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Volumn 40, Issue 15, 2015, Pages 5081-5091

Introducing polyethyleneimine (PEI) into the electrospun fibrous membranes containing diiron mimics of [FeFe]-hydrogenase: Membrane electrodes and their electrocatalysis on proton reduction in aqueous media

Author keywords

Electrocatalysis; Electrospun fibre; Hydrogen evolution; Membrane electrode; Fe Fe hydrogenase

Indexed keywords

CATALYSIS; CELLULOSE; ELECTROCATALYSIS; ELECTROCHEMICAL ELECTRODES; ELECTRODES; ELECTROSPINNING; GRAPHENE; IRON COMPOUNDS; MEMBRANES; PROTON TRANSFER; REDUCTION; SPINNING (FIBERS);

EID: 85014825293     PISSN: 03603199     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ijhydene.2015.02.050     Document Type: Article
Times cited : (21)

References (54)
  • 2
    • 0032483966 scopus 로고    scopus 로고
    • X-ray crystal structure of the Fe-only hydrogenase (Cpl) from Clostridium pasteurianum to 1.8 angstrom resolution
    • [2] Peters, J.W., Lanzilotta, W.N., Lemon, B.J., Seefeldt, L.C., X-ray crystal structure of the Fe-only hydrogenase (Cpl) from Clostridium pasteurianum to 1.8 angstrom resolution. Science 282 (1998), 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
  • 3
    • 77952428962 scopus 로고    scopus 로고
    • Stepwise FeFe -hydrogenase H-cluster assembly revealed in the structure of HydA(Delta EFG)
    • [3] Mulder, D.W., Boyd, E.S., Sarma, R., Lange, R.K., Endrizzi, J.A., Broderick, J.B., et al. Stepwise FeFe -hydrogenase H-cluster assembly revealed in the structure of HydA(Delta EFG). Nature 465 (2010), 248–251.
    • (2010) Nature , vol.465 , pp. 248-251
    • Mulder, D.W.1    Boyd, E.S.2    Sarma, R.3    Lange, R.K.4    Endrizzi, J.A.5    Broderick, J.B.6
  • 4
    • 77957264750 scopus 로고    scopus 로고
    • Maturation of [FeFe]-hydrogenases: structures and mechanisms
    • [4] Nicolet, Y., Fontecilla-Camps, J.C., Fontecave, M., Maturation of [FeFe]-hydrogenases: structures and mechanisms. Int J Hydrogen Energy 35 (2010), 10750–10760.
    • (2010) Int J Hydrogen Energy , vol.35 , pp. 10750-10760
    • Nicolet, Y.1    Fontecilla-Camps, J.C.2    Fontecave, M.3
  • 5
    • 23644455996 scopus 로고    scopus 로고
    • Iron-only hydrogenase: synthetic, structural and reactivity studies of model compounds
    • [5] Liu, X.M., Ibrahim, S.K., Tard, C., Pickett, C.J., Iron-only hydrogenase: synthetic, structural and reactivity studies of model compounds. Coord Chem Rev 249 (2005), 1641–1652.
    • (2005) Coord Chem Rev , vol.249 , pp. 1641-1652
    • Liu, X.M.1    Ibrahim, S.K.2    Tard, C.3    Pickett, C.J.4
  • 6
    • 12444272776 scopus 로고    scopus 로고
    • 6 and related species
    • [6] Song, L.C., Investigations on butterfly Fe/S cluster S-centered anions (μ-S-)2Fe2(CO)6, (μ-S)(μ-RS)Fe2(CO)6 and related species. Acc Chem Res 38 (2005), 21–28.
    • (2005) Acc Chem Res , vol.38 , pp. 21-28
    • Song, L.C.1
  • 7
    • 23644434830 scopus 로고    scopus 로고
    • Iron hydrogenase active site mimics in supramolecular systems aiming for light-driven hydrogen production
    • [7] Sun, L.C., Akermark, B., Ott, S., Iron hydrogenase active site mimics in supramolecular systems aiming for light-driven hydrogen production. Coord Chem Rev 249 (2005), 1653–1663.
