메뉴 건너뛰기




Volumn 16, Issue 1-2, 2012, Pages 26-34

The hows and whys of aerobic H 2 metabolism

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; BACTERIAL PROTEIN; FERROUS SULFIDE; HYDROGEN; HYDROGENASE; MOLYBDENUM; NICKEL; NICKEL IRON HYDROGENASE; NITROGENASE; OXYGEN; PROTEIN HOXO; PROTEIN HOXQ; PROTEIN HUPG; PROTEIN HUPH; PROTEIN HYAE; PROTEIN HYAF; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; RUBREDOXIN; THIOREDOXIN; UNCLASSIFIED DRUG;

EID: 84859638884     PISSN: 13675931     EISSN: 18790402     Source Type: Journal    
DOI: 10.1016/j.cbpa.2012.01.012     Document Type: Review
Times cited : (56)

References (49)
  • 1
    • 0037149937 scopus 로고    scopus 로고
    • Direct comparison of the electrocatalytic oxidation of hydrogen by an enzyme and a platinum catalyst
    • Jones A.K., Sillery E., Albracht S.P.J., Armstrong F.A. Direct comparison of the electrocatalytic oxidation of hydrogen by an enzyme and a platinum catalyst. Chem Commun 2002, 866-867.
    • (2002) Chem Commun , pp. 866-867
    • Jones, A.K.1    Sillery, E.2    Albracht, S.P.J.3    Armstrong, F.A.4
  • 2
    • 35748974830 scopus 로고    scopus 로고
    • Occurrence, classification, and biological function of hydrogenases: an overview
    • Vignais P.M., Billoud B. Occurrence, classification, and biological function of hydrogenases: an overview. Chem Rev 2007, 107:4206-4272.
    • (2007) Chem Rev , vol.107 , pp. 4206-4272
    • Vignais, P.M.1    Billoud, B.2
  • 4
    • 35848964033 scopus 로고    scopus 로고
    • 2 production and storage
    • 2 production and storage. Chem Rev 2007, 107:4152-4205.
    • (2007) Chem Rev , vol.107 , pp. 4152-4205
    • Kubas, G.J.1
  • 5
    • 80555150640 scopus 로고    scopus 로고
    • Wireless solar water splitting using silicon-based semiconductors and earth-abundant catalysts
    • Reece S.Y., Hamel J.A., Sung K., Jarvi T.D., Esswein A.J., Pijpers J.J.H., Nocera D.G. Wireless solar water splitting using silicon-based semiconductors and earth-abundant catalysts. Science 2011, 334:645-648.
    • (2011) Science , vol.334 , pp. 645-648
    • Reece, S.Y.1    Hamel, J.A.2    Sung, K.3    Jarvi, T.D.4    Esswein, A.J.5    Pijpers, J.J.H.6    Nocera, D.G.7
  • 7
    • 70350234815 scopus 로고    scopus 로고
    • Electrochemical kinetic investigations of the reactions of [FeFe]-hydrogenases with carbon monoxide and oxygen: comparing the importance of gas tunnels and active-site electronic/redox effects
    • Goldet G., Brandmayr C., Stripp S.T., Happe T., Cavazza C., Fontecilla-Camps J.C., Armstrong F.A. Electrochemical kinetic investigations of the reactions of [FeFe]-hydrogenases with carbon monoxide and oxygen: comparing the importance of gas tunnels and active-site electronic/redox effects. J Am Chem Soc 2009, 131:14979-14989.
    • (2009) J Am Chem Soc , vol.131 , pp. 14979-14989
    • Goldet, G.1    Brandmayr, C.2    Stripp, S.T.3    Happe, T.4    Cavazza, C.5    Fontecilla-Camps, J.C.6    Armstrong, F.A.7
  • 10
    • 77955336661 scopus 로고    scopus 로고
    • Characteristics of enzyme-based hydrogen fuel cells using an oxygen-tolerant hydrogenase as the anodic catalyst
    • Wait A.F., Parkin A., Morley G.M., dos Santos L., Armstrong F.A. Characteristics of enzyme-based hydrogen fuel cells using an oxygen-tolerant hydrogenase as the anodic catalyst. J Phys Chem C 2010, 114:12003-12009.
    • (2010) J Phys Chem C , vol.114 , pp. 12003-12009
    • Wait, A.F.1    Parkin, A.2    Morley, G.M.3    dos Santos, L.4    Armstrong, F.A.5
  • 12
    • 35748930865 scopus 로고    scopus 로고
    • Structure/function relationships of [NiFe]- and [FeFe]-hydrogenases
    • Fontecilla-Camps J.C., Volbeda A., Cavazza C., Nicolet Y. Structure/function relationships of [NiFe]- and [FeFe]-hydrogenases. Chem Rev 2007, 107:4273-4303.
