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Volumn 1853, Issue 6, 2015, Pages 1350-1369

[FeFe]- and [NiFe]-hydrogenase diversity, mechanism, and maturation

Author keywords

Bifurcation; Carbon monoxide; Cyanide; Hydrogen oxidation; Iron sulfur; Proton reduction

Indexed keywords

ARCHAEAL PROTEIN; BACTERIAL PROTEIN; HYDROGEN; HYDROGENASE; IRON HYDROGENASE; IRON SULFUR PROTEIN; NICKEL-IRON HYDROGENASE;

EID: 84929366162     PISSN: 01674889     EISSN: 18792596     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2014.11.021     Document Type: Review
Times cited : (383)

References (267)
  • 1
    • 0029066353 scopus 로고
    • Infrared-detectable group senses changes in charge density on the nickel center in hydrogenase from chromatium vinosum
    • Bagley K.A., Duin E.C., Roseboom W., Albracht S.P.J., Woodruff W.H. Infrared-detectable group senses changes in charge density on the nickel center in hydrogenase from chromatium vinosum. Biochemistry 1995, 34:5527-5535.
    • (1995) Biochemistry , vol.34 , pp. 5527-5535
    • Bagley, K.A.1    Duin, E.C.2    Roseboom, W.3    Albracht, S.P.J.4    Woodruff, W.H.5
  • 2
    • 0028048410 scopus 로고
    • Infrared studies on the interaction of carbon monoxide with divalent nickel in hydrogenase from chromatium vinosum
    • Bagley K.A., Van Garderen C.J., Chen M., Woodruff W.H., Duin E.C., Albracht S.P.J. Infrared studies on the interaction of carbon monoxide with divalent nickel in hydrogenase from chromatium vinosum. Biochemistry 1994, 33:9229-9236.
    • (1994) Biochemistry , vol.33 , pp. 9229-9236
    • Bagley, K.A.1    Van Garderen, C.J.2    Chen, M.3    Woodruff, W.H.4    Duin, E.C.5    Albracht, S.P.J.6
  • 3
    • 0036523377 scopus 로고    scopus 로고
    • Hydrogenases: hydrogen-activating enzymes
    • Frey M. Hydrogenases: hydrogen-activating enzymes. ChemBioChem 2002, 3:153-160.
    • (2002) ChemBioChem , vol.3 , pp. 153-160
    • Frey, M.1
  • 8
    • 0033556301 scopus 로고    scopus 로고
    • Desulfovibrio desulfuricans iron hydrogenase: the structure shows unusual coordination to an active site Fe binuclear center
    • Nicolet Y., Piras C., Legrand P., Hatchikian C.E., Fontecilla-Camps J.C. Desulfovibrio desulfuricans iron hydrogenase: the structure shows unusual coordination to an active site Fe binuclear center. Struct. Fold. Des. 1999, 7:13-23.
    • (1999) Struct. Fold. Des. , vol.7 , pp. 13-23
    • Nicolet, Y.1    Piras, C.2    Legrand, P.3    Hatchikian, C.E.4    Fontecilla-Camps, J.C.5
  • 9
    • 0032483966 scopus 로고    scopus 로고
    • X-ray crystal structure of the Fe-only hydrogenase (CpI) from Clostridium pasteurianum to 1.8 angstrom resolution
    • Peters J.W., Lanzilotta W.N., Lemon B.J., Seefeldt L.C. X-ray crystal structure of the Fe-only hydrogenase (CpI) from Clostridium pasteurianum to 1.8 angstrom resolution. Science 1998, 282:1853-1858.
    • (1998) Science , vol.282 , pp. 1853-1858
    • Peters, J.W.1    Lanzilotta, W.N.2    Lemon, B.J.3    Seefeldt, L.C.4
  • 10
    • 0032403791 scopus 로고    scopus 로고
    • A low-spin iron with CN and CO as intrinsic ligands forms the core of the active site in [Fe]-hydrogenases
    • Pierik A.J., Hulstein M., Hagen W.R., Albracht S.P.J. A low-spin iron with CN and CO as intrinsic ligands forms the core of the active site in [Fe]-hydrogenases. Eur. J. Biochem. 1998, 258:572-578.
    • (1998) Eur. J. Biochem. , vol.258 , pp. 572-578
    • Pierik, A.J.1    Hulstein, M.2    Hagen, W.R.3    Albracht, S.P.J.4
  • 12
    • 35748933836 scopus 로고    scopus 로고
    • Investigating and exploiting the electrocatalytic properties of hydrogenases
    • Vincent K.A., Parkin A., Armstrong F.A. Investigating and exploiting the electrocatalytic properties of hydrogenases. Chem. Rev. 2007, 107:4366-4413.
    • (2007) Chem. Rev. , vol.107 , pp. 4366-4413
    • Vincent, K.A.1    Parkin, A.2    Armstrong, F.A.3
  • 14
    • 84884318673 scopus 로고    scopus 로고
    • Molecular basis of [FeFe]-hydrogenase function: An insight into the complex interplay between protein and catalytic cofactor
    • Winkler M., Esselborn J., Happe T. Molecular basis of [FeFe]-hydrogenase function: An insight into the complex interplay between protein and catalytic cofactor. Biochim. Biophys. Acta Bioenerg. 2013, 1827:974-985.
    • (2013) Biochim. Biophys. Acta Bioenerg. , vol.1827 , pp. 974-985
    • Winkler, M.1    Esselborn, J.2    Happe, T.3
  • 16
    • 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
  • 19
    • 0033551444 scopus 로고    scopus 로고
    • Catalytic electron transport in chromatium vinosum [NiFe]-hydrogenase: application of voltammetry in detecting redox-active centers and establishing that hydrogen oxidation is very fast even at potentials close to the reversible H+/H2 value
    • Pershad H.R., Duff J.L.C., Heering H.A., Duin E.C., Albracht S.P.J., Armstrong F.A. Catalytic electron transport in chromatium vinosum [NiFe]-hydrogenase: application of voltammetry in detecting redox-active centers and establishing that hydrogen oxidation is very fast even at potentials close to the reversible H+/H2 value. Biochemistry 1999, 38:8992-8999.
    • (1999) Biochemistry , vol.38 , pp. 8992-8999
    • Pershad, H.R.1    Duff, J.L.C.2    Heering, H.A.3    Duin, E.C.4    Albracht, S.P.J.5    Armstrong, F.A.6
  • 20
    • 80055086260 scopus 로고    scopus 로고
    • Mechanism of proton transfer in [FeFe]-hydrogenase from Clostridium pasteurianum
    • Cornish A.J., Gärtner K., Yang H., Peters J.W., Hegg E.L. Mechanism of proton transfer in [FeFe]-hydrogenase from Clostridium pasteurianum. J. Biol. Chem. 2011, 286:38341-38347.
    • (2011) J. Biol. Chem. , vol.286 , pp. 38341-38347
    • Cornish, A.J.1    Gärtner, K.2    Yang, H.3    Peters, J.W.4    Hegg, E.L.5
  • 21
    • 84906262240 scopus 로고    scopus 로고
    • Beyond the active site: the impact of the outer coordination sphere on electrocatalysts for hydrogen production and oxidation
    • Ginovska-Pangovska B., Dutta A., Reback M.L., Linehan J.C., Shaw W.J. Beyond the active site: the impact of the outer coordination sphere on electrocatalysts for hydrogen production and oxidation. Acc. Chem. Res. 2014, 46:2621-2630.
    • (2014) Acc. Chem. Res. , vol.46 , pp. 2621-2630
    • Ginovska-Pangovska, B.1    Dutta, A.2    Reback, M.L.3    Linehan, J.C.4    Shaw, W.J.5
  • 24
    • 77649271875 scopus 로고    scopus 로고
    • The three-dimensional structure of [NiFeSe] hydrogenase from Desulfovibrio vulgaris hildenborough: a hydrogenase without a bridging ligand in the active site in its oxidised, "as-isolated" state
    • Marques M.C., Coelho R., De Lacey A.L., Pereira I.A.C., Matias P.M. The three-dimensional structure of [NiFeSe] hydrogenase from Desulfovibrio vulgaris hildenborough: a hydrogenase without a bridging ligand in the active site in its oxidised, "as-isolated" state. J. Mol. Biol. 2010, 396:893-907.
    • (2010) J. Mol. Biol. , vol.396 , pp. 893-907
    • Marques, M.C.1    Coelho, R.2    De Lacey, A.L.3    Pereira, I.A.C.4    Matias, P.M.5
  • 25
    • 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
  • 29
    • 77953200590 scopus 로고    scopus 로고
    • The surprising diversity of clostridial hydrogenases: a comparative genomic perspective
    • Calusinska M., Happe T., Joris B., Wilmotte A. The surprising diversity of clostridial hydrogenases: a comparative genomic perspective. Microbiology 2010, 156:1575-1588.
    • (2010) Microbiology , vol.156 , pp. 1575-1588
    • Calusinska, M.1    Happe, T.2    Joris, B.3    Wilmotte, A.4
  • 30
    • 34247577593 scopus 로고    scopus 로고
    • [FeFe] hydrogenases and their evolution: a genomic perspective
    • Meyer J. [FeFe] hydrogenases and their evolution: a genomic perspective. Cell. Mol. Life Sci. 2007, 64:1063-1084.
    • (2007) Cell. Mol. Life Sci. , vol.64 , pp. 1063-1084
    • Meyer, J.1
  • 31
    • 2942565619 scopus 로고    scopus 로고
    • The hydrogenase-like Nar1p is essential for maturation of cytosolic and nuclear iron-sulphur proteins
    • Balk J., Pierik A.J., Netz D.J.A., Mühlenhoff U., Lill R. The hydrogenase-like Nar1p is essential for maturation of cytosolic and nuclear iron-sulphur proteins. EMBO J. 2004, 23:2105-2115.
    • (2004) EMBO J. , vol.23 , pp. 2105-2115
    • Balk, J.1    Pierik, A.J.2    Netz, D.J.A.3    Mühlenhoff, U.4    Lill, R.5
  • 33
    • 84924800614 scopus 로고    scopus 로고
    • Hydrogen metabolism and the evolution of biological respiration
    • Boyd E.S., Schut G.J., Adams M.W.W., Peters J.W. Hydrogen metabolism and the evolution of biological respiration. Microbe 2014, 9:361-367.
    • (2014) Microbe , vol.9 , pp. 361-367
    • Boyd, E.S.1    Schut, G.J.2    Adams, M.W.W.3    Peters, J.W.4
  • 34
    • 2142697116 scopus 로고    scopus 로고
    • Energy-converting [NiFe] hydrogenases from archaea and extremophiles: ancestors of complex I
    • Hedderich R. Energy-converting [NiFe] hydrogenases from archaea and extremophiles: ancestors of complex I. J. Bioenerg. Biomembr. 2004, 36:65-75.
    • (2004) J. Bioenerg. Biomembr. , vol.36 , pp. 65-75
    • Hedderich, R.1
  • 35
    • 84873290195 scopus 로고    scopus 로고
    • The modular respiratory complexes involved in hydrogen and sulfur metabolism by heterotrophic hyperthermophilic archaea and their evolutionary implications
    • Schut G.J., Boyd E.S., Peters J.W., Adams M.W. The modular respiratory complexes involved in hydrogen and sulfur metabolism by heterotrophic hyperthermophilic archaea and their evolutionary implications. FEMS Microbiol. Rev. 2013, 37:182-203.
    • (2013) FEMS Microbiol. Rev. , vol.37 , pp. 182-203
    • Schut, G.J.1    Boyd, E.S.2    Peters, J.W.3    Adams, M.W.4
  • 39
    • 84896768069 scopus 로고    scopus 로고
    • The importance of iron in the biosynthesis and assembly of [NiFe]-hydrogenases
    • Pinske C., Sawers R.G. The importance of iron in the biosynthesis and assembly of [NiFe]-hydrogenases. BioMolecular concepts 2014, 55.
    • (2014) BioMolecular concepts , pp. 55
    • Pinske, C.1    Sawers, R.G.2
  • 40
    • 2942586665 scopus 로고    scopus 로고
    • Discovery of two novel radical S-adenosylmethionine proteins required for the assembly of an active [Fe] hydrogenase
    • Posewitz M.C., King P.W., Smolinski S.L., Zhang L., Seibert M., Ghirardi M.L. Discovery of two novel radical S-adenosylmethionine proteins required for the assembly of an active [Fe] hydrogenase. J. Biol. Chem. 2004, 279:25711-25720.