    • (2005) Coord Chem Rev , vol.249 , pp. 1653-1663
    • Sun, L.C.1    Akermark, B.2    Ott, S.3
  • 8
    • 35748933836 scopus 로고    scopus 로고
    • Investigating and exploiting the electrocatalytic properties of hydrogenases
    • [8] Vincent, K.A., Parkin, A., Armstrong, F.A., Investigating and exploiting the electrocatalytic properties of hydrogenases. Chem Rev 107 (2007), 4366–4413.
    • (2007) Chem Rev , vol.107 , pp. 4366-4413
    • Vincent, K.A.1    Parkin, A.2    Armstrong, F.A.3
  • 9
    • 61549134543 scopus 로고    scopus 로고
    • Electron and proton transfers at diiron dithiolate sites relevant to the catalysis of proton reduction by the FeFe -hydrogenases
    • [9] Capon, J.F., Gloaguen, F., Petillon, F.Y., Schollhammer, P., Talarmin, J., Electron and proton transfers at diiron dithiolate sites relevant to the catalysis of proton reduction by the FeFe -hydrogenases. Coord Chem Rev 253 (2009), 1476–1494.
    • (2009) Coord Chem Rev , vol.253 , pp. 1476-1494
    • Capon, J.F.1    Gloaguen, F.2    Petillon, F.Y.3    Schollhammer, P.4    Talarmin, J.5
  • 10
    • 67650085455 scopus 로고    scopus 로고
    • 2 core characteristic of FeFe -hydrogenases including catalysis by these complexes of the reduction of acids to form dihydrogen
    • [10] Felton, G.A.N., Mebi, C.A., Petro, B.J., Vannucci, A.K., Evans, D.H., Glass, R.S., et al. Review of electrochemical studies of complexes containing the Fe2S2 core characteristic of FeFe -hydrogenases including catalysis by these complexes of the reduction of acids to form dihydrogen. J Organomet Chem 694 (2009), 2681–2699.
    • (2009) J Organomet Chem , vol.694 , pp. 2681-2699
    • Felton, G.A.N.1    Mebi, C.A.2    Petro, B.J.3    Vannucci, A.K.4    Evans, D.H.5    Glass, R.S.6
  • 11
    • 67649283572 scopus 로고    scopus 로고
    • Structural and functional analogues of the active sites of the Fe -, NiFe -, and FeFe -Hydrogenases
    • [11] Tard, C., Pickett, C.J., Structural and functional analogues of the active sites of the Fe -, NiFe -, and FeFe -Hydrogenases. Chem Rev 109 (2009), 2245–2274.
    • (2009) Chem Rev , vol.109 , pp. 2245-2274
    • Tard, C.1    Pickett, C.J.2
  • 12
    • 77955300546 scopus 로고    scopus 로고
    • Mechanism of hydrogen production in [Fe–Fe]-hydrogenases: a quantum mechanics/molecular mechanics study
    • [12] Trohalaki, S., Pachter, R., Mechanism of hydrogen production in [Fe–Fe]-hydrogenases: a quantum mechanics/molecular mechanics study. Int J Hydrogen Energy 35 (2010), 5318–5331.
    • (2010) Int J Hydrogen Energy , vol.35 , pp. 5318-5331
    • Trohalaki, S.1    Pachter, R.2
  • 14
    • 77957253763 scopus 로고    scopus 로고
    • Tuning of electron transfer in diiron azo-bridged complexes relevant to hydrogenases
    • [14] Orain, P.-Y., Capon, J.-F., Gloaguen, F., Schollhammer, P., Talarmin, J., Tuning of electron transfer in diiron azo-bridged complexes relevant to hydrogenases. Int J Hydrogen Energy 35 (2010), 10797–10802.
    • (2010) Int J Hydrogen Energy , vol.35 , pp. 10797-10802
    • Orain, P.-Y.1    Capon, J.-F.2    Gloaguen, F.3    Schollhammer, P.4    Talarmin, J.5
  • 15
    • 80051538667 scopus 로고    scopus 로고
    • Insights into FeFe -Hydrogenase structure, mechanism, and maturation
    • [15] Mulder, D.W., Shepard, E.M., Meuser, J.E., Joshi, N., King, P.W., Posewitz, M.C., et al. Insights into FeFe -Hydrogenase structure, mechanism, and maturation. Structure 19 (2011), 1038–1052.
