Source:http://linkedlifedata.com/resource/pubmed/id/17295467
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
2007-3-12
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pubmed:abstractText |
The displacement of CO in a few simple Fe(I)-Fe(I) hydrogenase model complexes by bisphosphine ligands Ph2P-(CH2)n-PPh2 [with n = 1 (dppm) or n = 2 (dppe)] is described. The reaction of [{mu-(SCH2)2CH2}Fe2(CO)6] (1) and [{mu-(SCH2)2N(CH2CH2CH3)}Fe2(CO)6] (2) with dppe gave double butterfly complexes [{mu-(SCH2)2CH2}Fe2(CO)5(Ph2PCH2)]2 (3) and [{mu-(SCH2)2N(CH2CH2CH3)}Fe2(CO)5(Ph2PCH2)]2 (4), where two Fe2S2 units are linked by the bisphosphine. In addition, an unexpected byproduct, [{mu-(SCH2)2N(CH2CH2CH3)}Fe2(CO)5{Ph2PCH2CH2(Ph2PS)}] (5), was isolated when 2 was used as a substrate, where only one phosphorus atom of dppe is coordinated, while the other has been converted to P=S, presumably by nucleophilic attack on bridging sulfur. By contrast, the reaction of 1 and 2 with dppm under mild conditions gave only complexes [{mu-(SCH2)2CH2}Fe2(CO)5(Ph2PCH2PPh2)] (6) and [{mu-(SCH2)2N(CH2CH2CH3)}Fe2(CO)5(Ph2PCH2PPh2)] (8), where one ligand coordinated in a monodentate fashion to one Fe2S2 unit. Furthermore, under forcing conditions, the complexes [{mu-(SCH2)2CH2}Fe2(CO)4{mu-(Ph2P)2CH2}] (7) and [{mu-(SCH2)2N(CH2CH2CH3)}Fe2(CO)4{mu-(Ph2P)2CH2}] (9) were formed, where the phosphine acts as a bidentate ligand, binding to both the iron atoms in the same molecular unit. Electrochemical studies show that the complexes 3, 4, and 9 catalyze the reduction of protons to molecular hydrogen, with 4 electrolyzed already at -1.40 V versus Ag/AgNO3 (-1.0 V vs NHE).
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Hydrogenase,
http://linkedlifedata.com/resource/pubmed/chemical/Iron,
http://linkedlifedata.com/resource/pubmed/chemical/Iron-Sulfur Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphines,
http://linkedlifedata.com/resource/pubmed/chemical/Protons,
http://linkedlifedata.com/resource/pubmed/chemical/Sulfur,
http://linkedlifedata.com/resource/pubmed/chemical/iron hydrogenase
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0020-1669
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
19
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pubmed:volume |
46
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1981-91
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:17295467-Binding Sites,
pubmed-meshheading:17295467-Catalysis,
pubmed-meshheading:17295467-Hydrogenase,
pubmed-meshheading:17295467-Iron,
pubmed-meshheading:17295467-Iron-Sulfur Proteins,
pubmed-meshheading:17295467-Ligands,
pubmed-meshheading:17295467-Magnetic Resonance Spectroscopy,
pubmed-meshheading:17295467-Models, Molecular,
pubmed-meshheading:17295467-Phosphines,
pubmed-meshheading:17295467-Protons,
pubmed-meshheading:17295467-Spectrometry, Mass, Electrospray Ionization,
pubmed-meshheading:17295467-Spectrophotometry, Infrared,
pubmed-meshheading:17295467-Sulfur
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pubmed:year |
2007
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pubmed:articleTitle |
Binuclear iron-sulfur complexes with bidentate phosphine ligands as active site models of Fe-hydrogenase and their catalytic proton reduction.
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pubmed:affiliation |
State Key Laboratory of Fine Chemicals, DUT-KTH Joint Education and Research Center on Molecular Devices, Dalian University of Technology, 116012 Dalian, China.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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