    • (2004) J. Biol. Chem. , vol.279 , pp. 25711-25720
    • Posewitz, M.C.1    King, P.W.2    Smolinski, S.L.3    Zhang, L.4    Seibert, M.5    Ghirardi, M.L.6
  • 44
    • 48249113394 scopus 로고    scopus 로고
    • New frontiers in hydrogenase structure and biosynthesis
    • Posewitz M.C., Mulder D.W., Peters J.W. New frontiers in hydrogenase structure and biosynthesis. Curr. Chem. Biol. 2008, 2:178-199.
    • (2008) Curr. Chem. Biol. , vol.2 , pp. 178-199
    • Posewitz, M.C.1    Mulder, D.W.2    Peters, J.W.3
  • 45
    • 84878116752 scopus 로고    scopus 로고
    • Function of the chloroplast hydrogenase in the microalga Chlamydomonas: the role of hydrogenase and state transitions during photosynthetic activation in anaerobiosis
    • Ghysels B., Godaux D., Matagne R.F., Cardol P., Franck F. Function of the chloroplast hydrogenase in the microalga Chlamydomonas: the role of hydrogenase and state transitions during photosynthetic activation in anaerobiosis. PLoS One 2013, 8:e64161.
    • (2013) PLoS One , vol.8 , pp. e64161
    • Ghysels, B.1    Godaux, D.2    Matagne, R.F.3    Cardol, P.4    Franck, F.5
  • 46
    • 84873692596 scopus 로고    scopus 로고
    • Pyruvate:ferredoxin oxidoreductase is coupled to light-independent hydrogen production in Chlamydomonas reinhardtii
    • Noth J., Krawietz D., Hemschemeier A., Happe T. Pyruvate:ferredoxin oxidoreductase is coupled to light-independent hydrogen production in Chlamydomonas reinhardtii. J. Biol. Chem. 2013, 288:4368-4377.
    • (2013) J. Biol. Chem. , vol.288 , pp. 4368-4377
    • Noth, J.1    Krawietz, D.2    Hemschemeier, A.3    Happe, T.4
  • 49
    • 0029077725 scopus 로고
    • Characterization of an operon encoding an NADP-reducing hydrogenase in Desulfovibrio fructosovorans
    • Malki S., Saimmaime I., De Luca G., Rousset M., Dermoun Z., Belaich J.P. Characterization of an operon encoding an NADP-reducing hydrogenase in Desulfovibrio fructosovorans. J. Bacteriol. 1995, 177:2628-2636.
    • (1995) J. Bacteriol. , vol.177 , pp. 2628-2636
    • Malki, S.1    Saimmaime, I.2    De Luca, G.3    Rousset, M.4    Dermoun, Z.5    Belaich, J.P.6
  • 50
    • 4344700076 scopus 로고    scopus 로고
    • A multisubunit membrane-bound [NiFe] hydrogenase and an NADH-dependent Fe-only hydrogenase in the fermenting bacterium Thermoanaerobacter tengcongensis
    • Soboh B., Linder D., Hedderich R. A multisubunit membrane-bound [NiFe] hydrogenase and an NADH-dependent Fe-only hydrogenase in the fermenting bacterium Thermoanaerobacter tengcongensis. Microbiology 2004, 150:2451-2463.
    • (2004) Microbiology , vol.150 , pp. 2451-2463
    • Soboh, B.1    Linder, D.2    Hedderich, R.3
  • 51
    • 0035078895 scopus 로고    scopus 로고
    • Fe-only hydrogenase from Thermotoga maritima
    • Verhagen M.F., Adams M.W. Fe-only hydrogenase from Thermotoga maritima. Methods Enzymol. 2001, 331:216-226.
    • (2001) Methods Enzymol. , vol.331 , pp. 216-226
    • Verhagen, M.F.1    Adams, M.W.2
  • 52
    • 67649413347 scopus 로고    scopus 로고
    • The iron-hydrogenase of Thermotoga maritima utilizes ferredoxin and NADH synergistically: a new perspective on anaerobic hydrogen production
    • Schut G.J., Adams M.W. The iron-hydrogenase of Thermotoga maritima utilizes ferredoxin and NADH synergistically: a new perspective on anaerobic hydrogen production. J. Bacteriol. 2009, 191:4451-4457.
    • (2009) J. Bacteriol. , vol.191 , pp. 4451-4457
    • Schut, G.J.1    Adams, M.W.2
  • 53
    • 38649143651 scopus 로고    scopus 로고
    • Energy conservation via electron-transferring flavoprotein in anaerobic bacteria
    • Herrmann G., Jayamani E., Mai G., Buckel W. Energy conservation via electron-transferring flavoprotein in anaerobic bacteria. J. Bacteriol. 2008, 190:784-791.
    • (2008) J. Bacteriol. , vol.190 , pp. 784-791
    • Herrmann, G.1    Jayamani, E.2    Mai, G.3    Buckel, W.4
  • 54
    • 38649099718 scopus 로고    scopus 로고
    • Coupled ferredoxin and crotonyl coenzyme A (CoA) reduction with NADH catalyzed by the butyryl-CoA dehydrogenase/Etf complex from Clostridium kluyveri
    • Li F., Hinderberger J., Seedorf H., Zhang J., Buckel W., Thauer R.K. Coupled ferredoxin and crotonyl coenzyme A (CoA) reduction with NADH catalyzed by the butyryl-CoA dehydrogenase/Etf complex from Clostridium kluyveri. J. Bacteriol. 2008, 190:843-850.
    • (2008) J. Bacteriol. , vol.190 , pp. 843-850
    • Li, F.1    Hinderberger, J.2    Seedorf, H.3    Zhang, J.4    Buckel, W.5    Thauer, R.K.6
  • 56
    • 0029066951 scopus 로고
    • A variable-temperature direct electrochemical study of metalloproteins from hyperthermophilic microorganisms involved in hydrogen production from pyruvate
    • Smith E.T., Blamey J.M., Zhou Z.H., Adams M.W. A variable-temperature direct electrochemical study of metalloproteins from hyperthermophilic microorganisms involved in hydrogen production from pyruvate. Biochemistry 1995, 34:7161-7169.
    • (1995) Biochemistry , vol.34 , pp. 7161-7169
    • Smith, E.T.1    Blamey, J.M.2    Zhou, Z.H.3    Adams, M.W.4
  • 57
    • 0034980543 scopus 로고    scopus 로고
    • Ferredoxin from Thermotoga maritima
    • Sterner R. Ferredoxin from Thermotoga maritima. Methods Enzymol. 2001, 334:23-30.
    • (2001) Methods Enzymol. , vol.334 , pp. 23-30
    • Sterner, R.1
  • 58
    • 70350455960 scopus 로고    scopus 로고
    • Identification of the [FeFe]-hydrogenase responsible for hydrogen generation in Thermoanaerobacterium saccharolyticum and demonstration of increased ethanol yield via hydrogenase knockout
    • Shaw A.J., Hogsett D.A., Lynd L.R. Identification of the [FeFe]-hydrogenase responsible for hydrogen generation in Thermoanaerobacterium saccharolyticum and demonstration of increased ethanol yield via hydrogenase knockout. J. Bacteriol. 2009, 191:6457-6464.
    • (2009) J. Bacteriol. , vol.191 , pp. 6457-6464
    • Shaw, A.J.1    Hogsett, D.A.2    Lynd, L.R.3
  • 59
    • 84866142108 scopus 로고    scopus 로고
    • A bacterial electron-bifurcating hydrogenase
    • Schuchmann K., Muller V. A bacterial electron-bifurcating hydrogenase. J. Biol. Chem. 2012, 287:31165-31171.
    • (2012) J. Biol. Chem. , vol.287 , pp. 31165-31171
    • Schuchmann, K.1    Muller, V.2
  • 61
    • 84887087494 scopus 로고    scopus 로고
    • + and is reversibly coupled to the membrane potential
    • + and is reversibly coupled to the membrane potential. J. Biol. Chem. 2013, 288:31496-31502.
    • (2013) J. Biol. Chem. , vol.288 , pp. 31496-31502
    • Hess, V.1    Schuchmann, K.2    Muller, V.3
  • 62
    • 84874743762 scopus 로고    scopus 로고
    • A reversible electron-bifurcating ferredoxin- and NAD-dependent [FeFe]-hydrogenase (HydABC) in Moorella thermoacetica
    • Wang S., Huang H., Kahnt J., Thauer R.K. A reversible electron-bifurcating ferredoxin- and NAD-dependent [FeFe]-hydrogenase (HydABC) in Moorella thermoacetica. J. Bacteriol. 2013, 195:1267-1275.
    • (2013) J. Bacteriol. , vol.195 , pp. 1267-1275
    • Wang, S.1    Huang, H.2    Kahnt, J.3    Thauer, R.K.4
  • 63
    • 84884198848 scopus 로고    scopus 로고
    • NADP-specific electron-bifurcating [FeFe]-hydrogenase in a functional complex with formate dehydrogenase in Clostridium autoethanogenum grown on CO
    • Wang S., Huang H., Kahnt J., Mueller A.P., Kopke M., Thauer R.K. NADP-specific electron-bifurcating [FeFe]-hydrogenase in a functional complex with formate dehydrogenase in Clostridium autoethanogenum grown on CO. J. Bacteriol. 2013, 195:4373-4386.
    • (2013) J. Bacteriol. , vol.195 , pp. 4373-4386
    • Wang, S.1    Huang, H.2    Kahnt, J.3    Mueller, A.P.4    Kopke, M.5    Thauer, R.K.6
  • 64
    • 84997585139 scopus 로고    scopus 로고
    • Genome sequence of the autotrophic acetogen Clostridium autoethanogenum JA1-1 strain DSM 10061, a producer of ethanol from carbon monoxide
    • Bruno-Barcena J.M., Chinn M.S., Grunden A.M. Genome sequence of the autotrophic acetogen Clostridium autoethanogenum JA1-1 strain DSM 10061, a producer of ethanol from carbon monoxide. Genome Announc. 2013, 1.
    • (2013) Genome Announc. , vol.1
    • Bruno-Barcena, J.M.1    Chinn, M.S.2    Grunden, A.M.3
  • 65
    • 84879327113 scopus 로고    scopus 로고
    • Genome sequencing of rumen bacteria and archaea and its application to methane mitigation strategies
    • Leahy S.C., Kelly W.J., Ronimus R.S., Wedlock N., Altermann E., Attwood G.T. Genome sequencing of rumen bacteria and archaea and its application to methane mitigation strategies. Animal 2013, 7(Suppl. 2):235-243.
    • (2013) Animal , vol.7 , pp. 235-243
    • Leahy, S.C.1    Kelly, W.J.2    Ronimus, R.S.3    Wedlock, N.4    Altermann, E.5    Attwood, G.T.6
  • 66
    • 84894028767 scopus 로고    scopus 로고
    • Symbiotic digestion of lignocellulose in termite guts
    • Brune A. Symbiotic digestion of lignocellulose in termite guts. Nat. Rev. Microbiol. 2014, 12:168-180.
    • (2014) Nat. Rev. Microbiol. , vol.12 , pp. 168-180
    • Brune, A.1
  • 67
    • 0037151768 scopus 로고    scopus 로고
    • An [Fe] hydrogenase from the anaerobic hydrogenosome-containing fungus Neocallimastix frontalis L2
    • Davidson E.A., van der Giezen M., Horner D.S., Embley T.M., Howe C.J. An [Fe] hydrogenase from the anaerobic hydrogenosome-containing fungus Neocallimastix frontalis L2. Gene 2002, 296:45-52.
    • (2002) Gene , vol.296 , pp. 45-52
    • Davidson, E.A.1    van der Giezen, M.2    Horner, D.S.3    Embley, T.M.4    Howe, C.J.5
  • 68
    • 84877356167 scopus 로고    scopus 로고
    • Some are more equal than others: the role of "keystone" species in the degradation of recalcitrant substrates
    • Ze X., Le Mougen F., Duncan S.H., Louis P., Flint H.J. Some are more equal than others: the role of "keystone" species in the degradation of recalcitrant substrates. Gut Microbes 2013, 4:236-240.
    • (2013) Gut Microbes , vol.4 , pp. 236-240
    • Ze, X.1    Le Mougen, F.2    Duncan, S.H.3    Louis, P.4    Flint, H.J.5
  • 69
    • 85140279169 scopus 로고    scopus 로고
    • Structure and function of [NiFe]-hydrogenases
    • Fontecilla-Camps J.C. Structure and function of [NiFe]-hydrogenases. Met. Ions Life Sci. 2009, 6:151-178.
    • (2009) Met. Ions Life Sci. , vol.6 , pp. 151-178
    • Fontecilla-Camps, J.C.1
  • 70
    • 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
  • 71
    • 84858700660 scopus 로고    scopus 로고
    • Characterization of Escherichia coli [NiFe]-hydrogenase distribution during fermentative growth at different pHs
    • Trchounian K., Pinske C., Sawers R.G., Trchounian A. Characterization of Escherichia coli [NiFe]-hydrogenase distribution during fermentative growth at different pHs. Cell Biochem. Biophys. 2012, 62:433-440.
