Artificial hydrogenases

被引:80
作者
Barton, Bryan E. [1 ]
Olsen, Matthew T. [1 ]
Rauchfuss, Thomas B. [1 ]
机构
[1] Univ Illinois, Sch Chem Sci, Urbana, IL 61801 USA
基金
美国国家卫生研究院;
关键词
ACTIVE-SITE MODELS; DE-NOVO DESIGN; H-2; PRODUCTION; STRUCTURAL-PROPERTIES; ELECTRONIC-PROPERTIES; MOLECULAR-HYDROGEN; IRON HYDROGENASE; COMPLEXES; CATALYSIS; DIHYDROGEN;
D O I
10.1016/j.copbio.2010.03.003
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Decades of biophysical study on the hydrogenase (H(2)ase) enzymes have yielded sufficient information to guide the synthesis of analogs of their active sites. Three families of enzymes serve as inspiration for this work: the [FeFe]-H(2)ases, [NiFe]-H(2)ases, and [Fe]-H(2)ases, all of which feature iron centers bound to both CO and thiolate. Artificial H(2)ases affect the oxidation of H-2 and the reverse reaction, the reduction of protons. These reactions occur via the intermediacy of metal hydrides. The inclusion of amine bases within the catalysts is an important design feature that is emulated in related bioinspired catalysts. Continuing challenges are the low reactivity of H-2 toward biomimetic H(2)ases.
引用
收藏
页码:292 / 297
页数:6
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