea urchin egg. Arch. Phys. Biol. 7 (1929) 80-101
329. Rekha K., Gouda M.D., Thakur M.S., and Karanth N.G. Ascorbate oxidase-based amperometric biosensor for organophosphorous pesticide monitoring. Biosens. Bioelectron. 15 (2000) 499-502
330. Rhoten M.C., Burgess J.D., and Hawkridge F.M. Temperature and pH effects on cytochrome c oxidase immobilized in an electrode-supported lipid bilayer membrane. Electrochim. Acta 45 (2000) 2855-2860
331. Rhoten M.C., Burgess J.D., and Hawkridge F.M. The reaction of cytochrome c from different species with cytochrome c oxidase immobilized in an electrode supported lipid bilayer membrane. J. Electroanal. Chem. 534 (2002) 143-150
332. Rhoten M.C., Hawkridge F.M., and Wilczek J. The reaction of cytochrome c with bovine and Bacillus stearothermophilus cytochrome c oxidase immobilized in electrode-supported lipid bilayer membranes. J. Electroanal. Chem. 535 (2002) 97-106
333. Riklin A., Katz E., Willner I., Stocker A., and Bückmann A. Improving enzyme-electrode contacting by redox modification of cofactors. Nature 376 (1995) 672-675
334. Rodkey F.L., and Ball E.G. Oxidation-reduction potentials of the cytochrome c system. J. Biol. Chem. 182 (1950) 17-28
335. Rodriguez-López J.N., Tudela J., Varón R., García-Carmona F., and García-Cánovas F. Analysis of a kinetic model for melanin biosynthesis pathway. J. Biol. Chem. 267 (1992) 3801-3810
336. Rogers M.S., and Dooley D.M. Post-translationally modified tyrosines from galactose oxidase and cytochrome c oxidase. Adv. Protein Chem. 58 (2001) 387-436
337. Rorabacher D.B. Electron transfer by copper centers. Chem. Rev. 104 (2004) 651-697
338. Rowe D.J.F., Watson I.D., Williams J., and Berry D.J. The clinical use and measurement of theophylline. Ann. Clin. Biochem. 25 (1988) 4-26
339. Roy B.P., Dumonceaux T., Koukoulas A.A., and Archibald F.S. Purification and characterization of cellobiose dehydrogenases from the white rot fungus Trametes versicolor. Appl. Environ. Microbiol. 62 (1996) 4417-4427
340. Rusling J.F. Enzyme bioelectrochemistry in cast biomembrane-like films. Acc. Chem. Res. 31 (1998) 363-369
341. Ruzgas T., Csöregi E., Emnéus J., Gorton L., and Marko-Varga G. Peroxidase-modified electrodes: Fundamentals and application. Anal. Chim. Acta 330 (1996) 123-138
342. Ruzgas T., Gaigalas A., and Gorton L. Diffusionless electron transfer of microperoxidase-11 on gold electrodes. J. Electroanal. Chem. 469 (1999) 123-131
343. Ruzgas T., Gorton L., Emnéus J., Csörgi E., and Marko-Varga G. Direct bioelectrocatalytic reduction of hydrogen peroxide at chloroperoxidase-modified graphite electrode. Anal. Proc. 32 (1995) 207-208
344. Ruzgas T., Gorton L., Emnéus J., and Marko-Varga G. Kinetic models of horseradish peroxidase action on a graphite electrode. J. Electroanal. Chem. 391 (1995) 41-49
345. Ruzgas T., Lindgren A., Gorton L., Hecht H.-J., Reichelt J., and Bilitewski U. Electrochemistry of peroxidases. In: Brajter-Toth A., and Chambers J.Q. (Eds). Electroanalytical Methods for Biological Materials (2002), Marcel Decker, New York 233-254
346. Ruzgas T., Wong L., Gaigalas A.K., and Vilker V.L. Electron transfer between surface-confined cytochrome c and an N-acetylcysteine-modified gold electrode. Langmuir 14 (1998) 7298-7305