    • (2007) Chem Rev , vol.107 , pp. 4273-4303
    • Fontecilla-Camps, J.C.1    Volbeda, A.2    Cavazza, C.3    Nicolet, Y.4
  • 13
    • 80855156729 scopus 로고    scopus 로고
    • Structural basis for a [4Fe-3S] cluster in the oxygen-tolerant membrane-bound [NiFe]-hydrogenase
    • Shomura Y., Yoon K.-S., Nishihara H., Higuchi Y. Structural basis for a [4Fe-3S] cluster in the oxygen-tolerant membrane-bound [NiFe]-hydrogenase. Nature 2011, 479:253-256.
    • (2011) Nature , vol.479 , pp. 253-256
    • Shomura, Y.1    Yoon, K.-S.2    Nishihara, H.3    Higuchi, Y.4
  • 15
    • 8844220418 scopus 로고    scopus 로고
    • Electrochemical potential-step investigations of the aerobic interconversions of [NiFe]-hydrogenase from Allochromatium vinosum: insights into the puzzling difference between unready and ready oxidized inactive states
    • Lamle S.E., Albracht S.P.J., Armstrong F.A. Electrochemical potential-step investigations of the aerobic interconversions of [NiFe]-hydrogenase from Allochromatium vinosum: insights into the puzzling difference between unready and ready oxidized inactive states. J Am Chem Soc 2004, 126:14899-14909.
    • (2004) J Am Chem Soc , vol.126 , pp. 14899-14909
    • Lamle, S.E.1    Albracht, S.P.J.2    Armstrong, F.A.3
  • 17
    • 70349289233 scopus 로고    scopus 로고
    • [NiFe] hydrogenases: structural and spectroscopic studies of the reaction mechanism
    • Ogata H., Lubitz W., Higuchi Y. [NiFe] hydrogenases: structural and spectroscopic studies of the reaction mechanism. Dalton Trans 2009, 7577-7587.
    • (2009) Dalton Trans , pp. 7577-7587
    • Ogata, H.1    Lubitz, W.2    Higuchi, Y.3
  • 19
    • 77956759468 scopus 로고    scopus 로고
    • The crystal structure of the [NiFe] hydrogenase from the photosynthetic bacterium Allochromatium vinosum: characterization of the oxidized enzyme (Ni-A state)
    • Ogata H., Kellers P., Lubitz W. The crystal structure of the [NiFe] hydrogenase from the photosynthetic bacterium Allochromatium vinosum: characterization of the oxidized enzyme (Ni-A state). J Mol Biol 2010, 402:428-444.
    • (2010) J Mol Biol , vol.402 , pp. 428-444
    • Ogata, H.1    Kellers, P.2    Lubitz, W.3
  • 20
    • 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
    • Ogata H., Hirota S., Nakahara A., Komori H., Shibata N., Kato T., Kano K., Higuchi Y. Activation process of [NiFe] hydrogenase elucidated by high-resolution X-ray analyses: conversion of the ready to the unready state. Structure 2005, 13:1635-1642.
    • (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
  • 21
    • 4644245238 scopus 로고    scopus 로고
    • Inhibition and aerobic inactivation kinetics of Desulfovibrio fructosovorans NiFe hydrogenase studied by protein film voltammetry
    • Léger C., Dementin S., Bertrand P., Rousset M., Guigliarelli B. Inhibition and aerobic inactivation kinetics of Desulfovibrio fructosovorans NiFe hydrogenase studied by protein film voltammetry. J Am Chem Soc 2004, 126:12162-12172.
    • (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
  • 22
    • 0024962473 scopus 로고
    • Redox intermediates of Desulfovibrio gigas [NiFe] hydrogenase generated under hydrogen. Mössbauer and EPR characterization of the metal centers
    • Teixeira M., Moura I., Xavier A.V., Moura J.J., LeGall J., DerVartanian D.V., Peck H.D., Huynh B.H. Redox intermediates of Desulfovibrio gigas [NiFe] hydrogenase generated under hydrogen. Mössbauer and EPR characterization of the metal centers. J Biol Chem 1989, 264:16435-16450.
    • (1989) J Biol Chem , vol.264 , pp. 16435-16450
    • Teixeira, M.1    Moura, I.2    Xavier, A.V.3    Moura, J.J.4    LeGall, J.5    DerVartanian, D.V.6    Peck, H.D.7    Huynh, B.H.8
  • 23
    • 0023759565 scopus 로고
    • The potential diagram for oxygen at pH 7
    • Wood P.M. The potential diagram for oxygen at pH 7. Biochem J 1988, 253:287-289.
