Publication Date:
2013-02-09
Description:
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).〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ogo, Seiji -- Ichikawa, Koji -- Kishima, Takahiro -- Matsumoto, Takahiro -- Nakai, Hidetaka -- Kusaka, Katsuhiro -- Ohhara, Takashi -- New York, N.Y. -- Science. 2013 Feb 8;339(6120):682-4. doi: 10.1126/science.1231345.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉World Premier International Research Center Initiative-International Institute for Carbon-Neutral Energy Research, Kyushu University, 744 Moto-oka, Nishi-ku, Fukuoka 819-0395, Japan. ogotcm@mail.cstm.kyushu-u.ac.jp〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23393260" target="_blank"〉PubMed〈/a〉
Keywords:
Catalysis
;
*Electrons
;
Hydrogen/*chemistry
;
Hydrogenase/*chemistry/metabolism
;
Iron/*chemistry
;
Ligands
;
Models, Chemical
;
Molecular Mimicry
;
Molecular Structure
;
Nickel/*chemistry
;
Organometallic Compounds/*chemistry
;
Oxidation-Reduction
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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