A Functional [NiFe]Hydrogenase Mimic That Catalyzes Electron and Hydride Transfer from H 2
Hydrogenase enzymes possess unusual bimetallic active sites that cleave H 2 . The enzymes make use of abundant metals (iron and sometimes nickel), in contrast to the often expensive synthetic catalysts that rely on rarer elements such as ruthenium or platinum. Ogo et al. (p. 682 ; see the Perspectiv...
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Veröffentlicht in: | Science (American Association for the Advancement of Science) 2013-02, Vol.339 (6120), p.682-684 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | Hydrogenase enzymes possess unusual bimetallic active sites that cleave H
2
. The enzymes make use of abundant metals (iron and sometimes nickel), in contrast to the often expensive synthetic catalysts that rely on rarer elements such as ruthenium or platinum.
Ogo
et al.
(p.
682
; see the Perspective by
Armstrong
) now report a bimetallic coordination compound of iron and nickel that can catalyze electron and hydride transfers from H
2
in a manner analogous to the corresponding enzyme and characterize the structure of an intermediate with bound hydride.
A bimetallic complex mimics a widely studied enzyme class of particular interest in renewable energy research.
[Also see Perspective by
Armstrong
]
Chemists have long sought to mimic enzymatic hydrogen activation with structurally simpler compounds. Here, we report a functional [NiFe]-based model of [NiFe]hydrogenase enzymes. This complex heterolytically activates hydrogen to form a hydride complex that is capable of reducing substrates by either hydride ion or electron transfer. Structural investigations were performed by a range of techniques, including x-ray diffraction and neutron scattering, resulting in crystal structures and the finding that the hydrido ligand is predominantly associated with the Fe center. The ligand's hydridic character is manifested in its reactivity with strong acid to liberate H
2
. |
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ISSN: | 0036-8075 1095-9203 |
DOI: | 10.1126/science.1231345 |