347. Sakurai, T., 1996, Cyclic voltammetry of cucumber ascorbate oxidase, Chem. Lett. 481-482.
348. Sakurai T., Nose F., Fujiki T., and Suzuki S. Reduction and oxidation processes of blue copper proteins, azurin, pseudoazurin, umecyanin, stellacyanin, plantacyanin, and plastocyanin approached by cyclic and potential step voltammetries. Bull. Chem. Soc. Jpn. 69 (1996) 2855-2862
349. Sakurai T., Zhan L., Fujita T., Kataoka K., Shimizu A., Samejima T., and Yamaguchi S. Authentic and recombinant bilirubin oxidases are in different resting forms. Biosci. Biotechnol. Biochem. 67 (2003) 1157-1159
350. Samejima M., and Eriksson K.-E. A comparison of the catalytic properties of cellobiose:quinone oxidoreductase and cellobiose oxidase from Phanerochaete chrysosporium. Eur. J. Biochem. 207 (1992) 103-107
351. Santucci R., Ferri T., Morpurgo L., Savini I., and Avigliano L. Unmediated heterogeneous electron transfer reaction of ascorbate oxidase and laccase at a gold electrode. Biochem. J. 332 (1998) 611-615
352. Scheller F.W., Wollenberger U., Lei C., Jin W., Ge B., Lehmann C., Lisdat F., and Fridman V. Bioelectrocatalysis by redox enzymes at modified electrodes. Rev. Mol. Biotechnol. 82 (2002) 411-424
353. Schlereth D.D. Biosensors based on self-assembled monolayers. In: Gorton L. (Ed). Biosensors and Modern Biospecific Analytical Techniques Vol. XLIV (2005), Elsevier, Amsterdam 1-63
354. Schneider P., Caspersen M.B., Mondorf K., Halkier T., Skov L.K., Østergaard P.R., Brown K.M., Brown S.H., and Xu F. Characterization of a Coprinus cinereus laccase. Enzyme Microb. Technol. 25 (1999) 502-508
355. Schuhmann W. Amperometric enzyme biosensors based on optimized electron-transfer pathways and non-manual immobilization procedures. Rev. Mol. Biotechnol. 82 (2002) 425-441
356. Schuhmann W., Zimmermann H., Habermüller K., and Laurinavicius V. Electron-transfer pathways between redox enzymes and electrodes surfaces: Reagentless biosensors based on thiol-monolayer-bound and polypyrrole-entrapped enzymes. Farad. Discuss. 116 (2000) 245-255
357. Schuller D.J., Ban N., van Huystee R.B., McPherson A., and Poulos T.L. The crystal structure of peanut peroxidase. Structure 4 (1996) 311-321
358. Schumacher J.T., Hecht H.-J., Dengler U., Reichelt J., and Bilitewski U. Direct electron transfer observed for peroxidase to screen-printed graphite electrodes. Electroanalysis 13 (2001) 779-785
359. Scott D.L., and Bowden E.F. Enzyme-substrate kinetics of adsorbed cytochrome c peroxidase on pyrolytic graphite electrodes. Anal. Chem. 66 (1994) 1217-1223
360. Scott D.L., Paddock R.M., and Bowden E.F. The electrocatalytic enzyme function of adsorbed cytochrome c peroxidase on pyrolytic graphite. J. Electroanal. Chem. 341 (1992) 307-321
361. Scott, R.A. and A.G. Mauk, Eds., 1996, Cytochrome c: A Multidisciplinary Approach, University Science Books, Sausalito.
