메뉴 건너뛰기




Volumn , Issue , 2010, Pages 237-255

The Importance of Enzymes: Benchmarks for Electrocatalysts

Author keywords

Active sites and fuel cell enzyme structures; Enzyme importance, benchmarks for electrocatalysts; Niche applications, new ideas and roles for enzyme fuel cells in self powered implantable sensors or logic gates

Indexed keywords


EID: 84885564674     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9780470630693.ch7     Document Type: Chapter
Times cited : (3)

References (40)
  • 1
    • 60849107722 scopus 로고    scopus 로고
    • Integrated enzyme-based biofuel cells-a review
    • I. Willner et al., Integrated enzyme-based biofuel cells-a review, Fuel Cells 9(1); 7-24 (2009).
    • (2009) Fuel Cells , vol.9 , Issue.1 , pp. 7-24
    • Willner, I.1
  • 2
    • 7544227821 scopus 로고    scopus 로고
    • Enzymatic biofuel cells for implantable and microscale devices
    • S. C. Barton, J. Gallaway, and P. Atanassov, Enzymatic biofuel cells for implantable and microscale devices, Chem. Rev. 104(10); 4867-4886 (2004).
    • (2004) Chem. Rev. , vol.104 , Issue.10 , pp. 4867-4886
    • Barton, S.C.1    Gallaway, J.2    Atanassov, P.3
  • 3
    • 49049118534 scopus 로고    scopus 로고
    • Enzymes as working or inspirational electrocatalysts for fuel cells and electrolysis
    • J. A. Cracknell, K. A. Vincent, and F. A. Armstrong, Enzymes as working or inspirational electrocatalysts for fuel cells and electrolysis, Chem. Rev. 108; 2439-2461 (2008).
    • (2008) Chem. Rev. , vol.108 , pp. 2439-2461
    • Cracknell, J.A.1    Vincent, K.A.2    Armstrong, F.A.3
  • 4
    • 84885532282 scopus 로고    scopus 로고
    • Miniature biological fuel cell that is operational under physiological conditions comprising enzymes, Patent Application WO WO, Therasense, Inc.
    • A. Heller et al., Miniature biological fuel cell that is operational under physiological conditions comprising enzymes, Patent Application WO WO, Therasense, Inc., (2003).
    • (2003)
    • Heller, A.1
  • 5
    • 34548270983 scopus 로고    scopus 로고
    • Rapid and efficient electrocatalytic CO2/CO interconversions by Carboxydothermus hydrogenoformans CO dehydrogenase I on an electrode
    • A. Parkin et al., Rapid and efficient electrocatalytic CO2/CO interconversions by Carboxydothermus hydrogenoformans CO dehydrogenase I on an electrode, J. Am. Chem. Soc. 129(34); 10328-10329 (2007).
    • (2007) J. Am. Chem. Soc. , vol.129 , Issue.34 , pp. 10328-10329
    • Parkin, A.1
  • 6
    • 49449111220 scopus 로고    scopus 로고
    • Reversible interconversion of carbon dioxide and formate by an electroactive enzyme
    • T. Reda et al., Reversible interconversion of carbon dioxide and formate by an electroactive enzyme, Proc. Natl. Acad. Sci. USA 105(31); 10654-10658 (2008).
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , Issue.31 , pp. 10654-10658
    • Reda, T.1
  • 7
    • 0037613548 scopus 로고    scopus 로고
    • Reversible, electrochemical interconversion ofNADH and NAD(+) by the Catalytic (I lambda) subcomplex of mitochondrial NADH: Ubiquinone oxidoreductase (Complex I)
    • Y. B. Zu, R. J. Shannon, and J. Hirst, Reversible, electrochemical interconversion ofNADH and NAD(+) by the Catalytic (I lambda) subcomplex of mitochondrial NADH: Ubiquinone oxidoreductase (Complex I), J. Am. Chem. Soc. 125(20); 6020-6021 (2003).
