Diiron azadithiolate models with bulky bridgehead moiety: Synthesis, structure and electrochemistry

Gao, Xin-Ping; Li, Shun-Xi; Hu, Kui; Deng, Cheng-Long; Bai, Shu-Fen; Wang, Yan-Lan; Xie, Hao-Tian; Lü, Shuang; Li, Yu-Long; Li, Qian-Li

doi:10.1016/j.molstruc.2024.137881

Cited by 2 publications

(1 citation statement)

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“…5 and S37,† the reduction values for 2 , [ 3 ] Cl and [ 6 ] Cl begin to decrease at slow scan rates, then exhibit linearity at fast scan rates. Based on the reported analogous sulfur complexes, 42,47–50 it is suggested that the reduction wave of complexes 2 , [ 3 ] Cl , and [ 6 ] Cl arises from a one-electron reduction process. Therefore, the reductions for [ 3 ] Cl and [ 6 ] Cl and the first reduction of 2 could be assigned to Fe II Fe II to Fe II Fe I species.…”

Section: Resultsmentioning

confidence: 99%

Facile access to tetra-substituted Fe^IIFe^II biomimetics for the oxidized state active site of [FeFe]-hydrogenases

Gao,

Bai,

Wang

et al. 2024

Inorg. Chem. Front.

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Section: Resultsmentioning

confidence: 99%

Facile access to tetra-substituted Fe^IIFe^II biomimetics for the oxidized state active site of [FeFe]-hydrogenases

Gao,

Bai,

Wang

et al. 2024

Inorg. Chem. Front.

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Tertiary phosphine‐supported diiron model complexes relevant to [FeFe]‐hydrogenases

Gao,

Jin,

Zhang

et al. 2024

Applied Organom Chemis

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In an effort to better probe the structure–function relationship on the biological [Fe4S4] cluster of [FeFe]‐hydrogenases, a new library of tertiary phosphine‐supported diiron dithiolate complexes [Fe2(μ‐adtNR)(CO)5{P(C6H4X)3}] (1–3) with various substituents (X = F vs. H vs. Me), wherein adtNR is denoted as abbreviation for the (SCH2)2N(C6H4C2H4OC(O)CH2C6H4Me) unit, is prepared as the active site mimics of [FeFe]‐hydrogenases. Notably, the substituent influences of tertiary phosphines on the structures and electrochemical behaviors of 1–3 are studied by spectroscopic and crystallographic techniques as well as cyclic voltammetry. For example, the electronic effect of tertiary phosphines [P(C6H4X)3] is responsible for the electron density around diiron center and the key Fe–Fe as well as Fe–P lengths in 1–3 as revealed by IR spectroscopy and crystallographic analysis. Further, complexes 1–3 show the electrochemical activity for proton reduction into molecular hydrogen (H2) using acetic acid (AcOH) as a proton source. Noticeably, F‐substituent‐containing diiron model complex 1 exhibits greater turnover frequency (i.e., turnover frequency value) and similar overpotential for electrocatalytic H2 evolution relative to H‐ or Me‐substituent‐bearing diiron homologs 2 or 3.

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Diiron azadithiolate models with bulky bridgehead moiety: Synthesis, structure and electrochemistry

Cited by 2 publications

References 72 publications

Facile access to tetra-substituted Fe^IIFe^II biomimetics for the oxidized state active site of [FeFe]-hydrogenases

Facile access to tetra-substituted Fe^IIFe^II biomimetics for the oxidized state active site of [FeFe]-hydrogenases

Tertiary phosphine‐supported diiron model complexes relevant to [FeFe]‐hydrogenases

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Diiron azadithiolate models with bulky bridgehead moiety: Synthesis, structure and electrochemistry

Cited by 2 publications

References 72 publications

Facile access to tetra-substituted FeIIFeII biomimetics for the oxidized state active site of [FeFe]-hydrogenases

Facile access to tetra-substituted FeIIFeII biomimetics for the oxidized state active site of [FeFe]-hydrogenases

Tertiary phosphine‐supported diiron model complexes relevant to [FeFe]‐hydrogenases

Contact Info

Product

Resources

About

Facile access to tetra-substituted Fe^IIFe^II biomimetics for the oxidized state active site of [FeFe]-hydrogenases

Facile access to tetra-substituted Fe^IIFe^II biomimetics for the oxidized state active site of [FeFe]-hydrogenases