    • (2011) Structure , vol.19 , pp. 1038-1052
    • Mulder, D.W.1    Shepard, E.M.2    Meuser, J.E.3    Joshi, N.4    King, P.W.5    Posewitz, M.C.6
  • 16
    • 84859982642 scopus 로고    scopus 로고
    • Structure-function relationships in FeFe -Hydrogenase active site maturation
    • [16] Nicolet, Y., Fontecilla-Camps, J.C., Structure-function relationships in FeFe -Hydrogenase active site maturation. J Biol Chem 287 (2012), 13532–13540.
    • (2012) J Biol Chem , vol.287 , pp. 13532-13540
    • Nicolet, Y.1    Fontecilla-Camps, J.C.2
  • 17
    • 84873726380 scopus 로고    scopus 로고
    • Arginine171 of chlamydomonas reinhardtii [Fe–Fe] hydrogenase HydA1 plays a crucial role in electron transfer to its catalytic center
    • [17] Sybirna, K., Ezanno, P., Baffert, C., Léger, C., Bottin, H., Arginine171 of chlamydomonas reinhardtii [Fe–Fe] hydrogenase HydA1 plays a crucial role in electron transfer to its catalytic center. Int J Hydrogen Energy 38 (2013), 2998–3002.
    • (2013) Int J Hydrogen Energy , vol.38 , pp. 2998-3002
    • Sybirna, K.1    Ezanno, P.2    Baffert, C.3    Léger, C.4    Bottin, H.5
  • 19
    • 84904438591 scopus 로고    scopus 로고
    • Enhancement of the efficiency of photocatalytic reduction of protons to hydrogen via molecular assembly
    • [19] Wu, L.-Z., Chen, B., Li, Z.-J., Tung, C.-H., Enhancement of the efficiency of photocatalytic reduction of protons to hydrogen via molecular assembly. Acc Chem Res 47 (2014), 2177–2185.
    • (2014) Acc Chem Res , vol.47 , pp. 2177-2185
    • Wu, L.-Z.1    Chen, B.2    Li, Z.-J.3    Tung, C.-H.4
  • 20
    • 84908230266 scopus 로고    scopus 로고
    • Towards biomimetic models of the reduced [FeFe]-hydrogenase that preserve the key structural features of the enzyme active site; a DFT investigation
    • [20] Sicolo, S., Bruschi, M., Bertini, L., Zampella, G., Filippi, G., Arrigoni, F., et al. Towards biomimetic models of the reduced [FeFe]-hydrogenase that preserve the key structural features of the enzyme active site; a DFT investigation. Int J Hydrogen Energy 39 (2014), 18565–18573.
    • (2014) Int J Hydrogen Energy , vol.39 , pp. 18565-18573
    • Sicolo, S.1    Bruschi, M.2    Bertini, L.3    Zampella, G.4    Filippi, G.5    Arrigoni, F.6
  • 21
    • 84902539808 scopus 로고    scopus 로고
    • Iron–iron hydrogenase active subunit covalently linking to organic chromophore for light-driven hydrogen evolution
    • [21] Gao, S., Huang, S., Duan, Q., Hou, J., Jiang, D., Liang, Q., et al. Iron–iron hydrogenase active subunit covalently linking to organic chromophore for light-driven hydrogen evolution. Int J Hydrogen Energy 39 (2014), 10434–10444.
    • (2014) Int J Hydrogen Energy , vol.39 , pp. 10434-10444
    • Gao, S.1    Huang, S.2    Duan, Q.3    Hou, J.4    Jiang, D.5    Liang, Q.6
  • 22
    • 38349129455 scopus 로고    scopus 로고
    • Controlling carbon monoxide binding at di-iron units related to the iron-only hydrogenase sub-site
    • [22] Xu, F.F., Tard, C., Wang, X.F., Ibrahim, S.K., Hughes, D.L., Zhong, W., et al. Controlling carbon monoxide binding at di-iron units related to the iron-only hydrogenase sub-site. Chem Commun, 2008, 606–608.