    • (2012) Cell Biochem. Biophys. , vol.62 , pp. 433-440
    • Trchounian, K.1    Pinske, C.2    Sawers, R.G.3    Trchounian, A.4
  • 72
    • 84885437565 scopus 로고    scopus 로고
    • Roles of HynAB and Ech, the only two hydrogenases found in the model sulfate reducer Desulfovibrio gigas
    • Morais-Silva F.O., Santos C.I., Rodrigues R., Pereira I.A., Rodrigues-Pousada C. Roles of HynAB and Ech, the only two hydrogenases found in the model sulfate reducer Desulfovibrio gigas. J. Bacteriol. 2013, 195:4753-4760.
    • (2013) J. Bacteriol. , vol.195 , pp. 4753-4760
    • Morais-Silva, F.O.1    Santos, C.I.2    Rodrigues, R.3    Pereira, I.A.4    Rodrigues-Pousada, C.5
  • 75
    • 65249140547 scopus 로고    scopus 로고
    • New insights into the respiratory chains of the chemolithoautotrophic and hyperthermophilic bacterium Aquifex aeolicus
    • Guiral M., Prunetti L., Lignon S., Lebrun R., Moinier D., Giudici-Orticonit M.T. New insights into the respiratory chains of the chemolithoautotrophic and hyperthermophilic bacterium Aquifex aeolicus. J. Proteome Res. 2009, 8:1717-1730.
    • (2009) J. Proteome Res. , vol.8 , pp. 1717-1730
    • Guiral, M.1    Prunetti, L.2    Lignon, S.3    Lebrun, R.4    Moinier, D.5    Giudici-Orticonit, M.T.6
  • 76
    • 0141814895 scopus 로고    scopus 로고
    • Membrane-bound hydrogenase and sulfur reductase of the hyperthermophilic and acidophilic archaeon Acidianus ambivalens
    • Laska S., Lottspeich F., Kletzin A. Membrane-bound hydrogenase and sulfur reductase of the hyperthermophilic and acidophilic archaeon Acidianus ambivalens. Microbiology 2003, 149:2357-2371.
    • (2003) Microbiology , vol.149 , pp. 2357-2371
    • Laska, S.1    Lottspeich, F.2    Kletzin, A.3
  • 77
    • 0037388041 scopus 로고    scopus 로고
    • Nitrogen fixation and photosynthetic oxygen evolution in cyanobacteria
    • Berman-Frank I., Lundgren P., Falkowski P. Nitrogen fixation and photosynthetic oxygen evolution in cyanobacteria. Res. Microbiol. 2003, 154:157-164.
    • (2003) Res. Microbiol. , vol.154 , pp. 157-164
    • Berman-Frank, I.1    Lundgren, P.2    Falkowski, P.3
  • 79
    • 84893004441 scopus 로고    scopus 로고
    • The uptake hydrogenase in the unicellular diazotrophic cyanobacterium Cyanothece sp. strain PCC 7822 protects nitrogenase from oxygen toxicity
    • Zhang X., Sherman D.M., Sherman L.A. The uptake hydrogenase in the unicellular diazotrophic cyanobacterium Cyanothece sp. strain PCC 7822 protects nitrogenase from oxygen toxicity. J. Bacteriol. 2014, 196:840-849.
    • (2014) J. Bacteriol. , vol.196 , pp. 840-849
    • Zhang, X.1    Sherman, D.M.2    Sherman, L.A.3
  • 80
    • 84867198378 scopus 로고    scopus 로고
    • Inactivation of uptake hydrogenase leads to enhanced and sustained hydrogen production with high nitrogenase activity under high light exposure in the cyanobacterium Anabaena siamensis TISTR 8012
    • Khetkorn W., Lindblad P., Incharoensakdi A. Inactivation of uptake hydrogenase leads to enhanced and sustained hydrogen production with high nitrogenase activity under high light exposure in the cyanobacterium Anabaena siamensis TISTR 8012. J. Biol. Eng. 2012, 6:19.
    • (2012) J. Biol. Eng. , vol.6 , pp. 19
    • Khetkorn, W.1    Lindblad, P.2    Incharoensakdi, A.3
  • 82
    • 0025333468 scopus 로고
    • Cloning, sequence determination, and expression of the genes encoding the subunits of the nickel-containing 8-hydroxy-5-deazaflavin reducing hydrogenase from Methanobacterium thermoautotrophicum delta H
    • Alex L.A., Reeve J.N., Orme-Johnson W.H., Walsh C.T. Cloning, sequence determination, and expression of the genes encoding the subunits of the nickel-containing 8-hydroxy-5-deazaflavin reducing hydrogenase from Methanobacterium thermoautotrophicum delta H. Biochemistry 1990, 29:7237-7244.
    • (1990) Biochemistry , vol.29 , pp. 7237-7244
    • Alex, L.A.1    Reeve, J.N.2    Orme-Johnson, W.H.3    Walsh, C.T.4
  • 83
    • 84904263793 scopus 로고    scopus 로고
    • 420-reducing [NiFe]-yydrogenase complex from Methanothermobacter marburgensis, the first X-ray structure of a group 3 family member
    • 420-reducing [NiFe]-yydrogenase complex from Methanothermobacter marburgensis, the first X-ray structure of a group 3 family member. J. Mol. Biol. 2014, 426:2813-2826.
    • (2014) J. Mol. Biol. , vol.426 , pp. 2813-2826
    • Vitt, S.1    Ma, K.2    Warkentin, E.3    Moll, J.4    Pierik, A.J.5    Shima, S.6    Ermler, U.7
  • 84
    • 79958023257 scopus 로고    scopus 로고
    • Distinct physiological roles of the three [NiFe]-hydrogenase orthologs in the hyperthermophilic archaeon Thermococcus kodakarensis
    • Kanai T., Matsuoka R., Beppu H., Nakajima A., Okada Y., Atomi H., Imanaka T. Distinct physiological roles of the three [NiFe]-hydrogenase orthologs in the hyperthermophilic archaeon Thermococcus kodakarensis. J. Bacteriol. 2011, 193:3109-3116.
    • (2011) J. Bacteriol. , vol.193 , pp. 3109-3116
    • Kanai, T.1    Matsuoka, R.2    Beppu, H.3    Nakajima, A.4    Okada, Y.5    Atomi, H.6    Imanaka, T.7
  • 85
    • 0035085834 scopus 로고    scopus 로고
    • Hydrogenases I and II from Pyrococcus furiosus
    • Ma K., Adams M.W. Hydrogenases I and II from Pyrococcus furiosus. Methods Enzymol. 2001, 331:208-216.
    • (2001) Methods Enzymol. , vol.331 , pp. 208-216
    • Ma, K.1    Adams, M.W.2
  • 86
    • 84871389424 scopus 로고    scopus 로고
    • Mutational analyses of the enzymes involved in the metabolism of hydrogen by the hyperthermophilic archaeon Pyrococcus furiosus
    • Schut G.J., Nixon W.J., Lipscomb G.L., Scott R.A., Adams M.W. Mutational analyses of the enzymes involved in the metabolism of hydrogen by the hyperthermophilic archaeon Pyrococcus furiosus. Front. Microbiol. 2012, 3:163.
    • (2012) Front. Microbiol. , vol.3 , pp. 163
    • Schut, G.J.1    Nixon, W.J.2    Lipscomb, G.L.3    Scott, R.A.4    Adams, M.W.5
  • 88
    • 79952588675 scopus 로고    scopus 로고
    • Coupling of ferredoxin and heterodisulfide reduction via electron bifurcation in hydrogenotrophic methanogenic archaea
    • Kaster A.K., Moll J., Parey K., Thauer R.K. Coupling of ferredoxin and heterodisulfide reduction via electron bifurcation in hydrogenotrophic methanogenic archaea. Proc. Natl. Acad. Sci. U. S. A. 2011, 108:2981-2986.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 2981-2986
    • Kaster, A.K.1    Moll, J.2    Parey, K.3    Thauer, R.K.4
  • 90
    • 55249110895 scopus 로고    scopus 로고
    • Genomic view of energy metabolism in Ralstonia eutropha H16
    • Cramm R. Genomic view of energy metabolism in Ralstonia eutropha H16. J. Mol. Microbiol. Biotechnol. 2009, 16:38-52.
    • (2009) J. Mol. Microbiol. Biotechnol. , vol.16 , pp. 38-52
    • Cramm, R.1
  • 91
    • 84893141463 scopus 로고    scopus 로고
    • The bidirectional NiFe-hydrogenase in Synechocystis sp. PCC 6803 is reduced by flavodoxin and ferredoxin and is essential under mixotrophic, nitrate-limiting conditions
    • Gutekunst K., Chen X., Schreiber K., Kaspar U., Makam S., Appel J. The bidirectional NiFe-hydrogenase in Synechocystis sp. PCC 6803 is reduced by flavodoxin and ferredoxin and is essential under mixotrophic, nitrate-limiting conditions. J. Biol. Chem. 2014, 289:1930-1937.
    • (2014) J. Biol. Chem. , vol.289 , pp. 1930-1937
    • Gutekunst, K.1    Chen, X.2    Schreiber, K.3    Kaspar, U.4    Makam, S.5    Appel, J.6
  • 92
    • 0037934657 scopus 로고    scopus 로고
    • A simple energy-conserving system: proton reduction coupled to proton translocation
    • Sapra R., Bagramyan K., Adams M.W. A simple energy-conserving system: proton reduction coupled to proton translocation. Proc. Natl. Acad. Sci. U. S. A. 2003, 100:7545-7550.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 7545-7550
    • Sapra, R.1    Bagramyan, K.2    Adams, M.W.3
  • 93
    • 0033568398 scopus 로고    scopus 로고
    • Methanobacterium thermoautotrophicum encodes two multisubunit membrane-bound [NiFe] hydrogenases. Transcription of the operons and sequence analysis of the deduced proteins
    • Tersteegen A., Hedderich R. Methanobacterium thermoautotrophicum encodes two multisubunit membrane-bound [NiFe] hydrogenases. Transcription of the operons and sequence analysis of the deduced proteins. Eur. J. Biochem. 1999, 264:930-943.
    • (1999) Eur. J. Biochem. , vol.264 , pp. 930-943
    • Tersteegen, A.1    Hedderich, R.2
  • 95
    • 0022376555 scopus 로고
    • Differential expression of hydrogenase isoenzymes in Escherichia coli K-12: evidence for a third isoenzyme
    • Sawers R.G., Ballantine S.P., Boxer D.H. Differential expression of hydrogenase isoenzymes in Escherichia coli K-12: evidence for a third isoenzyme. J. Bacteriol. 1985, 164:1324-1331.
    • (1985) J. Bacteriol. , vol.164 , pp. 1324-1331
    • Sawers, R.G.1    Ballantine, S.P.2    Boxer, D.H.3
  • 97
    • 0036436922 scopus 로고    scopus 로고
    • 2-evolving enzyme complex from Carboxydothermus hydrogenoformans
    • 2-evolving enzyme complex from Carboxydothermus hydrogenoformans. Eur. J. Biochem. 2002, 269:5712-5721.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 5712-5721
    • Soboh, B.1    Linder, D.2    Hedderich, R.3
  • 98
    • 0033214609 scopus 로고    scopus 로고
    • Purification and catalytic properties of Ech hydrogenase from Methanosarcina barkeri
    • Meuer J., Bartoschek S., Koch J., Kunkel A., Hedderich R. Purification and catalytic properties of Ech hydrogenase from Methanosarcina barkeri. Eur. J. Biochem. 1999, 265:325-335.
    • (1999) Eur. J. Biochem. , vol.265 , pp. 325-335
    • Meuer, J.1    Bartoschek, S.2    Koch, J.3    Kunkel, A.4    Hedderich, R.5
  • 99
    • 0034045136 scopus 로고    scopus 로고
    • Purification and characterization of a membrane-bound hydrogenase from the hyperthermophilic archaeon Pyrococcus furiosus
    • Sapra R., Verhagen M.F.J.M., Adams M.W.W. Purification and characterization of a membrane-bound hydrogenase from the hyperthermophilic archaeon Pyrococcus furiosus. J. Bacteriol. 2000, 182:3423-3428.
    • (2000) J. Bacteriol. , vol.182 , pp. 3423-3428
    • Sapra, R.1    Verhagen, M.F.J.M.2    Adams, M.W.W.3
  • 102
    • 77955298231 scopus 로고    scopus 로고
    • Characterization of energy-conserving hydrogenase B in Methanococcus maripaludis
    • Major T.A., Liu Y., Whitman W.B. Characterization of energy-conserving hydrogenase B in Methanococcus maripaludis. J. Bacteriol. 2010, 192:4022-4030.
