期刊
SCIENCE
卷 339, 期 6120, 页码 682-684出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1231345
关键词
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资金
- WPI
- Ministry of Education, Culture, Sports, Science and Technology (MEXT), Japan [23655053, 24750058, 24109016]
- Basic Research Programs CREST Type, Development of the Foundation for Nano-Interface Technology from JST, Japan
- Grants-in-Aid for Scientific Research [24750058, 10J05090, 23655053, 24109016, 24681016] Funding Source: KAKEN
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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