    • (2008) Chem Commun , pp. 606-608
    • Xu, F.F.1    Tard, C.2    Wang, X.F.3    Ibrahim, S.K.4    Hughes, D.L.5    Zhong, W.6
  • 23
    • 44349146712 scopus 로고    scopus 로고
    • First insights into the protonation of dissymetrically disubstituted di-iron azadithiolate models of the FeFe H-2 ases active site
    • [23] Ezzaher, S., Orain, P.Y., Capon, J.F., Gloaguen, F., Petillon, F.Y., Roisnel, T., et al. First insights into the protonation of dissymetrically disubstituted di-iron azadithiolate models of the FeFe H-2 ases active site. Chem Commun, 2008, 2547–2549.
    • (2008) Chem Commun , pp. 2547-2549
    • Ezzaher, S.1    Orain, P.Y.2    Capon, J.F.3    Gloaguen, F.4    Petillon, F.Y.5    Roisnel, T.6
  • 24
    • 59849087976 scopus 로고    scopus 로고
    • Influence of a pendant amine in the second coordination sphere on proton transfer at a dissymmetrically disubstituted diiron system related to the 2Fe (H) subsite of FeFe H(2)ase
    • [24] Ezzaher, S., Capon, J.F., Gloaguen, F., Petillon, F.Y., Schollhammer, P., Talarmin, J., et al. Influence of a pendant amine in the second coordination sphere on proton transfer at a dissymmetrically disubstituted diiron system related to the 2Fe (H) subsite of FeFe H(2)ase. Inorg Chem 48 (2009), 2–4.
    • (2009) Inorg Chem , vol.48 , pp. 2-4
    • Ezzaher, S.1    Capon, J.F.2    Gloaguen, F.3    Petillon, F.Y.4    Schollhammer, P.5    Talarmin, J.6
  • 25
    • 77955204720 scopus 로고    scopus 로고
    • Directing protonation in [FeFe] hydrogenase active site models by modifications in their second coordination sphere
    • [25] Ezzaher, S., Gogoll, A., Bruhn, C., Ott, S., Directing protonation in [FeFe] hydrogenase active site models by modifications in their second coordination sphere. Chem Commun 46 (2010), 5775–5777.
    • (2010) Chem Commun , vol.46 , pp. 5775-5777
    • Ezzaher, S.1    Gogoll, A.2    Bruhn, C.3    Ott, S.4
  • 26
    • 77955433459 scopus 로고    scopus 로고
    • Secondary coordination sphere interactions within the biomimetic iron azadithiolate complexes related to Fe-only hydrogenase: dynamic measure of electron density about the Fe sites
    • [26] Liu, Y.-C., Tu, L.-K., Yen, T.-H., Lee, G.-H., Yang, S.-T., Chiang, M.-H., Secondary coordination sphere interactions within the biomimetic iron azadithiolate complexes related to Fe-only hydrogenase: dynamic measure of electron density about the Fe sites. Inorg Chem 49 (2010), 6409–6420.
    • (2010) Inorg Chem , vol.49 , pp. 6409-6420
    • Liu, Y.-C.1    Tu, L.-K.2    Yen, T.-H.3    Lee, G.-H.4    Yang, S.-T.5    Chiang, M.-H.6
  • 27
    • 78650285721 scopus 로고    scopus 로고
    • Role of the azadithiolate cofactor in models for [FeFe]-Hydrogenase: novel structures and catalytic implications
    • [27] Olsen, M.T., Rauchfuss, T.B., Wilson, S.R., Role of the azadithiolate cofactor in models for [FeFe]-Hydrogenase: novel structures and catalytic implications. J Am Chem Soc 132 (2010), 17733–17740.
    • (2010) J Am Chem Soc , vol.132 , pp. 17733-17740
    • Olsen, M.T.1    Rauchfuss, T.B.2    Wilson, S.R.3
  • 28
    • 75749143458 scopus 로고    scopus 로고
    • Influence of the basicity of internal bases in diiron model complexes on hydrides formation and their transformation into protonated diiron hexacarbonyl
    • [28] Xiao, Z.Y., Xu, F.F., Long, L., Liu, Y.Q., Zampella, G., De Gioia, L., et al. Influence of the basicity of internal bases in diiron model complexes on hydrides formation and their transformation into protonated diiron hexacarbonyl. J Organomet Chem 695 (2010), 721–729.