    • (2010) J. Bacteriol. , vol.192 , pp. 4022-4030
    • Major, T.A.1    Liu, Y.2    Whitman, W.B.3
  • 104
    • 84884237449 scopus 로고    scopus 로고
    • Novel, oxygen-insensitive group 5 [NiFe]-hydrogenase in Ralstonia eutropha
    • Schäfer C., Friedrich B., Lenz O. Novel, oxygen-insensitive group 5 [NiFe]-hydrogenase in Ralstonia eutropha. Appl. Environ. Microbiol. 2013, 79:5137-5145.
    • (2013) Appl. Environ. Microbiol. , vol.79 , pp. 5137-5145
    • Schäfer, C.1    Friedrich, B.2    Lenz, O.3
  • 105
    • 77953950338 scopus 로고    scopus 로고
    • Streptomycetes contributing to atmospheric molecular hydrogen soil uptake are widespread and encode a putative high-affinity [NiFe]-hydrogenase
    • Constant P., Chowdhury S.P., Pratscher J., Conrad R. Streptomycetes contributing to atmospheric molecular hydrogen soil uptake are widespread and encode a putative high-affinity [NiFe]-hydrogenase. Environ. Microbiol. 2010, 12:821-829.
    • (2010) Environ. Microbiol. , vol.12 , pp. 821-829
    • Constant, P.1    Chowdhury, S.P.2    Pratscher, J.3    Conrad, R.4
  • 108
    • 0033134667 scopus 로고    scopus 로고
    • Removal of the bridging ligand atom at the Ni-Fe active site of [NiFe] hydrogenase upon reduction with H2, as revealed by X-ray structure analysis at 1.4Å resolution
    • Higuchi Y., Ogata H., Miki K., Yasuoka N., Yagi T. Removal of the bridging ligand atom at the Ni-Fe active site of [NiFe] hydrogenase upon reduction with H2, as revealed by X-ray structure analysis at 1.4Å resolution. Structure 1999, 7:549-556.
    • (1999) Structure , vol.7 , pp. 549-556
    • Higuchi, Y.1    Ogata, H.2    Miki, K.3    Yasuoka, N.4    Yagi, T.5
  • 109
    • 0033135158 scopus 로고    scopus 로고
    • The crystal structure of a reduced [NiFeSe] hydrogenase provides an image of the activated catalytic center
    • Garcin E., Vernede X., Hatchikian E., Volbeda A., Frey M., Fontecilla-Camps J. The crystal structure of a reduced [NiFeSe] hydrogenase provides an image of the activated catalytic center. Structure 1999, 7:557-566.
    • (1999) Structure , vol.7 , pp. 557-566
    • Garcin, E.1    Vernede, X.2    Hatchikian, E.3    Volbeda, A.4    Frey, M.5    Fontecilla-Camps, J.6
  • 110
    • 0037009993 scopus 로고    scopus 로고
    • Structural studies of the carbon monoxide complex of [NiFe] hydrogenase from Desulfovibrio vulgaris Miyazaki F: suggestion for the initial activation site for dihydrogen
    • Ogata H., Mizoguchi Y., Mizuno N., Miki K., Adachi S.-i., Yasuoka N., Yagi T., Yamauchi O., Hirota S., Higuchi Y. Structural studies of the carbon monoxide complex of [NiFe] hydrogenase from Desulfovibrio vulgaris Miyazaki F: suggestion for the initial activation site for dihydrogen. J. Am. Chem. Soc. 2002, 124:11628-11635.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 11628-11635
    • Ogata, H.1    Mizoguchi, Y.2    Mizuno, N.3    Miki, K.4    Adachi, S.-I.5    Yasuoka, N.6    Yagi, T.7    Yamauchi, O.8    Hirota, S.9    Higuchi, Y.10
  • 112
    • 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
  • 113
    • 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
  • 114
    • 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
  • 117
    • 84871851876 scopus 로고    scopus 로고
    • Analyses of the large subunit histidine-rich motif expose an alternative proton transfer pathway in [NiFe] hydrogenases
    • Szo'ri-Dorogházi E., Maróti G., Szo'ri M., Nyilasi A., Rákhely G., Kovács K.L. Analyses of the large subunit histidine-rich motif expose an alternative proton transfer pathway in [NiFe] hydrogenases. PLoS One 2012, 7:e34666.
    • (2012) PLoS One , vol.7 , pp. e34666
    • Szo'ri-Dorogházi, E.1    Maróti, G.2    Szo'ri, M.3    Nyilasi, A.4    Rákhely, G.5    Kovács, K.L.6
  • 118
    • 35748942883 scopus 로고    scopus 로고
    • Computational studies of [NiFe] and [FeFe] hydrogenases
    • Siegbahn P.E.M., Tye J.W., Hall M.B. Computational studies of [NiFe] and [FeFe] hydrogenases. Chem. Rev. 2007, 107:4414-4435.
    • (2007) Chem. Rev. , vol.107 , pp. 4414-4435
    • Siegbahn, P.E.M.1    Tye, J.W.2    Hall, M.B.3
  • 119
    • 84884318697 scopus 로고    scopus 로고
    • [NiFe] hydrogenases: A common active site for hydrogen metabolism under diverse conditions
    • Shafaat H.S., Rüdiger O., Ogata H., Lubitz W. [NiFe] hydrogenases: A common active site for hydrogen metabolism under diverse conditions. Biochim. Biophys. Acta Bioenerg. 2013, 1827:986-1002.
    • (2013) Biochim. Biophys. Acta Bioenerg. , vol.1827 , pp. 986-1002
    • Shafaat, H.S.1    Rüdiger, O.2    Ogata, H.3    Lubitz, W.4
  • 120
    • 84893803129 scopus 로고    scopus 로고
    • Disclosure of Key stereoelectronic factors for efficient H2 binding and cleavage in the active site of [NiFe]-hydrogenases
    • Bruschi M., Tiberti M., Guerra A., De Gioia L. Disclosure of Key stereoelectronic factors for efficient H2 binding and cleavage in the active site of [NiFe]-hydrogenases. J. Am. Chem. Soc. 2014, 136:1803-1814.
    • (2014) J. Am. Chem. Soc. , vol.136 , pp. 1803-1814
    • Bruschi, M.1    Tiberti, M.2    Guerra, A.3    De Gioia, L.4
  • 121
    • 47949108165 scopus 로고    scopus 로고
    • Density functional theory on the larger active site models for [NiFe] hydrogenases: Two-state reactivity?
    • Wu H., Hall M.B. Density functional theory on the larger active site models for [NiFe] hydrogenases: Two-state reactivity?. C. R. Chim. 2008, 11:790-804.
    • (2008) C. R. Chim. , vol.11 , pp. 790-804
    • Wu, H.1    Hall, M.B.2
  • 122
    • 0026073745 scopus 로고
    • Detection and characterization of exchangeable protons bound to the hydrogen-activation nickel site of Desulfovibrio gigas hydrogenase: a proton and deuterium Q-band ENDOR study
    • Fan C., Teixeira M., Moura J., Moura I., Huynh Boi H., Le Gall J., Peck H.D., Hoffman B.M. Detection and characterization of exchangeable protons bound to the hydrogen-activation nickel site of Desulfovibrio gigas hydrogenase: a proton and deuterium Q-band ENDOR study. J. Am. Chem. Soc. 1991, 113:20-24.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 20-24
    • Fan, C.1    Teixeira, M.2    Moura, J.3    Moura, I.4    Huynh Boi, H.5    Le Gall, J.6    Peck, H.D.7    Hoffman, B.M.8
  • 123
    • 77955460505 scopus 로고    scopus 로고
    • Potential hydrogen bottleneck in nickel-iron hydrogenase
    • Keith J.M., Hall M.B. Potential hydrogen bottleneck in nickel-iron hydrogenase. Inorg. Chem. 2010, 49:6378-6380.
    • (2010) Inorg. Chem. , vol.49 , pp. 6378-6380
    • Keith, J.M.1    Hall, M.B.2
  • 124
    • 12944326891 scopus 로고    scopus 로고
    • An orientation-selected ENDOR and HYSCORE study of the Ni-C active state of Desulfovibrio vulgaris Miyazaki F hydrogenase
    • Foerster S., Gastel M., Brecht M., Lubitz W. An orientation-selected ENDOR and HYSCORE study of the Ni-C active state of Desulfovibrio vulgaris Miyazaki F hydrogenase. J. Biol. Inorg. Chem. 2005, 10:51-62.
    • (2005) J. Biol. Inorg. Chem. , vol.10 , pp. 51-62
    • Foerster, S.1    Gastel, M.2    Brecht, M.3    Lubitz, W.4
  • 125
    • 84874974421 scopus 로고    scopus 로고
    • Computational study of the electronic structure and magnetic properties of the Ni-C state in [NiFe] hydrogenases including the second coordination sphere
    • Kampa M., Lubitz W., van Gastel M., Neese F. Computational study of the electronic structure and magnetic properties of the Ni-C state in [NiFe] hydrogenases including the second coordination sphere. J. Biol. Inorg. Chem. 2012, 17:1269-1281.
    • (2012) J. Biol. Inorg. Chem. , vol.17 , pp. 1269-1281
    • Kampa, M.1    Lubitz, W.2    van Gastel, M.3    Neese, F.4
  • 127
    • 35048857033 scopus 로고    scopus 로고
    • The electronic structure of the H-cluster in the [FeFe]-hydrogenase from Desulfovibrio desulfuricans: a Q-band 57Fe-ENDOR and HYSCORE study
    • Silakov A., Reijerse E.J., Albracht S.P.J., Hatchikian E.C., Lubitz W. The electronic structure of the H-cluster in the [FeFe]-hydrogenase from Desulfovibrio desulfuricans: a Q-band 57Fe-ENDOR and HYSCORE study. J. Am. Chem. Soc. 2007, 129:11447-11458.
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 11447-11458
    • Silakov, A.1    Reijerse, E.J.2    Albracht, S.P.J.3    Hatchikian, E.C.4    Lubitz, W.5
  • 128
    • 0034801337 scopus 로고    scopus 로고
    • Mössbauer characterization of the iron-sulfur clusters in Desulfovibrio vulgaris hydrogenase
    • Pereira A.S., Tavares P., Moura I., Moura J.J.G., Huynh B.H. Mössbauer characterization of the iron-sulfur clusters in Desulfovibrio vulgaris hydrogenase. J. Am. Chem. Soc. 2001, 123:2771-2782.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 2771-2782
    • Pereira, A.S.1    Tavares, P.2    Moura, I.3    Moura, J.J.G.4    Huynh, B.H.5
  • 129
    • 0042357244 scopus 로고    scopus 로고
    • Electronic structure of the H cluster in [Fe]-hydrogenases
    • Popescu C.V., Münck E. Electronic structure of the H cluster in [Fe]-hydrogenases. J. Am. Chem. Soc. 1999, 121:7877-7884.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 7877-7884
    • Popescu, C.V.1    Münck, E.2
  • 130
    • 34548635010 scopus 로고    scopus 로고
    • Structural insights into the active-ready form of [FeFe]-hydrogenase and mechanistic details of its inhibition by carbon monoxide
    • Greco C., Bruschi M., Heimdal J., Fantucci P., De Gioia L., Ryde U. Structural insights into the active-ready form of [FeFe]-hydrogenase and mechanistic details of its inhibition by carbon monoxide. Inorg. Chem. 2007, 46:7256-7258.
    • (2007) Inorg. Chem. , vol.46 , pp. 7256-7258
    • Greco, C.1    Bruschi, M.2    Heimdal, J.3    Fantucci, P.4    De Gioia, L.5    Ryde, U.6
  • 132
    • 29544449553 scopus 로고    scopus 로고
    • Computational studies of the H-cluster of Fe-only hydrogenases: geometric, electronic, and magnetic properties and their dependence on the [Fe4S4] cubane
    • Fiedler A.T., Brunold T.C. Computational studies of the H-cluster of Fe-only hydrogenases: geometric, electronic, and magnetic properties and their dependence on the [Fe4S4] cubane. Inorg. Chem. 2005, 44:9322-9334.
    • (2005) Inorg. Chem. , vol.44 , pp. 9322-9334
    • Fiedler, A.T.1    Brunold, T.C.2
  • 133
    • 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
  • 134
    • 77950806359 scopus 로고    scopus 로고
    • Functionally relevant interplay between the Fe4S4 cluster and CN- ligands in the active site of [FeFe]-hydrogenases
    • Bruschi M., Greco C., Bertini L., Fantucci P., Ryde U., Gioia L.D. Functionally relevant interplay between the Fe4S4 cluster and CN- ligands in the active site of [FeFe]-hydrogenases. J. Am. Chem. Soc. 2010, 132:4992-4993.