    • (1988) Biochem J , vol.253 , pp. 287-289
    • Wood, P.M.1
  • 27
    • 77952566611 scopus 로고    scopus 로고
    • Membrane-bound hydrogenase I from the hyperthermophilic bacterium Aquifex aeolicus: enzyme activation, redox intermediates and oxygen tolerance
    • Pandelia M.-E., Fourmond V., Tron-Infossi P., Lojou E., Bertrand P., Leóger C., Giudici-Orticoni M.-T.r.s., Lubitz W. Membrane-bound hydrogenase I from the hyperthermophilic bacterium Aquifex aeolicus: enzyme activation, redox intermediates and oxygen tolerance. J Am Chem Soc 2010, 132:6991-7004.
    • (2010) J Am Chem Soc , vol.132 , pp. 6991-7004
    • Pandelia, M.-E.1    Fourmond, V.2    Tron-Infossi, P.3    Lojou, E.4    Bertrand, P.5    Leóger, C.6    Giudici-Orticoni, M.-T.7    Lubitz, W.8
  • 28
    • 79955027963 scopus 로고    scopus 로고
    • Characterization of a unique [FeS] cluster in the electron transfer chain of the oxygen tolerant [NiFe] hydrogenase from Aquifex aeolicus
    • Pandelia M.-E., Nitschke W., Infossi P., Giudici-Orticoni M.-T., Bill E., Lubitz W. Characterization of a unique [FeS] cluster in the electron transfer chain of the oxygen tolerant [NiFe] hydrogenase from Aquifex aeolicus. Proc Natl Acad Sci USA 2011, 108:6097-6102.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 6097-6102
    • Pandelia, M.-E.1    Nitschke, W.2    Infossi, P.3    Giudici-Orticoni, M.-T.4    Bill, E.5    Lubitz, W.6
  • 31
    • 80054971344 scopus 로고    scopus 로고
    • Oxygen-tolerant [NiFe]-hydrogenases: the individual and collective importance of supernumerary cysteines at the proximal Fe-S cluster
    • Lukey M.J., Roessler M.M., Parkin A., Evans R.M., Davies R.A., Lenz O., Friedrich B., Sargent F., Armstrong F.A. Oxygen-tolerant [NiFe]-hydrogenases: the individual and collective importance of supernumerary cysteines at the proximal Fe-S cluster. J Am Chem Soc 2011, 133:16881-16892.
    • (2011) J Am Chem Soc , vol.133 , pp. 16881-16892
    • Lukey, M.J.1    Roessler, M.M.2    Parkin, A.3    Evans, R.M.4    Davies, R.A.5    Lenz, O.6    Friedrich, B.7    Sargent, F.8    Armstrong, F.A.9
  • 34
    • 34250874525 scopus 로고    scopus 로고
    • Crystal structures of [NiFe] hydrogenase maturation proteins HypC, HypD, and HypE: insights into cyanation reaction by thiol redox signaling
    • Watanabe S., Matsumi R., Arai T., Atomi H., Imanaka T., Miki K. Crystal structures of [NiFe] hydrogenase maturation proteins HypC, HypD, and HypE: insights into cyanation reaction by thiol redox signaling. Mol Cell 2007, 27:29-40.
    • (2007) Mol Cell , vol.27 , pp. 29-40
    • Watanabe, S.1    Matsumi, R.2    Arai, T.3    Atomi, H.4    Imanaka, T.5    Miki, K.6
  • 36
    • 0035191007 scopus 로고    scopus 로고
    • Requirement of nickel metabolism proteins HypA and HypB for full activity of both hydrogenase and urease in Helicobacter pylori
    • Olson J.W., Mehta N.S., Maier R.J. Requirement of nickel metabolism proteins HypA and HypB for full activity of both hydrogenase and urease in Helicobacter pylori. Mol Microbiol 2001, 39:176-182.
    • (2001) Mol Microbiol , vol.39 , pp. 176-182
    • Olson, J.W.1    Mehta, N.S.2    Maier, R.J.3
  • 41
    • 79956101455 scopus 로고    scopus 로고
    • The maturation factors HoxR and HoxT contribute to oxygen tolerance of membrane-bound [NiFe]-hydrogenase in Ralstonia eutropha H16
    • Fritsch J., Lenz O., Friedrich B. The maturation factors HoxR and HoxT contribute to oxygen tolerance of membrane-bound [NiFe]-hydrogenase in Ralstonia eutropha H16. J Bacteriol 2011, 193:2487-2497.
