Challenge of new biological energy resources |
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Authors: | Qi Zhang Daizheng Liao Genglin Wang |
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Institution: | (1) Department of Chemistry, Nankai University, 300071 Tianjin, China |
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Abstract: | Hydrogenases are enzymes that can reversibly split molecular hydrogen. Study on the structure of the active site and the mechanism
of catalysis has drawn great attention because the results may be useful for the design of cheap biomimetic hydrogen catalysts
for fuel cells, or as model for the photoproduction of H2. At one time the active site was generally considered to be composed of mononuclear nickel complex with ligands from the
polypeptide. A breakthrough in the understanding of the structure of NiFe] Hases occurred with the resolution crystal structure
ofD. gigas NiFe] Hases in 1995. The unexpected result challenged the previously reported spectroscopic studies and caused some academic
arguments. Some methods and results used for insight into NiFe] Hases have to be reconsidered. Different viewpoints concerning
the structure of active site of NiFe] Hases in different periods and some remaining questions will be presented. |
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Keywords: | Hydrogenases nickel-iron complexes heterodinuclear cluster active site fuel cells |
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