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 4992-4993
    • Bruschi, M.1    Greco, C.2    Bertini, L.3    Fantucci, P.4    Ryde, U.5    Gioia, L.D.6
  • 137
    • 0035961483 scopus 로고    scopus 로고
    • Crystallographic and FTIR spectroscopic evidence of changes in Fe coordination upon reduction of the active site of the Fe-only hydrogenase from Desulfovibrio desulfuricans
    • Nicolet Y., de Lacey A.L., Vernède X., Fernandez V.M., Hatchikian E.C., Fontecilla-Camps J.C. Crystallographic and FTIR spectroscopic evidence of changes in Fe coordination upon reduction of the active site of the Fe-only hydrogenase from Desulfovibrio desulfuricans. J. Am. Chem. Soc. 2001, 123:1596-1601.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 1596-1601
    • Nicolet, Y.1    de Lacey, A.L.2    Vernède, X.3    Fernandez, V.M.4    Hatchikian, E.C.5    Fontecilla-Camps, J.C.6
  • 138
    • 0034822720 scopus 로고    scopus 로고
    • A capable bridging ligand for Fe-only hydrogenase: density functional calculations of a Low-energy route for heterolytic cleavage and formation of dihydrogen
    • Fan H.-J., Hall M.B. A capable bridging ligand for Fe-only hydrogenase: density functional calculations of a Low-energy route for heterolytic cleavage and formation of dihydrogen. J. Am. Chem. Soc. 2001, 123:3828-3829.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 3828-3829
    • Fan, H.-J.1    Hall, M.B.2
  • 140
    • 79958063384 scopus 로고    scopus 로고
    • Electron and spin density topology of the H-cluster and its biomimetic complexes
    • Giles L.J., Grigoropoulos A., Szilagyi R.K. Electron and spin density topology of the H-cluster and its biomimetic complexes. Eur. J. Inorg. Chem. 2011, 2011:2677-2690.
    • (2011) Eur. J. Inorg. Chem. , vol.2011 , pp. 2677-2690
    • Giles, L.J.1    Grigoropoulos, A.2    Szilagyi, R.K.3
  • 141
    • 84881173030 scopus 로고    scopus 로고
    • Does the environment around the H-cluster allow coordination of the pendant amine to the catalytic iron center in [FeFe] hydrogenases? Answers from theory
    • Miyake T., Bruschi M., Cosentino U., Baffert C., Fourmond V., Léger C., Moro G., De Gioia L., Greco C. Does the environment around the H-cluster allow coordination of the pendant amine to the catalytic iron center in [FeFe] hydrogenases? Answers from theory. J. Biol. Inorg. Chem. 2013, 18:693-700.
    • (2013) J. Biol. Inorg. Chem. , vol.18 , pp. 693-700
    • Miyake, T.1    Bruschi, M.2    Cosentino, U.3    Baffert, C.4    Fourmond, V.5    Léger, C.6    Moro, G.7    De Gioia, L.8    Greco, C.9
  • 142
    • 70349784948 scopus 로고    scopus 로고
    • Influence of the [2Fe] H subcluster environment on the properties of key intermediates in the catalytic cycle of [FeFe] hydrogenases: hints for the rational design of synthetic catalysts
    • Bruschi M., Greco C., Kaukonen M., Fantucci P., Ryde U., De Gioia L. Influence of the [2Fe] H subcluster environment on the properties of key intermediates in the catalytic cycle of [FeFe] hydrogenases: hints for the rational design of synthetic catalysts. Angew. Chem. Int. Ed. 2009, 48:3503-3506.
    • (2009) Angew. Chem. Int. Ed. , vol.48 , pp. 3503-3506
    • Bruschi, M.1    Greco, C.2    Kaukonen, M.3    Fantucci, P.4    Ryde, U.5    De Gioia, L.6
  • 143
    • 77955300546 scopus 로고    scopus 로고
    • Mechanism of hydrogen production in [Fe-Fe]-hydrogenases: A quantum mechanics/molecular mechanics study
    • Trohalaki S., Pachter R. Mechanism of hydrogen production in [Fe-Fe]-hydrogenases: A quantum mechanics/molecular mechanics study. Int. J. Hydrog. Energy 2010, 35:5318-5331.
    • (2010) Int. J. Hydrog. Energy , vol.35 , pp. 5318-5331
    • Trohalaki, S.1    Pachter, R.2
  • 144
    • 0034685468 scopus 로고    scopus 로고
    • Photochemistry at the active site of the carbon monoxide inhibited form of the iron-only hydrogenase (CpI)
    • Lemon B.J., Peters J.W. Photochemistry at the active site of the carbon monoxide inhibited form of the iron-only hydrogenase (CpI). J. Am. Chem. Soc. 2000, 122:3793-3794.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 3793-3794
    • Lemon, B.J.1    Peters, J.W.2
  • 145
    • 0034836307 scopus 로고    scopus 로고
    • Modeling the active sites in metalloenzymes. 3. Density functional calculations on models for [Fe]-hydrogenase: structures and vibrational frequencies of the observed redox forms and the reaction mechanism at the diiron active center
    • Cao Z., Hall M.B. Modeling the active sites in metalloenzymes. 3. Density functional calculations on models for [Fe]-hydrogenase: structures and vibrational frequencies of the observed redox forms and the reaction mechanism at the diiron active center. J. Am. Chem. Soc. 2001, 123:3734-3742.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 3734-3742
    • Cao, Z.1    Hall, M.B.2
  • 146
    • 0037065697 scopus 로고    scopus 로고
    • Infrared studies of the CO-inhibited form of the Fe-only hydrogenase from Clostridium pasteurianum I: Examination of its light sensitivity at cryogenic temperatures
    • Chen Z.J., Lemon B.J., Huang S., Swartz D.J., Peters J.W., Bagley K.A. Infrared studies of the CO-inhibited form of the Fe-only hydrogenase from Clostridium pasteurianum I: Examination of its light sensitivity at cryogenic temperatures. Biochemistry 2002, 41:2036-2043.
    • (2002) Biochemistry , vol.41 , pp. 2036-2043
    • Chen, Z.J.1    Lemon, B.J.2    Huang, S.3    Swartz, D.J.4    Peters, J.W.5    Bagley, K.A.6
  • 147
    • 83055179384 scopus 로고    scopus 로고
    • Mechanistic and physiological implications of the interplay among iron-sulfur clusters in [FeFe]-hydrogenases. A QM/MM perspective
    • Greco C., Bruschi M., Fantucci P., Ryde U., De Gioia L. Mechanistic and physiological implications of the interplay among iron-sulfur clusters in [FeFe]-hydrogenases. A QM/MM perspective. J. Am. Chem. Soc. 2011, 133:18742-18749.
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 18742-18749
    • Greco, C.1    Bruschi, M.2    Fantucci, P.3    Ryde, U.4    De Gioia, L.5
  • 149
    • 29544438599 scopus 로고    scopus 로고
    • The active site of the [FeFe]-hydrogenase from Desulfovibrio desulfuricans. II. Redox properties, light sensitivity and CO-ligand exchange as observed by infrared spectroscopy
    • Roseboom W., De Lacey A.L., Fernandez V.M., Hatchikian E.C., Albracht S.P.J. The active site of the [FeFe]-hydrogenase from Desulfovibrio desulfuricans. II. Redox properties, light sensitivity and CO-ligand exchange as observed by infrared spectroscopy. J. Biol. Inorg. Chem. 2006, 11:102-118.
    • (2006) J. Biol. Inorg. Chem. , vol.11 , pp. 102-118
    • Roseboom, W.1    De Lacey, A.L.2    Fernandez, V.M.3    Hatchikian, E.C.4    Albracht, S.P.J.5
  • 150
    • 84868533696 scopus 로고    scopus 로고
    • Identification and characterization of the "super-reduced" state of the H-cluster in [FeFe] hydrogenase: a New building block for the catalytic cycle?
    • Adamska A., Silakov A., Lambertz C., Rudiger O., Happe T., Reijerse E., Lubitz W. Identification and characterization of the "super-reduced" state of the H-cluster in [FeFe] hydrogenase: a New building block for the catalytic cycle?. Angew. Chem. Int. Ed. 2012, 51:11458-11462.
    • (2012) Angew. Chem. Int. Ed. , vol.51 , pp. 11458-11462
    • Adamska, A.1    Silakov, A.2    Lambertz, C.3    Rudiger, O.4    Happe, T.5    Reijerse, E.6    Lubitz, W.7
  • 151
    • 68949181269 scopus 로고    scopus 로고
    • Structure-function relationships of anaerobic gas-processing metalloenzymes
    • Fontecilla-Camps J.C., Amara P., Cavazza C., Nicolet Y., Volbeda A. Structure-function relationships of anaerobic gas-processing metalloenzymes. Nature 2009, 460:814-822.
    • (2009) Nature , vol.460 , pp. 814-822
    • Fontecilla-Camps, J.C.1    Amara, P.2    Cavazza, C.3    Nicolet, Y.4    Volbeda, A.5
  • 153
    • 69049116388 scopus 로고    scopus 로고
    • Spectroelectrochemical characterization of the active site of the [FeFe] hydrogenase HydA1 from Chlamydomonas reinhardtii
    • Silakov A., Kamp C., Reijerse E., Happe T., Lubitz W. Spectroelectrochemical characterization of the active site of the [FeFe] hydrogenase HydA1 from Chlamydomonas reinhardtii. Biochemistry 2009, 48:7780-7786.
    • (2009) Biochemistry , vol.48 , pp. 7780-7786
    • Silakov, A.1    Kamp, C.2    Reijerse, E.3    Happe, T.4    Lubitz, W.5
  • 155
    • 84893461087 scopus 로고    scopus 로고
    • Electronic and molecular structures of the active-site H-cluster in [FeFe]-hydrogenase determined by site-selective X-ray spectroscopy and quantum chemical calculations
    • Lambertz C., Chernev P., Klingan K., Leidel N., Sigfridsson K.G., Happe T., Haumann M. Electronic and molecular structures of the active-site H-cluster in [FeFe]-hydrogenase determined by site-selective X-ray spectroscopy and quantum chemical calculations. Chem. Sci. 2014, 5:1187-1203.
    • (2014) Chem. Sci. , vol.5 , pp. 1187-1203
    • Lambertz, C.1    Chernev, P.2    Klingan, K.3    Leidel, N.4    Sigfridsson, K.G.5    Happe, T.6    Haumann, M.7
  • 156
    • 35048826863 scopus 로고    scopus 로고
    • [NiFe] and [FeFe] hydrogenases studied by advanced magnetic resonance techniques
    • Lubitz W., Reijerse E., van Gastel M. [NiFe] and [FeFe] hydrogenases studied by advanced magnetic resonance techniques. Chem. Rev. 2007, 107:4331-4365.
    • (2007) Chem. Rev. , vol.107 , pp. 4331-4365
    • Lubitz, W.1    Reijerse, E.2    van Gastel, M.3
  • 158
    • 0021646579 scopus 로고
    • Mössbauer and electron nuclear double resonance study of oxidized bidirectional hydrogenase from Clostridium pasteurianum W5
    • Wang G., Benecky M.J., Huynh B.H., Clin J.F., Adams M.W.W., Mortenson L.E., Hoffman B.M., Münck E. Mössbauer and electron nuclear double resonance study of oxidized bidirectional hydrogenase from Clostridium pasteurianum W5. J. Biol. Chem. 1984, 259(23):14328-14331.
    • (1984) J. Biol. Chem. , vol.259 , Issue.23 , pp. 14328-14331
    • Wang, G.1    Benecky, M.J.2    Huynh, B.H.3    Clin, J.F.4    Adams, M.W.W.5    Mortenson, L.E.6    Hoffman, B.M.7    Münck, E.8
  • 160
    • 0009790182 scopus 로고
    • Desulfovibrio vulgaris hydrogenase: a nonheme iron enzyme lacking nickel that exhibits anomalous EPR and Mössbauer spectra
    • Huynh B.H., Czechowski M.H., Krüger H.J., DerVartanian D.V., Peck H.D., LeGall J. Desulfovibrio vulgaris hydrogenase: a nonheme iron enzyme lacking nickel that exhibits anomalous EPR and Mössbauer spectra. Proc. Natl. Acad. Sci. U. S. A. 1984, 81(12):3728-3732.
    • (1984) Proc. Natl. Acad. Sci. U. S. A. , vol.81 , Issue.12 , pp. 3728-3732
    • Huynh, B.H.1    Czechowski, M.H.2    Krüger, H.J.3    DerVartanian, D.V.4    Peck, H.D.5    LeGall, J.6
  • 163
    • 33845932878 scopus 로고    scopus 로고
    • Electrochemical investigations of the interconversions between catalytic and inhibited states of the [FeFe]-hydrogenase from Desulfovibrio desulfuricans
    • Parkin A., Cavazza C., Fontecilla-Camps J.C., Armstrong F.A. Electrochemical investigations of the interconversions between catalytic and inhibited states of the [FeFe]-hydrogenase from Desulfovibrio desulfuricans. J. Am. Chem. Soc. 2006, 128:16808-16815.