362. Sezgintürk M.K., and Dinckaya E. An amperometric inhibitor biosensor for the determination of reduced glutathione (GSH) without any derivatization in some plants. Biosens. Bioelectron. 19 (2004) 835-841
363. Sharma S.K., Singhal R., Malhotra B.D., Sehgal N., and Kumar A. Lactose biosensor based on Langmuir-Blodgett films of poly(3-hexyl thiophene). Biosens. Bioelectron. 20 (2004) 651-657
364. Sharma S.K., Singhal R., Malhotra B.D., Sehgal N., and Kumar A. Langmuir-Blodgett film-based biosensor for estimation of galactose in milk. Electrochim. Acta 48 (2004) 2479-2485
365. Shimizu A., Kwon J.H., Sasaki T., Satoh T., Sakurai N., Sakurai T., Yamaguchi S., and Samejima T. Myrothecium verrucaria bilirubin oxidase and its mutants for potential copper ligands. Biochemistry 38 (1999) 3034-3042
366. Shin K.-S., and Lee Y.-J. Purification and characterization of a new member of the laccase family from the white-rot basidiomycete Coriolus hirsutus. Arch. Biochem. Biophys. 384 (2000) 109-115
367. Shipovskov S., Ferapontova E.E., Gazaryan I.G., and Ruzgas T. Recombinant horseradish peroxidase- and cytochrome c-based two-electrode system for detection of superoxide radicals. Bioelectrochemistry 63 (2004) 277-280
368. Shleev S., Christenson A., Serezhenkov V., Burbaev D., Yaropolov A., Gorton L., and Ruzgas T. Electrochemically controlled redox transformations of T1 and T2 copper sites in native Trametes hirsuta laccase at bare gold electrode. Biochem. J. 385 (2005) 745-754
369. Shleev S., Jarosz-Wilkolazka A., Khalunina A., Morozova O., Yaropolov A., Ruzgas T., and Gorton L. Direct heterogeneous electron transfer reactions of laccases from different origins on carbon electrodes. Bioelectrochemistry 67 (2005) 115-124
370. Shleev S., Tkac J., Christenson A., Ruzgas T., Yaropolov A.I., Whittaker J., and Gorton L. Direct electron transfer between copper containing proteins and electrodes. Biosens. Bioelectron, 20 (2005) 2517-2554
371. Shleev S., El Kasmi A., Ruzgas T., and Gorton L. Direct heterogeneous electron transfer reactions of bilirubin oxidase at a spectrographic graphite electrode. Electrochem. Commun. 6 (2004) 934-939
372. Shleev S.V., Morozova O.V., Nikitina O.V., Gorshina E.S., Rusinova T.V., Serezhenkov V.A., Burbaev D.S., Gazaryan I.G., and Yaropolov A.I. Comparison of physico-chemical characteristics of four laccases from different basidiomycetes. Biochimie 86 (2004) 693-703
373. Shlev S.V., Zaitseva E.A., Gorshina E.S., Morozova O.V., Serezhenkov V.A., Burbaev D.S., Kuznetsov B.A., and Yaropolov A.I. Spectral and electrochemical study of laccases from basidiomycetes. Moscow University Chem. Bull. 44 (2003) 35-39
374. Shoham B., Migron Y., Riklin A., Willner I., and Tartakovsky B. A bilirubin biosensor based on a multilayer network enzyme electrode. Biosens. Bioelectron. 10 (1995) 341-352
375. Shumyantseva V.V., Ivanov Y.D., Bistolas N., Scheller F.W., Archakov A.I., and Wollenberger U. Direct electron transfer of cytochrome P450 2B4 at electrodes modified with nonionic detergent and colloidal clay nanoparticles. Anal. Chem. 76 (2004) 6046-6052
376. Smith M., Thurston C.F., and Wood D.A. Fungal laccases: role in delignification and possible industrial applications. In: Messerschmidt A. (Ed). Multi-Copper Oxidases (1997), World Scientific, Singapore 201-224
