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Volumn 102, Issue 2, 2009, Pages 541-550

Dynamic electrochemical experiments on hydrogenases

Author keywords

Electrochemistry; Hydrogen; Hydrogenase; Photosynthesis

Indexed keywords

ENZYME INHIBITOR; HYDROGENASE; OXYGEN;

EID: 76149104243     PISSN: 01668595     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11120-009-9428-0     Document Type: Review
Times cited : (21)

References (24)
  • 1
    • 57649243241 scopus 로고    scopus 로고
    • Dynamic electrochemical investigations of hydrogen oxidation and production by enzymes and implications for future technology
    • doi:10.1039/b801144n
    • Armstrong FA, Belsey NA, Cracknell JA, Goldet G, Parkin A, Reisner E, Vincent KA, Wait AF (2009) Dynamic electrochemical investigations of hydrogen oxidation and production by enzymes and implications for future technology. Chem Soc Rev 38: 38-51. doi: 10. 1039/b801144n.
    • (2009) Chem Soc Rev , vol.38 , pp. 38-51
    • Armstrong, F.A.1    Belsey, N.A.2    Cracknell, J.A.3    Goldet, G.4    Parkin, A.5    Reisner, E.6    Vincent, K.A.7    Wait, A.F.8
  • 2
    • 24344440880 scopus 로고    scopus 로고
    • 2 transport in Cpl [FeFe]-hydrogenase and the role of packing defects
    • doi:10.1016/j.str.2005.05.013
    • 2 transport in Cpl [FeFe]-hydrogenase and the role of packing defects. Structure 13: 1321-1329. doi: 10. 1016/j. str. 2005. 05. 013
    • (2005) Structure , vol.13 , pp. 1321-1329
    • Cohen, J.1    Kim, K.2    King, P.3    Seibert, M.4    Schulten, K.5
  • 4
    • 35748930865 scopus 로고    scopus 로고
    • Structure/function relationships of [NiFe]- and [FeFe]-hydrogenases
    • doi:10.1021/cr050195z
    • Fontecilla-Camps JC, Volbeda A, Cavazza C, Nicolet Y (2007) Structure/function relationships of [NiFe]- and [FeFe]-hydrogenases. Chem Rev 107: 4273-4303. doi: 10. 1021/cr050195z.
    • (2007) Chem Rev , vol.107 , pp. 4273-4303
    • Fontecilla-Camps, J.C.1    Volbeda, A.2    Cavazza, C.3    Nicolet, Y.4
  • 5
    • 34250902424 scopus 로고    scopus 로고
    • Hydrogenases and hydrogen photoproduction in oxygenic photosynthetic organisms
    • doi:10.1146/annurev.arplant.58.032806.103848
    • Ghirardi ML, Posewitz MC, Maness PC, Dubini A, Yu J, Seibert M (2007) Hydrogenases and hydrogen photoproduction in oxygenic photosynthetic organisms. Annu Rev Plant Biol 58: 71-91. doi: 10. 1146/annurev. arplant. 58. 032806. 103848.
    • (2007) Annu Rev Plant Biol , vol.58 , pp. 71-91
    • Ghirardi, M.L.1    Posewitz, M.C.2    Maness, P.C.3    Dubini, A.4    Yu, J.5    Seibert, M.6
  • 6
    • 50249104385 scopus 로고    scopus 로고
    • Hydrogen production under aerobic conditions by membrane-bound hydrogenases from Ralstonia species
    • doi:10.1021/ja8027668
    • Goldet G, Wait AF, Cracknell JA, Vincent KA, Ludwig M, Lenz O, Friedrich B, Armstrong FA (2008) Hydrogen production under aerobic conditions by membrane-bound hydrogenases from Ralstonia species. J Am Chem Soc 130: 11106-11113. doi: 10. 1021/ja8027668.
    • (2008) J Am Chem Soc , vol.130 , pp. 11106-11113
    • Goldet, G.1    Wait, A.F.2    Cracknell, J.A.3    Vincent, K.A.4    Ludwig, M.5    Lenz, O.6    Friedrich, B.7    Armstrong, F.A.8
  • 8
    • 0037149937 scopus 로고    scopus 로고