    • (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
  • 165
    • 83655183063 scopus 로고    scopus 로고
    • Combining acid-base, redox and substrate binding functionalities to give a complete model for the [FeFe]-hydrogenase
    • Camara J.M., Rauchfuss T.B. Combining acid-base, redox and substrate binding functionalities to give a complete model for the [FeFe]-hydrogenase. Nat. Chem. 2012, 4:26-30.
    • (2012) Nat. Chem. , vol.4 , pp. 26-30
    • Camara, J.M.1    Rauchfuss, T.B.2
  • 169
    • 0021194792 scopus 로고
    • The physical and catalytic properties of hydrogenase II of Clostridium pasteurianum. A comparison with hydrogenase I
    • Adams M.W., Mortenson L.E. The physical and catalytic properties of hydrogenase II of Clostridium pasteurianum. A comparison with hydrogenase I. J. Biol. Chem. 1984, 259:7045-7055.
    • (1984) J. Biol. Chem. , vol.259 , pp. 7045-7055
    • Adams, M.W.1    Mortenson, L.E.2
  • 170
    • 84863899218 scopus 로고    scopus 로고
    • Electrocatalytic mechanism of reversible hydrogen cycling by enzymes and distinctions between the major classes of hydrogenases
    • Hexter S.V., Grey F., Happe T., Climent V., Armstrong F.A. Electrocatalytic mechanism of reversible hydrogen cycling by enzymes and distinctions between the major classes of hydrogenases. Proc. Natl. Acad. Sci. 2012, 109:11516-11521.
    • (2012) Proc. Natl. Acad. Sci. , vol.109 , pp. 11516-11521
    • Hexter, S.V.1    Grey, F.2    Happe, T.3    Climent, V.4    Armstrong, F.A.5
  • 172
    • 0001030519 scopus 로고
    • Iron-sulfur clusters of hydrogenase I and hydrogenase II of Clostridium pasteurianum
    • Adams M., Eccleston E., Howard J.B. Iron-sulfur clusters of hydrogenase I and hydrogenase II of Clostridium pasteurianum. Proc. Natl. Acad. Sci. 1989, 86:4932.
    • (1989) Proc. Natl. Acad. Sci. , vol.86 , pp. 4932
    • Adams, M.1    Eccleston, E.2    Howard, J.B.3
  • 174
    • 0037386540 scopus 로고    scopus 로고
    • The organometallic active site of [Fe]hydrogenase: Models and entatic states
    • Darensbourg M.Y., Lyon E.J., Zhao X., Georgakaki I.P. The organometallic active site of [Fe]hydrogenase: Models and entatic states. Proc. Natl. Acad. Sci. 2003, 100:3683-3688.
    • (2003) Proc. Natl. Acad. Sci. , vol.100 , pp. 3683-3688
    • Darensbourg, M.Y.1    Lyon, E.J.2    Zhao, X.3    Georgakaki, I.P.4
  • 175
    • 67649283572 scopus 로고    scopus 로고
    • Structural and functional analogues of the active sites of the [Fe]-, [NiFe]-, and [FeFe]-hydrogenases†
    • Tard C., Pickett C.J. Structural and functional analogues of the active sites of the [Fe]-, [NiFe]-, and [FeFe]-hydrogenases†. Chem. Rev. 2009, 109:2245-2274.
    • (2009) Chem. Rev. , vol.109 , pp. 2245-2274
    • Tard, C.1    Pickett, C.J.2
  • 176
    • 84899452023 scopus 로고    scopus 로고
    • Development of molecular electrocatalysts for energy storage
    • DuBois D.L. Development of molecular electrocatalysts for energy storage. Inorg. Chem. 2014, 53:3935-3960.
    • (2014) Inorg. Chem. , vol.53 , pp. 3935-3960
    • DuBois, D.L.1
  • 177
    • 0029901484 scopus 로고    scopus 로고
    • Analysis of the hydA locus of Escherichia coli: two genes (hydN and hypF) involved in formate and hydrogen metabolism
    • Maier T., Binder U., Bock A. Analysis of the hydA locus of Escherichia coli: two genes (hydN and hypF) involved in formate and hydrogen metabolism. Arch. Microbiol. 1996, 165:333-341.
    • (1996) Arch. Microbiol. , vol.165 , pp. 333-341
    • Maier, T.1    Binder, U.2    Bock, A.3
  • 178
    • 0026446645 scopus 로고
    • The hyp operon gene products are required for the maturation of catalytically active hydrogenase isoenzymes in Escherichia coli
    • Jacobi A., Rossmann R., Bock A. The hyp operon gene products are required for the maturation of catalytically active hydrogenase isoenzymes in Escherichia coli. Arch. Microbiol. 1992, 158:444-451.
    • (1992) Arch. Microbiol. , vol.158 , pp. 444-451
    • Jacobi, A.1    Rossmann, R.2    Bock, A.3
  • 179
    • 0025975104 scopus 로고
    • Molecular characterization of an operon (hyp) necessary for the activity of the three hydrogenase isoenzymes in Escherichia coli
    • Lutz S., Jacobi A., Schlensog V., Bohm R., Sawers G., Bock A. Molecular characterization of an operon (hyp) necessary for the activity of the three hydrogenase isoenzymes in Escherichia coli. Mol. Microbiol. 1991, 5:123-135.
    • (1991) Mol. Microbiol. , vol.5 , pp. 123-135
    • Lutz, S.1    Jacobi, A.2    Schlensog, V.3    Bohm, R.4    Sawers, G.5    Bock, A.6
  • 181
    • 4344582395 scopus 로고    scopus 로고
    • Analysis of the transcarbamoylation-dehydration reaction catalyzed by the hydrogenase maturation proteins HypF and HypE
    • Blokesch M., Paschos A., Bauer A., Reissmann S., Drapal N., Bock A. Analysis of the transcarbamoylation-dehydration reaction catalyzed by the hydrogenase maturation proteins HypF and HypE. Eur. J. Biochem. 2004, 271:3428-3436.
    • (2004) Eur. J. Biochem. , vol.271 , pp. 3428-3436
    • Blokesch, M.1    Paschos, A.2    Bauer, A.3    Reissmann, S.4    Drapal, N.5    Bock, A.6
  • 182
    • 84865239562 scopus 로고    scopus 로고
    • Structural basis for the reaction mechanism of S-carbamoylation of HypE by HypF in the maturation of [NiFe]-hydrogenases
    • Shomura Y., Higuchi Y. Structural basis for the reaction mechanism of S-carbamoylation of HypE by HypF in the maturation of [NiFe]-hydrogenases. J. Biol. Chem. 2012, 287:28409-28419.
    • (2012) J. Biol. Chem. , vol.287 , pp. 28409-28419
    • Shomura, Y.1    Higuchi, Y.2
  • 185
    • 51049107924 scopus 로고    scopus 로고
    • Structure of the archaeal Kae1/Bud32 fusion protein MJ1130: a model for the eukaryotic EKC/KEOPS subcomplex
    • Hecker A., Lopreiato R., Graille M., Collinet B., Forterre P., Libri D., van Tilbeurgh H. Structure of the archaeal Kae1/Bud32 fusion protein MJ1130: a model for the eukaryotic EKC/KEOPS subcomplex. EMBO J. 2008, 27:2340-2351.
    • (2008) EMBO J. , vol.27 , pp. 2340-2351
    • Hecker, A.1    Lopreiato, R.2    Graille, M.3    Collinet, B.4    Forterre, P.5    Libri, D.6    van Tilbeurgh, H.7
  • 187
    • 0001007592 scopus 로고    scopus 로고
    • X-ray crystal structure of aminoimidazole ribonucleotide synthetase (PurM), from the Escherichia coli purine biosynthetic pathway at 2.5 A resolution
    • Li C., Kappock T.J., Stubbe J., Weaver T.M., Ealick S.E. X-ray crystal structure of aminoimidazole ribonucleotide synthetase (PurM), from the Escherichia coli purine biosynthetic pathway at 2.5 A resolution. Structure 1999, 7:1155-1166.
    • (1999) Structure , vol.7 , pp. 1155-1166
    • Li, C.1    Kappock, T.J.2    Stubbe, J.3    Weaver, T.M.4    Ealick, S.E.5
  • 188
    • 4043055054 scopus 로고    scopus 로고
    • Domain organization of Salmonella typhimurium formylglycinamide ribonucleotide amidotransferase revealed by X-ray crystallography
    • Anand R., Hoskins A.A., Stubbe J., Ealick S.E. Domain organization of Salmonella typhimurium formylglycinamide ribonucleotide amidotransferase revealed by X-ray crystallography. Biochemistry 2004, 43:10328-10342.
    • (2004) Biochemistry , vol.43 , pp. 10328-10342
    • Anand, R.1    Hoskins, A.A.2    Stubbe, J.3    Ealick, S.E.4
  • 190
    • 84890820987 scopus 로고    scopus 로고
    • Crystal structures of the carbamoylated and cyanated forms of HypE for [NiFe] hydrogenase maturation
    • Tominaga T., Watanabe S., Matsumi R., Atomi H., Imanaka T., Miki K. Crystal structures of the carbamoylated and cyanated forms of HypE for [NiFe] hydrogenase maturation. Proc. Natl. Acad. Sci. U. S. A. 2013, 110:20485-20490.
    • (2013) Proc. Natl. Acad. Sci. U. S. A. , vol.110 , pp. 20485-20490
    • Tominaga, T.1    Watanabe, S.2    Matsumi, R.3    Atomi, H.4    Imanaka, T.5    Miki, K.6
  • 191
    • 84939939183 scopus 로고    scopus 로고
    • [NiFe]-hydrogenase cofactor assembly
    • John Wiley & Sons, Chichester, U.K. V. Culotta, R.A. Scott (Eds.)
    • Soboh B., Sawers R.G. [NiFe]-hydrogenase cofactor assembly. Encylopedia of inorganic and bioinorganic chemistry 2013, 1-9. John Wiley & Sons, Chichester, U.K. V. Culotta, R.A. Scott (Eds.).
    • (2013) Encylopedia of inorganic and bioinorganic chemistry , pp. 1-9
    • Soboh, B.1    Sawers, R.G.2
  • 192
    • 0345647107 scopus 로고    scopus 로고
    • Interaction of the hydrogenase accessory protein HypC with HycE, the large subunit of Escherichia coli hydrogenase 3 during enzyme maturation
    • Drapal N., Bock A. Interaction of the hydrogenase accessory protein HypC with HycE, the large subunit of Escherichia coli hydrogenase 3 during enzyme maturation. Biochemistry 1998, 37:2941-2948.
    • (1998) Biochemistry , vol.37 , pp. 2941-2948
    • Drapal, N.1    Bock, A.2
  • 193
    • 0036440688 scopus 로고    scopus 로고
    • Maturation of [NiFe]-hydrogenases in Escherichia coli: the HypC cycle
    • Blokesch M., Bock A. Maturation of [NiFe]-hydrogenases in Escherichia coli: the HypC cycle. J. Mol. Biol. 2002, 324:287-296.
    • (2002) J. Mol. Biol. , vol.324 , pp. 287-296
    • Blokesch, M.1    Bock, A.2
  • 194
    • 7044222771 scopus 로고    scopus 로고
    • The complex between hydrogenase-maturation proteins HypC and HypD is an intermediate in the supply of cyanide to the active site iron of [NiFe]-hydrogenases
    • Blokesch M., Albracht S.P., Matzanke B.F., Drapal N.M., Jacobi A., Bock A. The complex between hydrogenase-maturation proteins HypC and HypD is an intermediate in the supply of cyanide to the active site iron of [NiFe]-hydrogenases. J. Mol. Biol. 2004, 344:155-167.
    • (2004) J. Mol. Biol. , vol.344 , pp. 155-167
    • Blokesch, M.1    Albracht, S.P.2    Matzanke, B.F.3    Drapal, N.M.4    Jacobi, A.5    Bock, A.6
  • 196
    • 84870548822 scopus 로고    scopus 로고
    • Crystal structures of the HypCD complex and the HypCDE ternary complex: transient intermediate complexes during [NiFe] hydrogenase maturation
    • Watanabe S., Matsumi R., Atomi H., Imanaka T., Miki K. Crystal structures of the HypCD complex and the HypCDE ternary complex: transient intermediate complexes during [NiFe] hydrogenase maturation. Structure 2012, 20:2124-2137.