377. Solomon E.I., Szilagyi R.K., George S.D., and Basumallick L. Electronic structures of metal sites in proteins and models: contributions to function in blue copper proteins. Chem. Rev. 104 (2004) 419-458
378. Solomon E.I., Baldwin M.J., and Lowery M.D. Electronic structures of active sites in copper proteins: Contributions to reactivity. Chem. Rev. 92 (1992) 521-542
379. Solomon E.I., Sundaram U.M., and Machonkin T.E. Multicopper oxidases and oxygenases. Chem. Rev. 96 (1996) 2563-2605
380. Song S., Clark R., Bowden E., and Tarlov M. Characterisation of cytochrome c/alkanethiolate structures prepared by self-assembly on gold. J. Phys. Chem. 97 (1993) 6564-6572
381. 2-electroreduction biocatalyst superior to platinum and a biofuel cell operating at 0.88 V. J. Am. Chem. Soc. 126 (2004) 8368-8369
382. 2. Anal. Chim. Acta 243 (1991) 167-171
383. Stigter E.C.A., Carnicero A.M., van der Lugt J.P., and Somers W.A.C. Electron transfer between galactose oxidase and an electrode via a redox polymer network. Biotechnol. Techniq. 10 (1996) 469-474
384. Stoica L., Dimcheva N., Haltrich D., Ruzgas T., and Gorton L. Electrochemical investigation of direct electron transfer between cellobiose dehydrogenase from new fungal sources on Au electrodes modified with different alkanethiols. Biosens. Bioelectron. 20 (2005) 2010-2018
385. Stoica L., Lindgren-Sjölin A., Ruzgas T., and Gorton L. Ultrasensitive biosensor based on cellobiose dehydrogenase (CDH) for detection of catecholamines. Anal. Chem. 76 (2004) 4690-4696
386. Streffer K., Vijgenboom E., Tepper A.W.J.W., Makower A., Scheller F.W., Canters G.W., and Wollenberger U. Determination of phenolic compounds using recombinant tyrosinase from Streptomyces antibioticus. Anal. Chim. Acta 427 (2001) 201-210
387. Sucheta A., Ackrell B.A.C., Cochran B., and Armstrong F.A. Diode-like behavior of a mitochondrial electron-transport enzyme. Nature 356 (1992) 361-362
388. Sucheta A., Cammack R., Weiner J., and Armstrong F.A. Reversible electrochemistry of fumarate reductase immobilized on an electrode surface: Direct voltammetric observations of redox centers and their participation in rapid catalytic electron transport. Biochemistry 32 (1993) 5455-5465
389. Sullivan E.P., Huzzard J.T., Tollin G., and Enemark J.H. Electron-transfer in sulfite oxidase - effects of pH and anions on transient kinetics. Biochemistry 32 (1993) 12465-12470
390. Sundaramoorthy M., Kishi K., Gold M.H., and Poulos T.L. Crystal structures of substrate-binding site mutants of manganese peroxidase. J. Biol. Chem. 272 (1997) 17574-17580
391. Sundaramoorthy M., Terner J., and Poulos T.L. The crystal structure of chloroperoxidase: A heme peroxidase-cytochrome P450 functional hybrid. Structure 3 (1995) 1367-1377
392. Surma-Slusarska B., and Leks-Stepien J. TCF bleaching of kraft pulps with laccase and xylanase. J. Wood Chem. Technol. 21 (2001) 361-370
393. Szeponik J., Möller B., Pfeiffer D., Lisdat F., Wollenberger U., Makower A., and Scheller F.W. Ultrasensitive bienzyme sensor for adrenaline. Biosens. Bioelectron. 12 (1997) 947-952