    • Direct comparison of the electrocatalytic oxidation of hydrogen by an enzyme and a platinum catalyst
    • doi: 10. 1039/b201337a
    • Jones AK, Sillery E, Albracht SPJ, Armstrong FA (2002) Direct comparison of the electrocatalytic oxidation of hydrogen by an enzyme and a platinum catalyst. Chem Commun 866-867. doi: 10. 1039/b201337a.
    • (2002) Chem Commun , pp. 866-867
    • Jones, A.K.1    Sillery, E.2    Albracht, S.P.J.3    Armstrong, F.A.4
  • 9
    • 8844220418 scopus 로고    scopus 로고
    • Electrochemical potential-step investigations of the aerobic interconversions of [NiFe]-hydrogenase from Allochromatium vinosum: New insights into the puzzling difference between unready and ready oxidized inactive states
    • doi:10.1021/ja047939v
    • Lamle SE, Albracht SP, Armstrong FA (2004) Electrochemical potential-step investigations of the aerobic interconversions of [NiFe]-hydrogenase from Allochromatium vinosum: new insights into the puzzling difference between unready and ready oxidized inactive states. J Am Chem Soc 126: 14899-14909. doi: 10. 1021/ja047939v.
    • (2004) J Am Chem Soc , vol.126 , pp. 14899-14909
    • Lamle, S.E.1    Albracht, S.P.2    Armstrong, F.A.3
  • 10
    • 18644373177 scopus 로고    scopus 로고
    • The mechanism of activation of a [NiFe]-hydrogenase by electrons, hydrogen and carbon monoxide
    • doi:10.1021/ja0424934
    • Lamle SE, Albracht SP, Armstrong FA (2005) The mechanism of activation of a [NiFe]-hydrogenase by electrons, hydrogen and carbon monoxide. J Am Chem Soc 127: 6595-6604. doi: 10. 1021/ja0424934.
    • (2005) J Am Chem Soc , vol.127 , pp. 6595-6604
    • Lamle, S.E.1    Albracht, S.P.2    Armstrong, F.A.3
  • 11
    • 49049115593 scopus 로고    scopus 로고
    • Direct electrochemistry of redox enzymes as a tool for mechanistic studies
    • doi:10.1021/cr0680742
    • Léger C, Bertrand P (2008) Direct electrochemistry of redox enzymes as a tool for mechanistic studies. Chem Rev 108: 2379-2438. doi: 10. 1021/cr0680742.
    • (2008) Chem Rev , vol.108 , pp. 2379-2438
    • Léger, C.1    Bertrand, P.2
  • 12
    • 4644245238 scopus 로고    scopus 로고
    • Inhibition and aerobic inactivation kinetics of Desulfovibrio fructosovorans NiFe hydrogenase studied by protein film voltammetry
    • doi:10.1021/ja046548d
    • Léger C, Dementin S, Bertrand P, Rousset M, Guigliarelli B (2004) Inhibition and aerobic inactivation kinetics of Desulfovibrio fructosovorans NiFe hydrogenase studied by protein film voltammetry. J Am Chem Soc 126: 12162-12172. doi: 10. 1021/ja046548d.
    • (2004) J Am Chem Soc , vol.126 , pp. 12162-12172
    • Léger, C.1    Dementin, S.2    Bertrand, P.3    Rousset, M.4    Guigliarelli, B.5
  • 13
    • 58649103743 scopus 로고    scopus 로고
    • 2: Design principles of photosystem II and hydrogenases
    • doi:10.1039/b808792j
    • 2: design principles of photosystem II and hydrogenases. Energ Environ Sci 1: 15-31. doi: 10. 1039/b808792j.
    • (2008) Energ Environ Sci , vol.1 , pp. 15-31
    • Lubitz, W.1    Reijerse, E.J.2    Messinger, J.3
  • 15
    • 0033556301 scopus 로고    scopus 로고
    • Desulfovibrio desulfuricans iron hydrogenase: The structure shows unusual coordination to an active site Fe binuclear center
    • doi:10.1016/S0969-2126(99)80005-7