    • (2012) Structure , vol.20 , pp. 2124-2137
    • Watanabe, S.1    Matsumi, R.2    Atomi, H.3    Imanaka, T.4    Miki, K.5
  • 198
  • 199
    • 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
  • 200
    • 33745867578 scopus 로고    scopus 로고
    • Properties of the [NiFe]-hydrogenase maturation protein HypD
    • Blokesch M., Bock A. Properties of the [NiFe]-hydrogenase maturation protein HypD. FEBS Lett. 2006, 580:4065-4068.
    • (2006) FEBS Lett. , vol.580 , pp. 4065-4068
    • Blokesch, M.1    Bock, A.2
  • 201
    • 84869456872 scopus 로고    scopus 로고
    • Structural basis of [NiFe] hydrogenase maturation by Hyp proteins
    • Watanabe S., Sasaki D., Tominaga T., Miki K. Structural basis of [NiFe] hydrogenase maturation by Hyp proteins. Biol. Chem. 2012, 393:1089-1100.
    • (2012) Biol. Chem. , vol.393 , pp. 1089-1100
    • Watanabe, S.1    Sasaki, D.2    Tominaga, T.3    Miki, K.4
  • 204
    • 11844252075 scopus 로고    scopus 로고
    • The biosynthetic routes for carbon monoxide and cyanide in the Ni-Fe active site of hydrogenases are different
    • Roseboom W., Blokesch M., Bock A., Albracht S.P. The biosynthetic routes for carbon monoxide and cyanide in the Ni-Fe active site of hydrogenases are different. FEBS Lett. 2005, 579:469-472.
    • (2005) FEBS Lett. , vol.579 , pp. 469-472
    • Roseboom, W.1    Blokesch, M.2    Bock, A.3    Albracht, S.P.4
  • 205
    • 0022632813 scopus 로고
    • Pleiotropic hydrogenase mutants of Escherichia coli K12: growth in the presence of nickel can restore hydrogenase activity
    • Waugh R., Boxer D.H. Pleiotropic hydrogenase mutants of Escherichia coli K12: growth in the presence of nickel can restore hydrogenase activity. Biochimie 1986, 68:157-166.
    • (1986) Biochimie , vol.68 , pp. 157-166
    • Waugh, R.1    Boxer, D.H.2
  • 206
    • 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
  • 207
    • 34248681266 scopus 로고    scopus 로고
    • Maturation of [NiFe]-hydrogenases in Escherichia coli
    • Forzi L., Sawers R.G. Maturation of [NiFe]-hydrogenases in Escherichia coli. Biometals 2007, 20:565-578.
    • (2007) Biometals , vol.20 , pp. 565-578
    • Forzi, L.1    Sawers, R.G.2
  • 208
    • 70350728386 scopus 로고    scopus 로고
    • Crystal structure of HypA, a nickel-binding metallochaperone for [NiFe] hydrogenase maturation
    • Watanabe S., Arai T., Matsumi R., Atomi H., Imanaka T., Miki K. Crystal structure of HypA, a nickel-binding metallochaperone for [NiFe] hydrogenase maturation. J. Mol. Biol. 2009, 394:448-459.
    • (2009) J. Mol. Biol. , vol.394 , pp. 448-459
    • Watanabe, S.1    Arai, T.2    Matsumi, R.3    Atomi, H.4    Imanaka, T.5    Miki, K.6
  • 209
    • 0037307747 scopus 로고    scopus 로고
    • Characterization of Helicobacter pylori nickel metabolism accessory proteins needed for maturation of both urease and hydrogenase
    • Mehta N., Olson J.W., Maier R.J. Characterization of Helicobacter pylori nickel metabolism accessory proteins needed for maturation of both urease and hydrogenase. J. Bacteriol. 2003, 185:726-734.
    • (2003) J. Bacteriol. , vol.185 , pp. 726-734
    • Mehta, N.1    Olson, J.W.2    Maier, R.J.3
  • 210
    • 1942539935 scopus 로고    scopus 로고
    • HybF, a zinc-containing protein involved in NiFe hydrogenase maturation
    • Blokesch M., Rohrmoser M., Rode S., Bock A. HybF, a zinc-containing protein involved in NiFe hydrogenase maturation. J. Bacteriol. 2004, 186:2603-2611.
    • (2004) J. Bacteriol. , vol.186 , pp. 2603-2611
    • Blokesch, M.1    Rohrmoser, M.2    Rode, S.3    Bock, A.4
  • 211
    • 0029054222 scopus 로고
    • GTP hydrolysis by HypB is essential for nickel insertion into hydrogenases of Escherichia coli
    • Maier T., Lottspeich F., Bock A. GTP hydrolysis by HypB is essential for nickel insertion into hydrogenases of Escherichia coli. Eur. J. Biochem. 1995, 230:133-138.
    • (1995) Eur. J. Biochem. , vol.230 , pp. 133-138
    • Maier, T.1    Lottspeich, F.2    Bock, A.3
  • 212
    • 0141681866 scopus 로고    scopus 로고
    • Roles of conserved nucleotide-binding domains in accessory proteins, HypB and UreG, in the maturation of nickel-enzymes required for efficient Helicobacter pylori colonization
    • Mehta N., Benoit S., Maier R.J. Roles of conserved nucleotide-binding domains in accessory proteins, HypB and UreG, in the maturation of nickel-enzymes required for efficient Helicobacter pylori colonization. Microb. Pathog. 2003, 35:229-234.
    • (2003) Microb. Pathog. , vol.35 , pp. 229-234
    • Mehta, N.1    Benoit, S.2    Maier, R.J.3
  • 213
    • 24644474525 scopus 로고    scopus 로고
    • Metal binding activity of the Escherichia coli hydrogenase maturation factor HypB
    • Leach M.R., Sandal S., Sun H., Zamble D.B. Metal binding activity of the Escherichia coli hydrogenase maturation factor HypB. Biochemistry 2005, 44:12229-12238.
    • (2005) Biochemistry , vol.44 , pp. 12229-12238
    • Leach, M.R.1    Sandal, S.2    Sun, H.3    Zamble, D.B.4
  • 214
    • 33748749374 scopus 로고    scopus 로고
    • Structural insights into HypB, a GTP-binding protein that regulates metal binding
    • Gasper R., Scrima A., Wittinghofer A. Structural insights into HypB, a GTP-binding protein that regulates metal binding. J. Biol. Chem. 2006, 281:27492-27502.
    • (2006) J. Biol. Chem. , vol.281 , pp. 27492-27502
    • Gasper, R.1    Scrima, A.2    Wittinghofer, A.3
  • 216
    • 79952385857 scopus 로고    scopus 로고
    • Effects of metal on the biochemical properties of Helicobacter pylori HypB, a maturation factor of [NiFe]-hydrogenase and urease
    • Sydor A.M., Liu J., Zamble D.B. Effects of metal on the biochemical properties of Helicobacter pylori HypB, a maturation factor of [NiFe]-hydrogenase and urease. J. Bacteriol. 2011, 193:1359-1368.
    • (2011) J. Bacteriol. , vol.193 , pp. 1359-1368
    • Sydor, A.M.1    Liu, J.2    Zamble, D.B.3
  • 217
    • 84894203851 scopus 로고    scopus 로고
    • Relationship between Ni(II) and Zn(II) coordination and nucleotide binding by the Helicobacter pylori [NiFe]-hydrogenase and urease maturation factor HypB
    • Sydor A.M., Lebrette H., Ariyakumaran R., Cavazza C., Zamble D.B. Relationship between Ni(II) and Zn(II) coordination and nucleotide binding by the Helicobacter pylori [NiFe]-hydrogenase and urease maturation factor HypB. J. Biol. Chem. 2014, 289:3828-3841.
    • (2014) J. Biol. Chem. , vol.289 , pp. 3828-3841
    • Sydor, A.M.1    Lebrette, H.2    Ariyakumaran, R.3    Cavazza, C.4    Zamble, D.B.5
  • 218
    • 80051546547 scopus 로고    scopus 로고
    • Relationship between the GTPase, metal-binding, and dimerization activities of E. coli HypB
    • Cai F., Ngu T.T., Kaluarachchi H., Zamble D.B. Relationship between the GTPase, metal-binding, and dimerization activities of E. coli HypB. J. Biol. Inorg. Chem. 2011, 16:857-868.
    • (2011) J. Biol. Inorg. Chem. , vol.16 , pp. 857-868
    • Cai, F.1    Ngu, T.T.2    Kaluarachchi, H.3    Zamble, D.B.4
  • 219
    • 83355169703 scopus 로고    scopus 로고
    • Protein interactions and localization of the Escherichia coli accessory protein HypA during nickel insertion to [NiFe] hydrogenase
    • Chan Chung K.C., Zamble D.B. Protein interactions and localization of the Escherichia coli accessory protein HypA during nickel insertion to [NiFe] hydrogenase. J. Biol. Chem. 2011, 286:43081-43090.
    • (2011) J. Biol. Chem. , vol.286 , pp. 43081-43090
    • Chan Chung, K.C.1    Zamble, D.B.2
  • 220
    • 84863149329 scopus 로고    scopus 로고
    • Metallo-GTPase HypB from Helicobacter pylori and its interaction with nickel chaperone protein HypA
    • Xia W., Li H., Yang X., Wong K.B., Sun H. Metallo-GTPase HypB from Helicobacter pylori and its interaction with nickel chaperone protein HypA. J. Biol. Chem. 2012, 287:6753-6763.
    • (2012) J. Biol. Chem. , vol.287 , pp. 6753-6763
    • Xia, W.1    Li, H.2    Yang, X.3    Wong, K.B.4    Sun, H.5
  • 221
    • 34447518542 scopus 로고    scopus 로고
    • The role of complex formation between the Escherichia coli hydrogenase accessory factors HypB and SlyD
    • Leach M.R., Zhang J.W., Zamble D.B. The role of complex formation between the Escherichia coli hydrogenase accessory factors HypB and SlyD. J. Biol. Chem. 2007, 282:16177-16186.
    • (2007) J. Biol. Chem. , vol.282 , pp. 16177-16186
    • Leach, M.R.1    Zhang, J.W.2    Zamble, D.B.3
  • 223
    • 15744391209 scopus 로고    scopus 로고
    • A role for SlyD in the Escherichia coli hydrogenase biosynthetic pathway
    • Zhang J.W., Butland G., Greenblatt J.F., Emili A., Zamble D.B. A role for SlyD in the Escherichia coli hydrogenase biosynthetic pathway. J. Biol. Chem. 2005, 280:4360-4366.
    • (2005) J. Biol. Chem. , vol.280 , pp. 4360-4366
    • Zhang, J.W.1    Butland, G.2    Greenblatt, J.F.3    Emili, A.4    Zamble, D.B.5
  • 224
    • 84879853015 scopus 로고    scopus 로고
    • Interaction of SlyD with HypB of Helicobacter pylori facilitates nickel trafficking
    • Cheng T., Li H., Yang X., Xia W., Sun H. Interaction of SlyD with HypB of Helicobacter pylori facilitates nickel trafficking. Metallomics 2013, 5:804-807.
    • (2013) Metallomics , vol.5 , pp. 804-807
    • Cheng, T.1    Li, H.2    Yang, X.3    Xia, W.4    Sun, H.5
  • 225
    • 84883466577 scopus 로고    scopus 로고
    • Metal transfer within the Escherichia coli HypB-HypA complex of hydrogenase accessory proteins
    • Douglas C.D., Ngu T.T., Kaluarachchi H., Zamble D.B. Metal transfer within the Escherichia coli HypB-HypA complex of hydrogenase accessory proteins. Biochemistry 2013, 52:6030-6039.
    • (2013) Biochemistry , vol.52 , pp. 6030-6039
    • Douglas, C.D.1    Ngu, T.T.2    Kaluarachchi, H.3    Zamble, D.B.4
  • 226
    • 83455221556 scopus 로고    scopus 로고
    • Escherichia coli SlyD, more than a Ni(II) reservoir
    • Kaluarachchi H., Zhang J.W., Zamble D.B. Escherichia coli SlyD, more than a Ni(II) reservoir. Biochemistry 2011, 50:10761-10763.
    • (2011) Biochemistry , vol.50 , pp. 10761-10763
    • Kaluarachchi, H.1    Zhang, J.W.2    Zamble, D.B.3
  • 227
    • 14644401765 scopus 로고    scopus 로고
    • [NiFe]-Hydrogenase maturation endopeptidase: structure and function
    • Theodoratou E., Huber R., Bock A. [NiFe]-Hydrogenase maturation endopeptidase: structure and function. Biochem. Soc. Trans. 2005, 33:108-111.