    • (2003) J. Am. Chem. Soc. , vol.125 , Issue.20 , pp. 6020-6021
    • Zu, Y.B.1    Shannon, R.J.2    Hirst, J.3
  • 8
    • 35748933836 scopus 로고    scopus 로고
    • Investigating and exploiting the electrocatalytic properties of hydrogenases
    • K. A. Vincent, A. Parkin, and F. A. Armstrong, Investigating and exploiting the electrocatalytic properties of hydrogenases, Chem. Rev. 107(10); 4366-4413 (2007).
    • (2007) Chem. Rev. , vol.107 , Issue.10 , pp. 4366-4413
    • Vincent, K.A.1    Parkin, A.2    Armstrong, F.A.3
  • 9
    • 49049115593 scopus 로고    scopus 로고
    • Direct electrochemistry of redox enzymes as a tool for mechanistic studies
    • C. Léger and P. Bertrand, Direct electrochemistry of redox enzymes as a tool for mechanistic studies, Chem. Rev. 108(7); 2379-2438 (2008).
    • (2008) Chem. Rev. , vol.108 , Issue.7 , pp. 2379-2438
    • Léger, C.1    Bertrand, P.2
  • 10
    • 0001398340 scopus 로고
    • Alternative view of enzyme reactions
    • USA
    • M. J. S. Dewar, Alternative view of enzyme reactions, Proc. Natl. Acad. Sci. USA 82(8); 2225 (1985).
    • (1985) Proc. Natl. Acad. Sci. , vol.82 , Issue.8 , pp. 2225
    • Dewar, M.J.S.1
  • 11
    • 39049132264 scopus 로고    scopus 로고
    • [FeFe]-hydrogenase-catalysed H2 production in a photoelectrochemical biofuel cell
    • M. Hambourger et al., [FeFe]-hydrogenase-catalysed H2 production in a photoelectrochemical biofuel cell, J. Am. Chem. Soc. 130, 2015-2022 (2008).
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 2015-2022
    • Hambourger, M.1
  • 12
    • 0037149937 scopus 로고    scopus 로고
    • Direct comparison of the electrocatalytic oxidation of hydrogen by an enzyme and a platinum catalyst
    • A. K. Jones et al., Direct comparison of the electrocatalytic oxidation of hydrogen by an enzyme and a platinum catalyst, Chem. Commun. 866-867 (2002).
    • (2002) Chem. Commun. , pp. 866-867
    • Jones, A.K.1
  • 13
    • 35748930865 scopus 로고    scopus 로고
    • Structure/function relationships of [NiFe]- and [FeFe]-hydrogenases
    • J. C. Fontecilla-Camps et al., Structure/function relationships of [NiFe]- and [FeFe]-hydrogenases, Chem. Rev. 107; 4273-4303 (2007).
    • (2007) Chem. Rev. , vol.107 , pp. 4273-4303
    • Fontecilla-Camps, J.C.1
  • 14
    • 35848964033 scopus 로고    scopus 로고
    • Fundamentals of H2 binding and reactivity on transition metals underlying hydrogenase function and H2 production and storage
    • G. J. Kubas, Fundamentals of H2 binding and reactivity on transition metals underlying hydrogenase function and H2 production and storage, Chem. Rev. 107(10); 4152-4205 (2007).
    • (2007) Chem. Rev. , vol.107 , Issue.10 , pp. 4152-4205
    • Kubas, G.J.1
  • 15
    • 0034685468 scopus 로고    scopus 로고
    • Photochemistry at the active site of the carbon monoxide inhibited form of the iron-only hydrogenase (CpI)
    • B. J. Lemon and J. W. Peters, Photochemistry at the active site of the carbon monoxide inhibited form of the iron-only hydrogenase (CpI), J. Am. Chem. Soc. 122(15); 3793-3794 (2000).
    • (2000) J. Am. Chem. Soc. , vol.122 , Issue.15 , pp. 3793-3794
    • Lemon, B.J.1    Peters, J.W.2
  • 16
    • 0039182024 scopus 로고    scopus 로고
    • Binding of exogenously added carbon monoxide at the active site of the iron-only hydrogenase (CpI) from Clostridium pasteurianum
    • B. J. Lemon and J.W. Peters, Binding of exogenously added carbon monoxide at the active site of the iron-only hydrogenase (CpI) from Clostridium pasteurianum, Biochemistry 38(40); 12969-12973 (1999).
