期刊
CHEMISTRY-A EUROPEAN JOURNAL
卷 21, 期 10, 页码 3987-3996出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/chem.201405619
关键词
biomimetic chemistry; density functional calculations; enzyme models; hydrogenase; ligand effects
资金
- Paul B. and Mildred Seydel Foundation
- Fulbright US Student Program
- Swiss National Science Foundation (SNSF) [200020_152850/1]
- EPFL
- SNSF [20021_137529]
- Swiss National Science Foundation (SNF) [200020_152850] Funding Source: Swiss National Science Foundation (SNF)
The chemistry of [Fe]-hydrogenase has attracted significant interest due to its ability to activate molecular hydrogen. The intriguing properties of this enzyme have prompted the synthesis of numerous small molecule mimics aimed at activating H-2. Despite considerable effort, a majority of these compounds remain nonfunctional for hydrogenation reactions. By using a recently synthesized model as an entry point, seven biomimetic complexes have been examined through DFT computations to probe the influence of ligand environment on the ability of a mimic to bind and split H-2. One mimic, featuring a bidentate diphosphine group incorporating an internal nitrogen base, was found to have particularly attractive energetics, prompting a study of the role played by the proton/hydride acceptor necessary to complete the catalytic cycle. Computations revealed an experimentally accessible energetic pathway involving a benzaldehyde proton/hydride acceptor and the most promising catalyst.
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