    • (2010) J Organomet Chem , vol.695 , pp. 721-729
    • Xiao, Z.Y.1    Xu, F.F.2    Long, L.3    Liu, Y.Q.4    Zampella, G.5    De Gioia, L.6
  • 29
    • 77955417511 scopus 로고    scopus 로고
    • A rare bond between a soft metal (Fe-l) and a relatively hard base (RO-, R = phenolic moiety)
    • [29] Zhong, W., Tang, Y., Zampella, G., Wang, X.F., Yang, X.L., Hu, B., et al. A rare bond between a soft metal (Fe-l) and a relatively hard base (RO-, R = phenolic moiety). Inorg Chem Commun 13 (2010), 1089–1092.
    • (2010) Inorg Chem Commun , vol.13 , pp. 1089-1092
    • Zhong, W.1    Tang, Y.2    Zampella, G.3    Wang, X.F.4    Yang, X.L.5    Hu, B.6
  • 30
    • 79957683611 scopus 로고    scopus 로고
    • 2 activation by [FeFe]-hydrogenase models
    • [30] Camara, J.M., Rauchfuss, T.B., Mild redox complementation enables H2 activation by [FeFe]-hydrogenase models. J Am Chem Soc 133 (2011), 8098–8101.
    • (2011) J Am Chem Soc , vol.133 , pp. 8098-8101
    • Camara, J.M.1    Rauchfuss, T.B.2
  • 31
    • 79952147723 scopus 로고    scopus 로고
    • Influences on the rotated structure of diiron dithiolate complexes: electronic asymmetry vs. secondary coordination sphere interaction
    • [31] Liu, Y.-C., Tu, L.-K., Yen, T.-H., Lee, G.-H., Chiang, M.-H., Influences on the rotated structure of diiron dithiolate complexes: electronic asymmetry vs. secondary coordination sphere interaction. Dalton Trans 40 (2011), 2528–2541.
    • (2011) Dalton Trans , vol.40 , pp. 2528-2541
    • Liu, Y.-C.1    Tu, L.-K.2    Yen, T.-H.3    Lee, G.-H.4    Chiang, M.-H.5
  • 32
    • 79951919474 scopus 로고    scopus 로고
    • Diiron complexes with pendant phenol Group(s) as mimics of the diiron subunit of FeFe -hydrogenase: synthesis, characterisation, and electrochemical investigation
    • [32] Tang, Y., Wei, Z.H., Zhong, W., Liu, X.M., Diiron complexes with pendant phenol Group(s) as mimics of the diiron subunit of FeFe -hydrogenase: synthesis, characterisation, and electrochemical investigation. Eur J Inorg Chem, 2011, 1112–1120.
    • (2011) Eur J Inorg Chem , pp. 1112-1120
    • Tang, Y.1    Wei, Z.H.2    Zhong, W.3    Liu, X.M.4
  • 33
    • 84859588310 scopus 로고    scopus 로고
    • Pendant amine bases speed up proton transfers to metals by splitting the barriers
    • [33] Wang, Y., Wang, M., Sun, L., Ahlquist, M.S.G., Pendant amine bases speed up proton transfers to metals by splitting the barriers. Chem Commun 48 (2012), 4450–4452.
    • (2012) Chem Commun , vol.48 , pp. 4450-4452
    • Wang, Y.1    Wang, M.2    Sun, L.3    Ahlquist, M.S.G.4
  • 34
    • 84884498203 scopus 로고    scopus 로고
    • 2 under mild conditions by an FeFe -Hydrogenase model via an active μ-Hydride species
    • [34] Wang, N., Wang, M., Wang, Y., Zheng, D., Han, H., Ahlquist, M.S.G., et al. Catalytic activation of H2 under mild conditions by an FeFe -Hydrogenase model via an active μ-Hydride species. J Am Chem Soc 135 (2013), 13688–13691.