    • Nicolet Y, Piras C, Legrand P, Hatchikian CE, Fontecilla-Camps JC (1999) Desulfovibrio desulfuricans iron hydrogenase: the structure shows unusual coordination to an active site Fe binuclear center. Structure 7: 13-23. doi: 10. 1016/S0969-2126(99)80005-7.
    • (1999) Structure , vol.7 , pp. 13-23
    • Nicolet, Y.1    Piras, C.2    Legrand, P.3    Hatchikian, C.E.4    Fontecilla-Camps, J.C.5
  • 16
    • 27644552110 scopus 로고    scopus 로고
    • Activation process of [NiFe] hydrogenase elucidated by high-resolution X-ray analyses: Conversion of the ready to the unready state
    • doi:10.1016/j.str.2005.07.018
    • Ogata H, Hirota S, Nakahara A, Komori H, Shibata N, Kato T, Kano K, Higuchi Y (2005) Activation process of [NiFe] hydrogenase elucidated by high-resolution X-ray analyses: conversion of the ready to the unready state. Structure 13: 1635-1642. doi: 10. 1016/j. str. 2005. 07. 018.
    • (2005) Structure , vol.13 , pp. 1635-1642
    • Ogata, H.1    Hirota, S.2    Nakahara, A.3    Komori, H.4    Shibata, N.5    Kato, T.6    Kano, K.7    Higuchi, Y.8
  • 17
    • 33845932878 scopus 로고    scopus 로고
    • Electrochemical investigations of the interconversions between catalytic and inhibited states of the [FeFe]-hydrogenase from Desulfovibrio desulfuricans
    • doi:10.1021/ja064425i
    • Parkin A, Cavazza C, Fontecilla-Camps JC, Armstrong FA (2006) Electrochemical investigations of the interconversions between catalytic and inhibited states of the [FeFe]-hydrogenase from Desulfovibrio desulfuricans. J Am Chem Soc 128: 16808-16815. doi: 10. 1021/ja064425i.
    • (2006) J Am Chem Soc , vol.128 , pp. 16808-16815
    • Parkin, A.1    Cavazza, C.2    Fontecilla-Camps, J.C.3    Armstrong, F.A.4
  • 18
    • 53549119985 scopus 로고    scopus 로고
    • The difference a Se makes? Oxygen-tolerant hydrogen production by the [NiFeSe]-hydrogenase from Desulfomicrobium baculatum
    • doi:10.1021/ja803657d
    • Parkin A, Goldet G, Cavazza C, Fontecilla-Camps JC, Armstrong FA (2008) The difference a Se makes? Oxygen-tolerant hydrogen production by the [NiFeSe]-hydrogenase from Desulfomicrobium baculatum. J Am Chem Soc 130: 13410-13416. doi: 10. 1021/ja803657d.
    • (2008) J Am Chem Soc , vol.130 , pp. 13410-13416
    • Parkin, A.1    Goldet, G.2    Cavazza, C.3    Fontecilla-Camps, J.C.4    Armstrong, F.A.5
  • 20
    • 35748974830 scopus 로고    scopus 로고
    • Occurrence, classification, and biological function of hydrogenases: An overview
    • doi:10.1021/cr050196r
    • Vignais PM, Billoud B (2007) Occurrence, classification, and biological function of hydrogenases: an overview. Chem Rev 107: 4206-4272. doi: 10. 1021/cr050196r.
    • (2007) Chem Rev , vol.107 , pp. 4206-4272
    • Vignais, P.M.1    Billoud, B.2
  • 23
    • 35748933836 scopus 로고    scopus 로고
    • Investigating and exploiting the electrocatalytic properties of hydrogenases
    • doi:10.1021/cr050191u
    • Vincent KA, Parkin A, Armstrong FA (2007) Investigating and exploiting the electrocatalytic properties of hydrogenases. Chem Rev 107: 4366-4413. doi: 10. 1021/cr050191u.
    • (2007) Chem Rev , vol.107 , pp. 4366-4413
    • Vincent, K.A.1    Parkin, A.2    Armstrong, F.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.