394. Takahashi N., Ortel T.L., and Putnam F.W. Single-chain structure of human ceruloplasmin: The complete amino acid sequence of the whole molecule. Proc. Natl. Acad. Sci. USA 81 (1984) 390-394
395. Taniguchi I., Ishimoto H., Miyagawa K., Iwai M., Nagai H., Hanazono H., Taira K., Kubo A., Nishikawa A., Nishiyama K., Dursun Z., Hareau G.P.J., and Tazaki M. Surface functions of 2-mercaptopyridine, 2-mercaptopyrazine and 2-mercaptoquinoxaline modified Au (1 1 1) electrodes for direct rapid electron transfer of cytochrome c. Electrochem. Commun. 5 (2003) 857-861
396. Tarasevich M.R. Ways of using enzymes for acceleration of electrochemical reactions. Bioelectrochem. Bioenerg. 6 (1979) 587-591
397. 2 electroreduction on the peroxidase-promoted electrodes. Russ. J. Electrochem. 37 (2001) 7-14
398. Tarasevich M.R., Bogdanovskaya V.A., and Kuznetsova L.N. Bioelectrocatalytic reduction of oxygen in the presence of laccase adsorbed on carbon electrodes. Russ. J. Electrochem. 37 (2001) 833-837
399. Tarasevich M.R., Bogdanovskaya V.A., Zagudaeva N.M., and Kapustin A.V. Composite materials for direct bioelectrocatalysis of the hydrogen and oxygen reactions in biofuel cells. Russ. J. Electrochem. 38 (2002) 335
400. Tarasevich M.R., Yaropolov A.I., Bogdanovskaya V.A., and Varfolomeev S.D. Electrocatalysis of a cathodic oxygen reduction by laccase. Bioelectrochem. Bioenerg. 6 (1979) 393-403
401. Tatsuma T., Ariyama K., and Oyama N. Kinetic analysis of electron transfer from a graphite coating to horseradish peroxidase. J. Electroanal. Chem. 446 (1998) 205-209
402. Tatsuma T., Mori H., and Fujishima A. Electron transfer from diamond electrodes to heme peptide and peroxidase. Anal. Chem. 72 (2000) 2919-2924
403. Tatsuma T., and Watanabe T. Peroxidase model electrodes - heme peptide-modified electrodes as reagentless sensors for hydrogen peroxide. Anal. Chem. 63 (1991) 1580-1585
404. Thuesen M.H., Farver O., Reinhammar B., and Ulstrup J. Cyclic voltammetry and electrocatalysis of the blue copper oxidase Polyporus versicolor laccase. Acta Chem. Scand. 52 (1998) 555-562
405. Tian Y., Mao L., Okajima T., and Ohsaka T. Superoxide dismutase-based third-generation biosensor for superoxide anion. Anal. Chem. 74 (2002) 2428-2434
406. Tian Y., Shioda M., Kasahara S., Okajima T., Mao L., Hisaboli T., and Ohsaka T. A facilitated electron transfer of copper-zinc superoxide dismutase (SOD) based on cysteine-bridged SOD electrode. Biochim. Biophys. Acta 1569 (2002) 151-158
407. Tian Y., Mao L., Okajima T., and Ohsaka T. Electrochemistry and electrocatalytic activities of superoxide dismutases at gold electrodes modified with a self-assembled monolayer. Anal. Chem. 76 (2004) 4162-4168
408. Tkac, J., T. Ruzgas and J. W. Whittaker, 2005, Direct electrode transfer reactions of galactose oxidase on modified gold electrodes, in manuscript.
409. Tkac J., Vostiar I., Gemeiner P., and Sturdik E. Indirect evidence of direct electron communication between the active site of galactose oxidase and a graphite electrode. Bioelectrochemistry 56 (2002) 23-25
410. Torimura, M., K. Kano, T. Ikeda and T. Ueda, 1997, Spectroelectrochemical characterization of quinohemoprotein alcohol dehydrogenase from Gluconobacter suboxydans, Chem. Lett. 525-526.
