Hydrogenases as Catalysts in Renewable Energy Applications

作者: Jesse W. Tye , Michael B. Hall

DOI: 10.1002/9781119951438.EIBC2157

关键词:

摘要: This review details the role of hydrogenase enzymes in development new electrode materials for proton reduction and dihydrogen oxidation. Platinum is best catalyst these reactions, but it expensive rare. Graphite electrodes functionalized by are one possible route to synthesis inexpensive water splitting based on common, earth-abundant elements. The major shortcoming there extreme sensitivity oxygen. Experimental theoretical study mechanisms reduction, hydrogen oxidation, oxygen inactivation discussed. Natural synthetic methods increasing tolerance also discussed. Keywords: hydrogenases; hydrogen production; hydrogen oxidation; proton reduction; biomimetic chemistry; electrochemistry; catalyst inactivation; catalysis; water

参考文章(62)
Yasuhito Shomura, Ki-Seok Yoon, Hirofumi Nishihara, Yoshiki Higuchi, Structural basis for a [4Fe-3S] cluster in the oxygen-tolerant membrane-bound [NiFe]-hydrogenase Nature. ,vol. 479, pp. 253- 256 ,(2011) , 10.1038/NATURE10504
Christopher C. Page, Christopher C. Moser, Xiaoxi Chen, P. Leslie Dutton, Natural engineering principles of electron tunnelling in biological oxidation-reduction. Nature. ,vol. 402, pp. 47- 52 ,(1999) , 10.1038/46972
Tokuji Ikeda, Kazuyoshi Takagi, Hirosuke Tatsumi, Kenji Kano, Electrochemical Control of Hydrogenase Action ofDesulfovibrio vulgaris(Hildenborough) Chemistry Letters. ,vol. 26, pp. 5- 6 ,(1997) , 10.1246/CL.1997.5
Kevin D. Swanson, Benjamin R. Duffus, Trevor E. Beard, John W. Peters, Joan B. Broderick, Cyanide and Carbon Monoxide Ligand Formation in Hydrogenase Biosynthesis European Journal of Inorganic Chemistry. ,vol. 2011, pp. 935- 947 ,(2011) , 10.1002/EJIC.201001056
Yvain Nicolet, Claudine Piras, Pierre Legrand, Claude E Hatchikian, Juan C Fontecilla-Camps, Desulfovibrio desulfuricans iron hydrogenase: the structure shows unusual coordination to an active site Fe binuclear center. Structure. ,vol. 7, pp. 13- 23 ,(1999) , 10.1016/S0969-2126(99)80005-7
Pierre-Pol Liebgott, Sébastien Dementin, Christophe Léger, Marc Rousset, Towards engineering O2-tolerance in [Ni–Fe] hydrogenases Energy and Environmental Science. ,vol. 4, pp. 33- 41 ,(2011) , 10.1039/C0EE00093K
Marta C. Marques, Ricardo Coelho, Antonio L. De Lacey, Inês A.C. Pereira, Pedro M. Matias, 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 Journal of Molecular Biology. ,vol. 396, pp. 893- 907 ,(2010) , 10.1016/J.JMB.2009.12.013
Thorsten Buhrke, Oliver Lenz, Norbert Krauss, Bärbel Friedrich, Oxygen Tolerance of the H2-sensing [NiFe] Hydrogenase fromRalstonia eutrophaH16 Is Based on Limited Access of Oxygen to the Active Site Journal of Biological Chemistry. ,vol. 280, pp. 23791- 23796 ,(2005) , 10.1074/JBC.M503260200
E Garcin, X Vernede, EC Hatchikian, A Volbeda, M Frey, JC Fontecilla-Camps, The crystal structure of a reduced [NiFeSe] hydrogenase provides an image of the activated catalytic center. Structure. ,vol. 7, pp. 557- 566 ,(1999) , 10.1016/S0969-2126(99)80072-0