    • (2013) J Am Chem Soc , vol.135 , pp. 13688-13691
    • Wang, N.1    Wang, M.2    Wang, Y.3    Zheng, D.4    Han, H.5    Ahlquist, M.S.G.6
  • 35
    • 84893240550 scopus 로고    scopus 로고
    • Redox reactions of FeFe -Hydrogenase models containing an internal amine and a pendant phosphine
    • [35] Zheng, D., Wang, M., Chen, L., Wang, N., Sun, L., Redox reactions of FeFe -Hydrogenase models containing an internal amine and a pendant phosphine. Inorg Chem 53 (2014), 1555–1561.
    • (2014) Inorg Chem , vol.53 , pp. 1555-1561
    • Zheng, D.1    Wang, M.2    Chen, L.3    Wang, N.4    Sun, L.5
  • 37
    • 15044340431 scopus 로고    scopus 로고
    • Chemically modified electrode based on an organometallic model of the FeFe hydrogenase active center
    • [37] Vijaikanth, V., Capon, J.F., Gloaguen, F., Schollhammer, P., Talarmin, J., Chemically modified electrode based on an organometallic model of the FeFe hydrogenase active center. Electrochem Commun 7 (2005), 427–430.
    • (2005) Electrochem Commun , vol.7 , pp. 427-430
    • Vijaikanth, V.1    Capon, J.F.2    Gloaguen, F.3    Schollhammer, P.4    Talarmin, J.5
  • 38
    • 77957255512 scopus 로고    scopus 로고
    • Immobilization of FeFe hydrogenase mimics onto carbon and gold electrodes by controlled aryldiazonium salt reduction: an electrochemical, XPS and ATR-IR study
    • [38] Le Goff, A., Artero, V., Metaye, R., Moggia, F., Jousselme, B., Razavet, M., et al. Immobilization of FeFe hydrogenase mimics onto carbon and gold electrodes by controlled aryldiazonium salt reduction: an electrochemical, XPS and ATR-IR study. Int J Hydrogen Energy 35 (2010), 10790–10796.
    • (2010) Int J Hydrogen Energy , vol.35 , pp. 10790-10796
    • Le Goff, A.1    Artero, V.2    Metaye, R.3    Moggia, F.4    Jousselme, B.5    Razavet, M.6
  • 39
    • 34147188941 scopus 로고    scopus 로고
    • Electropolymeric materials incorporating subsite structures related to iron-only hydrogenase: active ester functionalised poly(pyrroles) for covalent binding of {2Fe3S}-carbonyl/cyanide assemblies
    • [39] Ibrahim, S.K., Liu, X.M., Tard, C., Pickett, C.J., Electropolymeric materials incorporating subsite structures related to iron-only hydrogenase: active ester functionalised poly(pyrroles) for covalent binding of {2Fe3S}-carbonyl/cyanide assemblies. Chem Commun, 2007, 1535–1537.
    • (2007) Chem Commun , pp. 1535-1537
    • Ibrahim, S.K.1    Liu, X.M.2    Tard, C.3    Pickett, C.J.4
  • 40
    • 77958496642 scopus 로고    scopus 로고
    • Artificial hydrogenases: assembly of an H-cluster analogue within a functionalised poly(pyrrole) matrix
    • [40] Ibrahim, S., Woi, P.M., Alias, Y., Pickett, C.J., Artificial hydrogenases: assembly of an H-cluster analogue within a functionalised poly(pyrrole) matrix. Chem Commun 46 (2010), 8189–8191.
    • (2010) Chem Commun , vol.46 , pp. 8189-8191
    • Ibrahim, S.1    Woi, P.M.2    Alias, Y.3    Pickett, C.J.4
  • 41
    • 67649219721 scopus 로고    scopus 로고
    • Resin-bound models of the FeFe -hydrogenase enzyme active site and studies of their reactivity
    • [41] Green, K.N., Hess, J.L., Thomas, C.M., Darensbourg, M.Y., Resin-bound models of the FeFe -hydrogenase enzyme active site and studies of their reactivity. Dalton Trans, 2009, 4344–4350.