411. Toyama H., Mathews F.S., Adachi O., and Matsushita K. Quinohemoprotein alcohol dehydrogenases: Structure, function, and physiology. Arch. Biochem. Biophys. 428 (2004) 10-21
412. Tsujimura S., Fujita M., Tatsumi H., Kano K., and Ikeda T. Bioelectrocatalysis-based dihydrogen/dioxygen fuel cell operating at physiological pH. Phys. Chem. Chem. Phys. 3 (2001) 1331-1335
413. Tsujimura S., Wadano A., Kano K., and Ikeda T. Photosynthetic bioelectrochemical cell utilizing cyanobacteria and water-generating oxidase. Enz. Microb. Technol. 29 (2001) 225-231
414. 2 reduction to water at highly positive electrode potentials near neutral pH. Electrochem. Commun. 5 (2003) 138-141
415. Tsujimura S., Nakagawa T., Kano K., and Ikeda T. Kinetic study of direct bioelectrocatalysis of dioxygen reduction with bilirubin oxidase at carbon electrodes. Electrochemistry 72 (2004) 437-439
416. Tsukihara T., Aoyama H., Yamashita E., Tomizaki T., Yamaguchi H., Shinzawa-Itoh K., Nakashima R., Yaono R., and Yoshikawa S. Structures of metal sites of oxidized bovine heart cytochrome c oxidase at 2.8 Å. Science 269 (1995) 1069-1074
417. 3 from Shewanella frigidimarina NCIMB400. Biochemistry 38 (1999) 3302-3309
418. Updike S.J., and Hicks G.P. The enzyme electrode. Nature 214 (1967) 986-988
419. Varfolomeev S.D., Kurochkin I.N., and Yaropolov A.I. Direct electron transfer effect biosensors. Biosens. Bioelectron. 11 (1996) 863-871
420. Vrbova E., Peckova J., and Marek M. Preparation and utilization of a biosensor based on galactose oxidase. Coll. Czech. Chem. Commun. 57 (1992) 2287-2294
421. Wang J., and Lin Y. On-line organic-phase enzyme detector. Anal. Chim. Acta 271 (1993) 53-58
422. Wang J., and Ozsoz M. A polishable amperometric biosensor for bilirubin. Electroanalysis 2 (1990) 647-650
423. Wang L., Wang J., and Zhou F. Direct electrochemistry of catalase at a gold electrode modified with single-wall carbon nanotubes. Electroanalysis 16 (2004) 627-632
424. White G.A., and Krupka R.M. Ascorbic acid oxidase and ascorbic acid oxygenase of Myrothecium verrucaria. Arch. Biochem. Biophys. 110 (1965) 448-461
425. Whitesides G.M., Mathias J.P., and Seto C.T. Molecular self-assembly and nanochemistry: A chemical strategy for the synthesis of nanostructures. Science 254 (1991) 1312-1319
426. Whittaker M.M., and Whittaker J.W. The active site of galactose oxidase. J. Biol. Chem. 263 (1988) 6074-6080
427. Willner I., Heleg-Shabtai V., Blonder R., Katz E., Tao G., Bückmann A.F., and Heller A. Electrical wiring of glucose oxidase by reconstitution of FAD-modified monolayers assembled onto Au electrodes. J. Am. Chem. Soc. 118 (1996) 10321-10322
428. Willner I., Katz E., and Willner B. Electrical contact of redox enzyme layers associated with electrodes: Routes to amperometric biosensors. Electroanalysis 9 (1997) 965-977
429. Wollenberger, U., 2005, Third generation biosensors - integrating recognition and transduction in electrochemical sensors. Biosensors and Modern Biospecific Analytical Techniques, Vol. XLIV, Ed. L. Gorton, Elsevier, Amsterdam, pp. 65-130.