    • (2011) J Bacteriol , vol.193 , pp. 2487-2497
    • Fritsch, J.1    Lenz, O.2    Friedrich, B.3
  • 42
    • 34748882510 scopus 로고    scopus 로고
    • Chaperones specific for the membrane-bound [NiFe]-hydrogenase interact with the Tat signal peptide of the small subunit precursor in Ralstonia eutropha H16
    • Schubert T., Lenz O., Krause E., Volkmer R., Friedrich B. Chaperones specific for the membrane-bound [NiFe]-hydrogenase interact with the Tat signal peptide of the small subunit precursor in Ralstonia eutropha H16. Mol Microbiol 2007, 66:453-467.
    • (2007) Mol Microbiol , vol.66 , pp. 453-467
    • Schubert, T.1    Lenz, O.2    Krause, E.3    Volkmer, R.4    Friedrich, B.5
  • 43
    • 26444605816 scopus 로고    scopus 로고
    • Gene products of the hupGHIJ operon are involved in maturation of the iron-sulfur subunit of the [NiFe] hydrogenase from Rhizobium leguminosarum bv. viciae
    • Manyani H., Rey L., Palacios J.M., Imperial J., Ruiz-Argueso T. Gene products of the hupGHIJ operon are involved in maturation of the iron-sulfur subunit of the [NiFe] hydrogenase from Rhizobium leguminosarum bv. viciae. J Bacteriol 2005, 187:7018-7026.
    • (2005) J Bacteriol , vol.187 , pp. 7018-7026
    • Manyani, H.1    Rey, L.2    Palacios, J.M.3    Imperial, J.4    Ruiz-Argueso, T.5
  • 44
    • 0036836358 scopus 로고    scopus 로고
    • How bacteria get energy from hydrogen: a genetic analysis of periplasmic hydrogen oxidation in Escherichia coli
    • Dubini A., Pye R.L., Jack R.L., Palmer T., Sargent F. How bacteria get energy from hydrogen: a genetic analysis of periplasmic hydrogen oxidation in Escherichia coli. Int J Hydrogen Energy 2002, 27:1413-1420.
    • (2002) Int J Hydrogen Energy , vol.27 , pp. 1413-1420
    • Dubini, A.1    Pye, R.L.2    Jack, R.L.3    Palmer, T.4    Sargent, F.5
  • 45
    • 0042564757 scopus 로고    scopus 로고
    • Assembly of Tat-dependent [NiFe] hydrogenases: identification of precursor-binding accessory proteins
    • Dubini A., Sargent F. Assembly of Tat-dependent [NiFe] hydrogenases: identification of precursor-binding accessory proteins. FEBS Lett 2003, 549:141-146.
    • (2003) FEBS Lett , vol.549 , pp. 141-146
    • Dubini, A.1    Sargent, F.2
  • 46
    • 57249113692 scopus 로고    scopus 로고
    • Protein chaperones Q8ZP25_SALTY from Salmonella typhimurium and HYAE_ECOLI from Escherichia coli exhibit thioredoxin-like structures despite lack of canonical thioredoxin active site sequence motif
    • Parish D., Benach J., Liu G., Singarapu K., Xiao R., Acton T., Su M., Bansal S., Prestegard J., Hunt J., et al. Protein chaperones Q8ZP25_SALTY from Salmonella typhimurium and HYAE_ECOLI from Escherichia coli exhibit thioredoxin-like structures despite lack of canonical thioredoxin active site sequence motif. J Struct Funct Genomics 2008, 9:41-49.
    • (2008) J Struct Funct Genomics , vol.9 , pp. 41-49
    • Parish, D.1    Benach, J.2    Liu, G.3    Singarapu, K.4    Xiao, R.5    Acton, T.6    Su, M.7    Bansal, S.8    Prestegard, J.9    Hunt, J.10
  • 47
    • 0025914936 scopus 로고
    • Mutational analysis and characterization of the Escherichia coli hya operon, which encodes [NiFe] hydrogenase 1
    • Menon N.K., Robbins J., Wendt J.C., Shanmugam K.T., Przybyla A.E. Mutational analysis and characterization of the Escherichia coli hya operon, which encodes [NiFe] hydrogenase 1. J Bacteriol 1991, 173:4851-4861.
    • (1991) J Bacteriol , vol.173 , pp. 4851-4861
    • Menon, N.K.1    Robbins, J.2    Wendt, J.C.3    Shanmugam, K.T.4    Przybyla, A.E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.