    • (1999) Biochemistry , vol.38 , Issue.40 , pp. 12969-12973
    • Lemon, B.J.1    Peters, J.W.2
  • 17
    • 0038375489 scopus 로고    scopus 로고
    • Enzyme electrokinetics: Electrochemical studies of the anaerobic interconversions between active and inactive states of Allochromatium vinosum [NiFe]-hydrogenase
    • A. K. Jones et al., Enzyme electrokinetics: Electrochemical studies of the anaerobic interconversions between active and inactive states of Allochromatium vinosum [NiFe]-hydrogenase, J. Am. Chem. Soc. 125; 8505-8514 (2003).
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 8505-8514
    • Jones, A.K.1
  • 18
    • 28044470050 scopus 로고    scopus 로고
    • Electrocatalytic hydrogen oxidation by an enzyme at high carbon monoxide or oxygen levels
    • USA
    • K. A. Vincent et al., Electrocatalytic hydrogen oxidation by an enzyme at high carbon monoxide or oxygen levels, Proc. Natl. Acad. Sci. USA 102; 16951-16954 (2005).
    • (2005) Proc. Natl. Acad. Sci. , vol.102 , pp. 16951-16954
    • Vincent, K.A.1
  • 19
    • 40149096419 scopus 로고    scopus 로고
    • Enzymatic oxidation of H2 in Atmospheric O2: The electrochemistry of energy generation from trace H2 by aerobic microorganisms
    • J. A. Cracknell et al., Enzymatic oxidation of H2 in Atmospheric O2: The electrochemistry of energy generation from trace H2 by aerobic microorganisms, J. Am. Chem. Soc. 130; 424-425 (2008).
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 424-425
    • Cracknell, J.A.1
  • 20
    • 50149121231 scopus 로고    scopus 로고
    • In situ formation of an oxygen-evolving catalyst in neutral water containing phosphate and Co2{thorn}
    • M.W. Kanan and D. G. Nocera, In situ formation of an oxygen-evolving catalyst in neutral water containing phosphate and Co2{thorn}, Science 321(5892); 1072-1075 (2008).
    • (2008) Science , vol.321 , Issue.5892 , pp. 1072-1075
    • Kanan, M.W.1    Nocera, D.G.2
  • 21
    • 34547805717 scopus 로고    scopus 로고
    • O2 and N2O activation by bi-, tri-, and tetranuclear Cu clusters in biology
    • E. I. Solomon et al., O2 and N2O activation by bi-, tri-, and tetranuclear Cu clusters in biology, Acc. Chem. Res. 40(7); 581-591 (2007).
    • (2007) Acc. Chem. Res. , vol.40 , Issue.7 , pp. 581-591
    • Solomon, E.I.1
  • 22
    • 0346850034 scopus 로고    scopus 로고
    • Oxygen is electroreduced to water on a "wired" enzyme electrode at a lesser overpotential than on platinum
    • N. Mano et al., Oxygen is electroreduced to water on a "wired" enzyme electrode at a lesser overpotential than on platinum, J. Am. Chem. Soc. 125(50); 15290-15291 (2003).
    • (2003) J. Am. Chem. Soc. , vol.125 , Issue.50 , pp. 15290-15291
    • Mano, N.1
  • 23
    • 33846596556 scopus 로고    scopus 로고
    • Improved oxygen reduction activity on Pt3Ni(111) via increased surface site availability
    • V. R. Stamenkovic et al., Improved oxygen reduction activity on Pt3Ni(111) via increased surface site availability, Science 315(5811); 493-497 (2007).
    • (2007) Science , vol.315 , Issue.5811 , pp. 493-497
    • Stamenkovic, V.R.1
  • 24
    • 33646230567 scopus 로고    scopus 로고
    • Methanol tolerance of a mediated, biocatalytic oxygen cathode
    • Y. Sun and S. C. Barton, Methanol tolerance of a mediated, biocatalytic oxygen cathode, J. Electroanal. Chem. 590(1); 57-65 (2006).