430. Wollenberger U., Bogdanovskaya V., Bobrin S., Scheller F., and Tarasevich M. Enzyme electrodes using bioelectrocatalytic reduction of hydrogen peroxide. Anal. Lett. 23 (1990) 1795-1808
431. Wollenberger U., Wang J., Ozsoz M., Gonzalez Romero E., and Scheller F. Bulk modified enzyme electrodes for reagentless detection of peroxides. Bioelectrochem. Bioenerg. 26 (1991) 287-296
432. Wong Y., and Yu J. Laccase-catalyzed decolorization of synthetic dyes. Water Res. 33 (1999) 3512-3520
433. Wood J.D., and Wood P.M. Homology between cellobiose oxidase from Phanerochaete chrysosporium and other proteins. Biochem. Soc. Trans. 20 (1992) 109S
434. Wright C., and Sykes A.G. Interconversion of Cu(I) and Cu(II) forms of galactose oxidase: Comparison of reduction potentials. J. Inorg. Biochem. 85 (2001) 237-243
435. Wu X.-Q., Meng X.-Y., Wang Z.-S., and Zhang Z.-R. Study of the direct electron transfer process of superoxide dismutase. Bioelectrochem. Bioenerg. 48 (1999) 227-231
436. Wynn R.M., Sarkar H.K., Holwerda R.A., and Knaff D.B. Fluorescence associated with the type 3 copper center of laccase. FEBS Lett. 156 (1983) 23-28
437. Xiao Y., Patolsky F., Katz E., Hainfeld J.F., and Willner I. "Plugging into enzymes": Nanowiring of redox enzymes by a gold particle. Science 299 (2003) 1877-1881
438. Xu F., Berka R.M., Wahleithner J.A., Nelson B.A., Shuster J.R., Brown S.H., Palmer A.E., and Solomon E.I. Site-directed mutations in fungal laccase: Effect on redox potential, activity and pH profile. Biochem. J. 334 (1998) 63-70
439. Xu F., Kulys J.J., Duke K., Li K., Krikstopaitis K., Deussen H.J., Abbate E., Galinyte V., and Schneider P. Redox chemistry in laccase-catalyzed oxidation of N-hydroxy compounds. Appl. Environ. Microbiol. 66 (2000) 2052-2056
440. Xu F., Palmer A.E., Yaver D.S., Berka R.M., Gambetta G.A., Brown S.H., and Solomon E.I. Targeted mutations in a Trametes villosa laccase, axial perturbations of the T1 copper. J. Biol. Chem. 274 (1999) 12372-12375
441. Xu F., Shin W., Brown S.H., Wahleithner J.A., Sundaram U.M., and Solomon E.I. A study of a series of recombinant fungal laccases and bilirubin oxidase that exhibit significant differences in redox potential, substrate specificity, and stability. Biochim. Biophys. Acta 1292 (1996) 303-311
442. Yabuki S., and Mizutani F. d-Fructose sensing electrode based on electron transfer of d-fructose dehydrogenase at colloidal gold-enzyme modified electrode. Electroanalysis 9 (1997) 23-25
443. Yamada Y., Aida K., and Uemura T. Enzymatic studies on the oxidation of sugar and sugar alcohol. I. Purification and properties of particle-bound fructose dehydrogenase. J. Biochem. 61 (1967) 636-646
444. Yamaguchi T., Murakami Y., Yokoyama K., Komura H., and Tamiya E. Electrochemical characterization of galactose oxidase coupled with ferrocene derivatives. Denki Kagaku 63 (1995) 1179-1182
445. Yamamoto K., Takagi K., Kano K., and Ikeda T. Bioelectrocatalytic detection of histamine using quinohemoprotein amine dehydrogenase and the native electron acceptor cytochrome c-550. Electroanalysis 13 (2001) 375-379
446. Yanai H., Miki K., Ikeda T., and Matsushita K. Bioelectrocatalysis by alcohol dehydrogenase from Acetobacter aceti adsorbed on bare and chemically modified electrodes. Denki Kagaku 62 (1994) 1247-1248
447. 2-electrooxidation with immobilized hydrogenase. Bioelectrochem. Bioenerg. 12 (1984) 267-277
448. Yaropolov A.I., Kharybin A.N., Emnéus J., Marko-Varga G., and Gorton L. Flow injection analysis of phenols at a graphite electrode modified with co-immobilized laccase and tyrosinase. Anal. Chim. Acta 308 (1995) 137-144
449. Yaropolov A.I., Kharybin A.N., Emnéus J., Marko-Varga G., and Gorton L. Electrochemical properties of some copper-containing oxidases. Bioelectrochem. Bioenerg. 40 (1996) 49-57
450. Yaropolov A.I., Malovik V., Varfolomeev S.D., and Berezin I.V. Electroreduction of hydrogen peroxide on an electrode with immobilized peroxidase. Dokl. Akad. Nauk. SSSR 249 (1979) 1399-1401
451. Yaropolov A.I., Naki A., Pepanyan G.S., Saenko E.L., and Varfolomeev S.D. Mechanism of laccase activation in pre-steady-state reaction stage. Moscow University Chem. Bull. 27 (1986) 93-96
452. Yaropolov A.I., Skorobogat'ko O.V., Vartanov S.S., and Varfolomeyev S.D. Laccase. Properties, catalytic mechanism, and applicability. Appl. Biochem. Biotechnol. 49 (1994) 257-280