    • (2005) Biochem. Soc. Trans. , vol.33 , pp. 108-111
    • Theodoratou, E.1    Huber, R.2    Bock, A.3
  • 228
    • 0028832110 scopus 로고
    • Characterisation of a protease from Escherichia coli involved in hydrogenase maturation
    • Rossmann R., Maier T., Lottspeich F., Bock A. Characterisation of a protease from Escherichia coli involved in hydrogenase maturation. Eur. J. Biochem. 1995, 227:545-550.
    • (1995) Eur. J. Biochem. , vol.227 , pp. 545-550
    • Rossmann, R.1    Maier, T.2    Lottspeich, F.3    Bock, A.4
  • 229
    • 0026714545 scopus 로고
    • Carboxyl-terminal processing may be essential for production of active NiFe hydrogenase in Azotobacter vinelandii
    • Gollin D.J., Mortenson L.E., Robson R.L. Carboxyl-terminal processing may be essential for production of active NiFe hydrogenase in Azotobacter vinelandii. FEBS Lett. 1992, 309:371-375.
    • (1992) FEBS Lett. , vol.309 , pp. 371-375
    • Gollin, D.J.1    Mortenson, L.E.2    Robson, R.L.3
  • 230
    • 0027233609 scopus 로고
    • A novel very small subunit of a selenium containing [NiFe] hydrogenase of Methanococcus voltae is postranslationally processed by cleavage at a defined position
    • Sorgenfrei O., Linder D., Karas M., Klein A. A novel very small subunit of a selenium containing [NiFe] hydrogenase of Methanococcus voltae is postranslationally processed by cleavage at a defined position. Eur. J. Biochem. 1993, 213:1355-1358.
    • (1993) Eur. J. Biochem. , vol.213 , pp. 1355-1358
    • Sorgenfrei, O.1    Linder, D.2    Karas, M.3    Klein, A.4
  • 232
    • 0028314544 scopus 로고
    • Maturation of the large subunit (HYCE) of Escherichia coli hydrogenase 3 requires nickel incorporation followed by C-terminal processing at Arg537
    • Rossmann R., Sauter M., Lottspeich F., Bock A. Maturation of the large subunit (HYCE) of Escherichia coli hydrogenase 3 requires nickel incorporation followed by C-terminal processing at Arg537. Eur. J. Biochem. 1994, 220:377-384.
    • (1994) Eur. J. Biochem. , vol.220 , pp. 377-384
    • Rossmann, R.1    Sauter, M.2    Lottspeich, F.3    Bock, A.4
  • 233
    • 0034031960 scopus 로고    scopus 로고
    • Nickel serves as a substrate recognition motif for the endopeptidase involved in hydrogenase maturation
    • Theodoratou E., Paschos A., Magalon A., Fritsche E., Huber R., Bock A. Nickel serves as a substrate recognition motif for the endopeptidase involved in hydrogenase maturation. Eur. J. Biochem. 2000, 267:1995-1999.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 1995-1999
    • Theodoratou, E.1    Paschos, A.2    Magalon, A.3    Fritsche, E.4    Huber, R.5    Bock, A.6
  • 235
    • 33644850541 scopus 로고    scopus 로고
    • Functional studies of [FeFe] hydrogenase maturation in an Escherichia coli biosynthetic system
    • King P.W., Posewitz M.C., Ghirardi M.L., Seibert M. Functional studies of [FeFe] hydrogenase maturation in an Escherichia coli biosynthetic system. J. Bacteriol. 2006, 188:2163-2172.
    • (2006) J. Bacteriol. , vol.188 , pp. 2163-2172
    • King, P.W.1    Posewitz, M.C.2    Ghirardi, M.L.3    Seibert, M.4
  • 236
    • 24144494192 scopus 로고    scopus 로고
    • Biochemical characterization of the HydE and HydG iron-only hydrogenase maturation enzymes from Thermatoga maritima
    • Rubach J.K., Brazzolotto X., Gaillard J., Fontecave M. Biochemical characterization of the HydE and HydG iron-only hydrogenase maturation enzymes from Thermatoga maritima. FEBS Lett. 2005, 579:5055-5060.
    • (2005) FEBS Lett. , vol.579 , pp. 5055-5060
    • Rubach, J.K.1    Brazzolotto, X.2    Gaillard, J.3    Fontecave, M.4
  • 237
    • 33644852344 scopus 로고    scopus 로고
    • The [Fe-Fe]-hydrogenase maturation protein HydF from Thermotoga maritima is a GTPase with an iron-sulfur cluster
    • Brazzolotto X., Rubach J.K., Gaillard J., Gambarelli S., Atta M., Fontecave M. The [Fe-Fe]-hydrogenase maturation protein HydF from Thermotoga maritima is a GTPase with an iron-sulfur cluster. J. Biol. Chem. 2006, 281:769-774.
    • (2006) J. Biol. Chem. , vol.281 , pp. 769-774
    • Brazzolotto, X.1    Rubach, J.K.2    Gaillard, J.3    Gambarelli, S.4    Atta, M.5    Fontecave, M.6
  • 239
    • 84873334687 scopus 로고    scopus 로고
    • Nuclear resonance vibrational spectroscopy and electron paramagnetic resonance spectroscopy of 57Fe-enriched [FeFe] hydrogenase indicate stepwise assembly of the H-cluster
    • Kuchenreuther J.M., Guo Y., Wang H., Myers W.K., George S.J., Boyke C.A., Yoda Y., Alp E.E., Zhao J., Britt R.D., Swartz J.R., Cramer S.P. Nuclear resonance vibrational spectroscopy and electron paramagnetic resonance spectroscopy of 57Fe-enriched [FeFe] hydrogenase indicate stepwise assembly of the H-cluster. Biochemistry 2013, 52:818-826.
    • (2013) Biochemistry , vol.52 , pp. 818-826
    • Kuchenreuther, J.M.1    Guo, Y.2    Wang, H.3    Myers, W.K.4    George, S.J.5    Boyke, C.A.6    Yoda, Y.7    Alp, E.E.8    Zhao, J.9    Britt, R.D.10    Swartz, J.R.11    Cramer, S.P.12
  • 240
    • 84861881676 scopus 로고    scopus 로고
    • Emerging paradigms for complex iron-sulfur cofactor assembly and insertion
    • Peters J.W., Broderick J.B. Emerging paradigms for complex iron-sulfur cofactor assembly and insertion. Annu. Rev. Biochem. 2012, 81:429-450.
    • (2012) Annu. Rev. Biochem. , vol.81 , pp. 429-450
    • Peters, J.W.1    Broderick, J.B.2
  • 244
    • 74249099497 scopus 로고    scopus 로고
    • The [FeFe]-hydrogenase maturase HydF from Clostridium acetobutylicum contains a CO and CN- ligated iron cofactor
    • Czech I., Silakov A., Lubitz W., Happe T. The [FeFe]-hydrogenase maturase HydF from Clostridium acetobutylicum contains a CO and CN- ligated iron cofactor. FEBS Lett. 2010, 584:638-642.
    • (2010) FEBS Lett. , vol.584 , pp. 638-642
    • Czech, I.1    Silakov, A.2    Lubitz, W.3    Happe, T.4
  • 245
    • 78650856177 scopus 로고    scopus 로고
    • The [FeFe]-hydrogenase maturation protein HydF contains a H-cluster like [4Fe4S]-2Fe site
    • Czech I., Stripp S., Sanganas O., Leidel N., Happe T., Haumann M. The [FeFe]-hydrogenase maturation protein HydF contains a H-cluster like [4Fe4S]-2Fe site. FEBS Lett. 2011, 585:225-230.
    • (2011) FEBS Lett. , vol.585 , pp. 225-230
    • Czech, I.1    Stripp, S.2    Sanganas, O.3    Leidel, N.4    Happe, T.5    Haumann, M.6
  • 246
    • 84868534275 scopus 로고    scopus 로고
    • Iron-sulfur cluster coordination in the [FeFe]-hydrogenase H cluster biosynthetic factor HydF
    • Joshi N., Shepard E.M., Byer A.S., Swanson K.D., Broderick J.B., Peters J.W. Iron-sulfur cluster coordination in the [FeFe]-hydrogenase H cluster biosynthetic factor HydF. FEBS Lett. 2012, 586:3939-3943.
    • (2012) FEBS Lett. , vol.586 , pp. 3939-3943
    • Joshi, N.1    Shepard, E.M.2    Byer, A.S.3    Swanson, K.D.4    Broderick, J.B.5    Peters, J.W.6
  • 247
    • 84866658489 scopus 로고    scopus 로고
    • New insights into [FeFe] hydrogenase activation and maturase function
    • Kuchenreuther J.M., Britt R.D., Swartz J.R. New insights into [FeFe] hydrogenase activation and maturase function. PLoS One 2012, 7:e45850.
    • (2012) PLoS One , vol.7 , pp. e45850
    • Kuchenreuther, J.M.1    Britt, R.D.2    Swartz, J.R.3
  • 252
    • 84867753153 scopus 로고    scopus 로고
    • Biochemical analysis of the interactions between the proteins involved in the [FeFe]-hydrogenase maturation process
    • Vallese F., Berto P., Ruzzene M., Cendron L., Sarno S., De Rosa E., Giacometti G.M., Costantini P. Biochemical analysis of the interactions between the proteins involved in the [FeFe]-hydrogenase maturation process. J. Biol. Chem. 2012, 287:36544-36555.
    • (2012) J. Biol. Chem. , vol.287 , pp. 36544-36555
    • Vallese, F.1    Berto, P.2    Ruzzene, M.3    Cendron, L.4    Sarno, S.5    De Rosa, E.6    Giacometti, G.M.7    Costantini, P.8
  • 254
    • 37349127348 scopus 로고    scopus 로고
    • Thiamine biosynthesis in Escherichia coli: identification of the intermediate and by-product derived from tyrosine
    • Kriek M., Martins F., Challand M.R., Croft A., Roach P.L. Thiamine biosynthesis in Escherichia coli: identification of the intermediate and by-product derived from tyrosine. Angew. Chem. Int. Ed. Engl. 2007, 46:9223-9226.
    • (2007) Angew. Chem. Int. Ed. Engl. , vol.46 , pp. 9223-9226
    • Kriek, M.1    Martins, F.2    Challand, M.R.3    Croft, A.4    Roach, P.L.5
  • 257
    • 77957134413 scopus 로고    scopus 로고
    • A glycyl free radical as the precursor in the synthesis of carbon monoxide and cyanide by the [FeFe]-hydrogenase maturase HydG
    • Nicolet Y., Martin L., Tron C., Fontecilla-Camps J.C. A glycyl free radical as the precursor in the synthesis of carbon monoxide and cyanide by the [FeFe]-hydrogenase maturase HydG. FEBS Lett. 2010, 584:4197-4202.
    • (2010) FEBS Lett. , vol.584 , pp. 4197-4202
    • Nicolet, Y.1    Martin, L.2    Tron, C.3    Fontecilla-Camps, J.C.4
  • 261
    • 79957854262 scopus 로고    scopus 로고
    • Cell-free H-cluster synthesis and [FeFe] hydrogenase activation: all five CO and CN ligands derive from tyrosine
    • Kuchenreuther J.M., George S.J., Grady-Smith C.S., Cramer S.P., Swartz J.R. Cell-free H-cluster synthesis and [FeFe] hydrogenase activation: all five CO and CN ligands derive from tyrosine. PLoS One 2011, 6:e20346.
    • (2011) PLoS One , vol.6 , pp. e20346
    • Kuchenreuther, J.M.1    George, S.J.2    Grady-Smith, C.S.3    Cramer, S.P.4    Swartz, J.R.5
  • 262
    • 84856471938 scopus 로고    scopus 로고
    • Crystal structure of methylornithine synthase (PylB): insights into the pyrrolysine biosynthesis
    • Quitterer F., List A., Eisenreich W., Bacher A., Groll M. Crystal structure of methylornithine synthase (PylB): insights into the pyrrolysine biosynthesis. Angew. Chem. Int. Ed. Engl. 2012, 51:1339-1342.
    • (2012) Angew. Chem. Int. Ed. Engl. , vol.51 , pp. 1339-1342
    • Quitterer, F.1    List, A.2    Eisenreich, W.3    Bacher, A.4    Groll, M.5
  • 265
    • 84876931201 scopus 로고    scopus 로고
    • X-ray snapshots of possible intermediates in the time course of synthesis and degradation of protein-bound Fe4S4 clusters
    • Nicolet Y., Rohac R., Martin L., Fontecilla-Camps J.C. X-ray snapshots of possible intermediates in the time course of synthesis and degradation of protein-bound Fe4S4 clusters. Proc. Natl. Acad. Sci. U. S. A. 2013, 110:7188-7192.
    • (2013) Proc. Natl. Acad. Sci. U. S. A. , vol.110 , pp. 7188-7192
    • Nicolet, Y.1    Rohac, R.2    Martin, L.3    Fontecilla-Camps, J.C.4


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