    • (2006) J. Electroanal. Chem. , vol.590 , Issue.1 , pp. 57-65
    • Sun, Y.1    Barton, S.C.2
  • 25
    • 0035812365 scopus 로고    scopus 로고
    • A miniature biofuel cell
    • T. Chen et al., A miniature biofuel cell, J. Am. Chem. Soc. 123(35); 8630-8631 (2001).
    • (2001) J. Am. Chem. Soc. , vol.123 , Issue.35 , pp. 8630-8631
    • Chen, T.1
  • 26
    • 60849084448 scopus 로고    scopus 로고
    • Performance of a glucose/O2 enzymatic biofuel cell containing a mediated Melanocarpus albomyces laccase cathode in a physiological buffer
    • P. Kavanagh et al., Performance of a glucose/O2 enzymatic biofuel cell containing a mediated Melanocarpus albomyces laccase cathode in a physiological buffer, Fuel Cells 9(1); 79-84 (2009).
    • (2009) Fuel Cells , vol.9 , Issue.1 , pp. 79-84
    • Kavanagh, P.1
  • 27
    • 52649106024 scopus 로고    scopus 로고
    • Highly efficient and versatile anodes for biofuel cells based on cellobiose dehydrogenase from Myriococcum thermophilum
    • F. Tasca et al., Highly efficient and versatile anodes for biofuel cells based on cellobiose dehydrogenase from Myriococcum thermophilum, J. Phys. Chem.C112(35); 13668-13673 (2008).
    • (2008) J. Phys. Chem. , vol.C112 , Issue.35 , pp. 13668-13673
    • Tasca, F.1
  • 28
    • 0036303472 scopus 로고    scopus 로고
    • Crystal structure of the flavoprotein domain of the extracellular flavocytochrome cellobiose dehydrogenase
    • B. M. Hallberg et al., Crystal structure of the flavoprotein domain of the extracellular flavocytochrome cellobiose dehydrogenase, J. Mol. Biol. 315(3); 421-434 (2002).
    • (2002) J. Mol. Biol. , vol.315 , Issue.3 , pp. 421-434
    • Hallberg, B.M.1
  • 29
    • 0036479218 scopus 로고    scopus 로고
    • Crystal structure of quinohemoprotein alcohol dehydrogenase from Comamonas testosteroni-structural basis for substrate oxidation and electron transfer
    • A. Oubrie et al., Crystal structure of quinohemoprotein alcohol dehydrogenase from Comamonas testosteroni-structural basis for substrate oxidation and electron transfer, J. Biol. Chem. 277(5); 3727-3732 (2002).
    • (2002) J. Biol. Chem. , vol.277 , Issue.5 , pp. 3727-3732
    • Oubrie, A.1
  • 30
    • 55049095938 scopus 로고    scopus 로고
    • Efficient electrocatalytic oxygen reduction by the "blue" copper oxidase, laccase, directly attached to chemically modified carbons
    • C. F. Blanford et al., Efficient electrocatalytic oxygen reduction by the "blue" copper oxidase, laccase, directly attached to chemically modified carbons, Faraday Discuss. 140; 319-335 (2008).
    • (2008) Faraday Discuss , vol.140 , pp. 319-335
    • Blanford, C.F.1
  • 31
    • 0030661175 scopus 로고    scopus 로고
    • Modification of carbon fiber surfaces by electrochemical reduction of aryl diazonium salts: Application to carbon epoxy composites
    • M. Delamar et al., Modification of carbon fiber surfaces by electrochemical reduction of aryl diazonium salts: Application to carbon epoxy composites, Carbon 35(6); 801-807 (1997).
    • (1997) Carbon , vol.35 , Issue.6 , pp. 801-807
    • Delamar, M.1
  • 32
    • 33751516325 scopus 로고    scopus 로고
    • Electron-conducting redox hydrogels: Design, characteristics and synthesis
    • A. Heller, Electron-conducting redox hydrogels: Design, characteristics and synthesis, Curr. Opin. Chem. Biol. 10; 664-672 (2006).
