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Preparation, structures and electrochemical property of phosphine substituted diiron azadithiolates relevant to the active site of Fe-only hydrogenases
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2007 (English)In: Journal of Inorganic Biochemistry, ISSN 0162-0134, E-ISSN 1873-3344, Vol. 101, no 3, 506-513 p.Article in journal (Refereed) Published
Abstract [en]

Mono- and di-phosphine diiron azadithiolate complexes [{(mu-SCH2)(2)N(4-NO2C6H4)}Fe-2(CO)(5)(PMe3)] (2), [{(mu-SCH2)(2)N(4NO(2)C(6)H(4))} {Fe(CO)(2)L}(2)] (3, L = PMe3; 4, PMe2Ph) and the mu-hydride diiron complex [3(FeHFe)](+)[PF6](-) were prepared as biontimetic models of the active site of Fe-only hydrogenases. The complexes 2-4 and [3(FeHFe)](+)[PF6](-) were characterized by IR P-31, H-1 and C-13 NMR spectra and their molecular structures were determined by single crystal X-ray analyses. The PMe3 ligand in complex 2 lies on the basal position. The PMe3-disubstituted complex 3 exists as two configuration isomers, transoid basal/basal and apical/basal, in the crystalline state, while two PMe2Ph ligands of 4 are in an apical/basal orientation. The variable temperature P-31 NMR spectra of 2 and 3 were made to have an insight into the existence of the possible conformation isomers of 2 and 3 in solution. The [3(FeHFe)](+) cation possesses the sole transoid ba/ba geometry as other reported mu-hydride diiron analogues. The electrocatalytic property of {(mu-SCH2)(2)NC6H5}[Fe(CO)(2)PMe3](2) (5) was studied for proton reduction in the presence of HOAc.

Place, publisher, year, edition, pages
2007. Vol. 101, no 3, 506-513 p.
Keyword [en]
bioinorganic chemistry, diiron azadithiolate, iron hydrogenase, iron complex, P ligands, all-iron hydrogenase, model complexes, coordination, exchange, analogs, ligand, photosensitizer, reduction, evolution, subsite
URN: urn:nbn:se:kth:diva-16437DOI: 10.1016/j.jinorgbio.2006.11.013ISI: 000244773800014ScopusID: 2-s2.0-33846637193OAI: diva2:334479
QC 20100525Available from: 2010-08-05 Created: 2010-08-05Bibliographically approved

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Sun, Licheng
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