    • (2009) Dalton Trans , pp. 4344-4350
    • Green, K.N.1    Hess, J.L.2    Thomas, C.M.3    Darensbourg, M.Y.4
  • 42
    • 79951919895 scopus 로고    scopus 로고
    • Artificial FeFe -Hydrogenase: on resin modification of an amino acid to anchor a Hexacarbonyldiiron cluster in a peptide Framework
    • [42] Roy, S., Shinde, S., Hamilton, G.A., Hartnett, H.E., Jones, A.K., Artificial FeFe -Hydrogenase: on resin modification of an amino acid to anchor a Hexacarbonyldiiron cluster in a peptide Framework. Eur J Inorg Chem, 2011, 1050–1055.
    • (2011) Eur J Inorg Chem , pp. 1050-1055
    • Roy, S.1    Shinde, S.2    Hamilton, G.A.3    Hartnett, H.E.4    Jones, A.K.5
  • 43
    • 84866245294 scopus 로고    scopus 로고
    • Photo-induced hydrogen production in a helical peptide incorporating a [FeFe] hydrogenase active site mimic
    • [43] Roy, A., Madden, C., Ghirlanda, G., Photo-induced hydrogen production in a helical peptide incorporating a [FeFe] hydrogenase active site mimic. Chem Commun 48 (2012), 9816–9818.
    • (2012) Chem Commun , vol.48 , pp. 9816-9818
    • Roy, A.1    Madden, C.2    Ghirlanda, G.3
  • 44
    • 77952175216 scopus 로고    scopus 로고
    • Bioinspired polymer functionalized with a diiron carbonyl model complex and its assembly onto the surface of a gold electrode via “Click” chemistry
    • [44] Ru, X., Zeng, X.H., Li, Z.M., Evans, D.J., Zhan, C.X., Tang, Y., et al. Bioinspired polymer functionalized with a diiron carbonyl model complex and its assembly onto the surface of a gold electrode via “Click” chemistry. J Polym Sci Part A Polym Chem 48 (2010), 2410–2417.
    • (2010) J Polym Sci Part A Polym Chem , vol.48 , pp. 2410-2417
    • Ru, X.1    Zeng, X.H.2    Li, Z.M.3    Evans, D.J.4    Zhan, C.X.5    Tang, Y.6
  • 45
    • 79960910605 scopus 로고    scopus 로고
    • A polyene-based polymer functionalized with a model of FeFe -hydrogenase and film electrodes assembled from the polymer via spin-coating
    • [45] Liu, X.M., Ru, X., Li, Y., Zhang, K.K., Chen, D.Y., A polyene-based polymer functionalized with a model of FeFe -hydrogenase and film electrodes assembled from the polymer via spin-coating. Int J Hydrogen Energy 36 (2011), 9612–9619.
    • (2011) Int J Hydrogen Energy , vol.36 , pp. 9612-9619
    • Liu, X.M.1    Ru, X.2    Li, Y.3    Zhang, K.K.4    Chen, D.Y.5
  • 46
    • 78649281581 scopus 로고    scopus 로고
    • Synthesis and characterisation of polymeric materials consisting of {Fe-2(CO)(5)}-unit and their relevance to the diiron sub-unit of [FeFe]-hydrogenase
    • [46] Zhan, C.X., Wang, X.F., Wei, Z.H., Evans, D.J., Ru, X.A., Zeng, X.H., et al. Synthesis and characterisation of polymeric materials consisting of {Fe-2(CO)(5)}-unit and their relevance to the diiron sub-unit of [FeFe]-hydrogenase. Dalton Trans 39 (2010), 11255–11262.
    • (2010) Dalton Trans , vol.39 , pp. 11255-11262
    • Zhan, C.X.1    Wang, X.F.2    Wei, Z.H.3    Evans, D.J.4    Ru, X.A.5    Zeng, X.H.6
  • 47
    • 84859119803 scopus 로고    scopus 로고
    • Enable PVC plastic for a novel role: its functionalisation with diiron models of the sub-unit of FeFe -hydrogenase, assembly of film electrodes, and electrochemical investigations
    • [47] Wang, L.J., Xiao, Z.Y., Ru, X., Liu, X.M., Enable PVC plastic for a novel role: its functionalisation with diiron models of the sub-unit of FeFe -hydrogenase, assembly of film electrodes, and electrochemical investigations. RSC Adv 1 (2011), 1211–1219.