453. Ye B., and Zhou X. Direct electrochemical redox of tyrosinase at silver electrodes. Talanta 44 (1997) 831-836
454. Yeh, P. and T. Kuwana, 1977, Reversible electrode reaction of cytochrome c, Chem. Lett. 1145-1148.
455. Yu A., and Caruso F. Thin films of polyelectrolyte-encapsulated catalase microcrystals for biosensing. Anal. Chem. 75 (2003) 3031-3037
456. Yu X., Chattopadhyay D., Galeska I., Papadimitrakopoulos F., and Rusling J.F. Peroxidase activity of enzymes bound to the ends of single-wall carbon nanotube forest electrodes. Electrochem. Commun. 5 (2003) 408-411
457. Yu X., Sotzing G.A., Papadimitrakopoulos F., and Rusling J.F. Wiring of enzymes to electrodes by ultrathin conductive polyion underlayers: Enhanced catalytic response to hydrogen peroxide. Anal. Chem. 75 (2003) 4565-4571
458. Zaitsev V., Zaitseva I., Card G., Bax B., Ralph A., and Lindley P. The three-dimensional structure of human ceruloplasmin at 3.0 Å resolution. Fold. Design 1 (1996) S71
459. Zamocky M., Hallberg M., Ludwig R., Divne C., and Haltrich D. Ancestral gene fusion in cellobiose dehydrogenases reflects a specific evolution of GMC oxidoreductases in fungi. Gene 338 (2004) 1-14
460. Zeravik J., Ruzgas T., and Franek M. A highly sensitive flow-through amperometric immunosensor based on the peroxidase chip and enzyme-channeling principle. Biosens. Bioelectron. 18 (2003) 1321-1327
461. Zhang J., Chi Q., Kuznetsov A.M., Hansen A.G., Wackerbarth H., Christensen H.E.M., Andersen J.E.T., and Ulstrup J. Electronic properties of functional biomolecules at metal/aqueous solution interfaces. J. Phys. Chem. B 106 (2002) 1131-1152
462. Zhang J.D., Chi Q.J., Albrecht T., Kuznetsov A.M., Grubb M., Hansen A.G., Wackerbarth H., Welinder A.C., and Ulstrup J. Electrochemistry and bioelectrochemistry towards the single-molecule level. Theoretical notions and systems 50 (2005) 3143-3159
463. Zhang Z., Chouchane S., Magliozzo R.S., and Rusling J.F. Direct voltammetry and catalysis with Mycobacterium tuberculosis catalase-peroxidase, peroxidases, and catalase in lipid films. Anal. Chem. 74 (2002) 163-170
464. Zhang W.J., and Li G.X. Third-generation biosensors based on direct electron transfer of proteins. Anal. Sci. 20 (2004) 603-609
465. 2 as the substrate. Anal. Chem. 76 (2004) 4093-4097
466. 3 on mercury, glassy carbon, and gold electrodes. Anal. Chem. 66 (1994) 3873-3881
467. Zherdev A.V., Bizova N.A., Yaropolov A.I., Lyubimova N.V., Morozova O.V., and Dzantiev B.B. Laccase from Coriolus hirsutus as alternative label for enzyme immunoassay: Determination of pesticide 2,4-dichlorophenoxyacetic acid. Appl. Biochem. Biotechnol. 76 (1999) 203-215
468. Zhou Y., Hu N., Zeng Y., and Rusling J.F. Heme protein-clay films: Direct electrochemistry and electrochemical catalysis. Langmuir 18 (2002) 211-219
469. Zimmermann H., Lindgren A., Schuhmann W., and Gorton L. Anisotropic orientation of horseradish peroxidase by reconstitution on a thiol-modified gold electrode. Chem. Eur. J. 6 (2000) 592-599