    • (2006) Curr. Opin. Chem. Biol. , vol.10 , pp. 664-672
    • Heller, A.1
  • 33
    • 34147178293 scopus 로고    scopus 로고
    • Fructose/dioxygen biofuel cell based on direct electron transfer-type bioelectrocatalysis
    • Y. Kamitaka et al., Fructose/dioxygen biofuel cell based on direct electron transfer-type bioelectrocatalysis, Phys. Chem. Chem. Phys. 9(15); 1793-1801 (2007).
    • (2007) Phys. Chem. Chem. Phys. , vol.9 , Issue.15 , pp. 1793-1801
    • Kamitaka, Y.1
  • 34
    • 46049112697 scopus 로고    scopus 로고
    • Kinetics of redox polymer-mediated enzyme electrodes
    • J. W. Gallaway and S. A. Calabrese Barton, Kinetics of redox polymer-mediated enzyme electrodes, J. Am. Chem. Soc. 130(26); 8527-8536 (2008).
    • (2008) J. Am. Chem. Soc. , vol.130 , Issue.26 , pp. 8527-8536
    • Gallaway, J.W.1    Calabrese Barton, S.A.2
  • 35
    • 34547269611 scopus 로고    scopus 로고
    • Hydrogenase-coated carbon nanotubes for efficient H2 oxidation
    • M. A. Alonso-Lomillo et al., Hydrogenase-coated carbon nanotubes for efficient H2 oxidation, Nano Lett. 7(6); 1603-1608 (2007).
    • (2007) Nano Lett , vol.7 , Issue.6 , pp. 1603-1608
    • Alonso-Lomillo, M.A.1
  • 36
    • 58649121731 scopus 로고    scopus 로고
    • Oxygen-tolerant H2 oxidation by membrane-bound [NiFe]- hydrogenases of Ralstonia species: Coping with low-level H2 in air
    • M. Ludwig et al., Oxygen-tolerant H2 oxidation by membrane-bound [NiFe]- hydrogenases of Ralstonia species: Coping with low-level H2 in air, J. Biol. Chem. 284; 465-477 (2009).
    • (2009) J. Biol. Chem , vol.284 , pp. 465-477
    • Ludwig, M.1
  • 37
    • 33845270211 scopus 로고    scopus 로고
    • Electricity from low-levelH2 in still air-anultimate test for an oxygen tolerant hydrogenase
    • K. A.Vincent et al., Electricity from low-levelH2 in still air-anultimate test for an oxygen tolerant hydrogenase, Chem. Commun. 2006 (48); 5033-5035 (2006).
    • (2006) Chem. Commun. 2006 , vol.48 , pp. 5033-5035
    • Vincent, K.A.1
  • 38
    • 33646888422 scopus 로고    scopus 로고
    • Potentially implantable miniature batteries
    • A. Heller, Potentially implantable miniature batteries, Anal. Bioanal. Chem. 385(3); 469-473 (2006).
    • (2006) Anal. Bioanal. Chem. , vol.385 , Issue.3 , pp. 469-473
    • Heller, A.1
  • 39
    • 62849098726 scopus 로고    scopus 로고
    • Biofuel cell controlled by enzyme logic systems
    • L. Amir et al., Biofuel cell controlled by enzyme logic systems, J. Am. Chem. Soc. 131(2); 826-832 (2009).
    • (2009) J. Am. Chem. Soc. , vol.131 , Issue.2 , pp. 826-832
    • Amir, L.1
  • 40
    • 58249118878 scopus 로고    scopus 로고
    • Oxygen reduction activity of a copper complex of 3,5-diamino-1,2,4-triazole supported on carbon black
    • M. S. Thorum, J.Yadav, and A. A. Gewirth, Oxygen reduction activity of a copper complex of 3,5-diamino-1,2,4-triazole supported on carbon black, Angew. Chem. Int. Ed. 48(1); 165-167 (2009).
    • (2009) Angew. Chem. Int. Ed , vol.48 , Issue.1 , pp. 165-167
    • Thorum, M.S.1    Yadav, J.2    Gewirth, A.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.