    • (2011) RSC Adv , vol.1 , pp. 1211-1219
    • Wang, L.J.1    Xiao, Z.Y.2    Ru, X.3    Liu, X.M.4
  • 48
    • 84867380034 scopus 로고    scopus 로고
    • [FeFe]-hydrogenase-inspired membrane electrode and its catalytic evolution of hydrogen in water
    • [48] Xu, E., Xiao, Z., Liu, H., Long, L., Li, L., Liu, X., [FeFe]-hydrogenase-inspired membrane electrode and its catalytic evolution of hydrogen in water. RSC Adv 2 (2012), 10171–10174.
    • (2012) RSC Adv , vol.2 , pp. 10171-10174
    • Xu, E.1    Xiao, Z.2    Liu, H.3    Long, L.4    Li, L.5    Liu, X.6
  • 50
    • 84865675242 scopus 로고    scopus 로고
    • Three diiron complexes bearing an aromatic ring as mimics of the diiron subunit of FeFe -hydrogenase: synthesis, electron transfer and coupled chemical reactions
    • [50] Zhao, J., Wei, Z., Zeng, X., Liu, X., Three diiron complexes bearing an aromatic ring as mimics of the diiron subunit of FeFe -hydrogenase: synthesis, electron transfer and coupled chemical reactions. Dalton Trans 41 (2012), 11125–11133.
    • (2012) Dalton Trans , vol.41 , pp. 11125-11133
    • Zhao, J.1    Wei, Z.2    Zeng, X.3    Liu, X.4
  • 51
    • 84886429509 scopus 로고    scopus 로고
    • Water-soluble diiron hexacarbonyl complex as a CO-RM: controllable CO-releasing, releasing mechanism and biocompatibility
    • [51] Long, L., Jiang, X., Wang, X., Xiao, Z., Liu, X., Water-soluble diiron hexacarbonyl complex as a CO-RM: controllable CO-releasing, releasing mechanism and biocompatibility. Dalton Trans 42 (2013), 15663–15669.
    • (2013) Dalton Trans , vol.42 , pp. 15663-15669
    • Long, L.1    Jiang, X.2    Wang, X.3    Xiao, Z.4    Liu, X.5
  • 52
    • 84902281538 scopus 로고    scopus 로고
    • Diiron hexacarbonyl complexes as potential CO-RMs: CO-releasing initiated by a substitution reaction with cysteamine and structural correlation to the bridging linkage
    • [52] Jiang, X., Long, L., Wang, H., Chen, L., Liu, X., Diiron hexacarbonyl complexes as potential CO-RMs: CO-releasing initiated by a substitution reaction with cysteamine and structural correlation to the bridging linkage. Dalton Trans 43 (2014), 9968–9975.
    • (2014) Dalton Trans , vol.43 , pp. 9968-9975
    • Jiang, X.1    Long, L.2    Wang, H.3    Chen, L.4    Liu, X.5
  • 53
    • 33947461960 scopus 로고
    • Preparation of graphitic oxide
    • [53] Hummers, W.S., Offeman, R.E., Preparation of graphitic oxide. J Am Chem Soc, 80, 1958, 1339.
    • (1958) J Am Chem Soc , vol.80 , pp. 1339
    • Hummers, W.S.1    Offeman, R.E.2
  • 54
    • 53849085330 scopus 로고    scopus 로고
    • Nano-graphene oxide for cellular imaging and drug delivery
    • [54] Sun, X.M., Liu, Z., Welsher, K., Robinson, J.T., Goodwin, A., Zaric, S., et al. Nano-graphene oxide for cellular imaging and drug delivery. Nano Res 1 (2008), 203–212.
    • (2008) Nano Res , vol.1 , pp. 203-212
    • Sun, X.M.1    Liu, Z.2    Welsher, K.3    Robinson, J.T.4    Goodwin, A.5    Zaric, S.6


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