A Functional Model of [Fe]-Hydrogenase

Xu, Tao; Yin, Chih-Juo Madeline; Wodrich, Matthew D.; Mazza, Simona; Schultz, Katherine M.; Scopelliti, Rosario; Hu, Xile

doi:10.1021/jacs.5b12095

Cited by 67 publications

(56 citation statements)

References 51 publications

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“…Many Fe complexes have been made to model the active site of [Fe]‐hydrogenase . Among them, only few complexes could activate H 2 –. Complex 1 (Figure c), the best structural model, is inactive towards H 2 presumably because the 2‐OH group first needs to be deprotonated.…”

Section: Figurementioning

confidence: 99%

“…This complex became active only when incorporated into the apo‐enzyme of [Fe]‐hydrogenase . To alleviate the stability problem associated with a 2‐OH group while maintaining a viable internal base, complex 2 , which contains a robust 2‐OMe group and a basic pendant N was prepared (Figure c) . This complex was indeed able to activate H 2 and mediate the hydrogenation of an aldehyde.…”

Section: Figurementioning

confidence: 99%

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Biomimetic Hydrogenation Catalyzed by a Manganese Model of [Fe]‐Hydrogenase

Pan

2020

Angew Chem Int Ed

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[Fe]‐hydrogenase is an efficient biological hydrogenation catalyst. Despite intense research, Fe complexes mimicking the active site of [Fe]‐hydrogenase have not achieved turnovers in hydrogenation reactions. Herein, we describe the design and development of a manganese(I) mimic of [Fe]‐hydrogenase. This complex exhibits the highest activity and broadest scope in catalytic hydrogenation among known mimics. Thanks to its biomimetic nature, the complex exhibits unique activity in the hydrogenation of compounds analogous to methenyl‐H4MPT+, the natural substrate of [Fe]‐hydrogenase. This activity enables asymmetric relay hydrogenation of benzoxazinones and benzoxazines, involving the hydrogenation of a chiral hydride transfer agent using our catalyst coupled to Lewis acid‐catalyzed hydride transfer from this agent to the substrates.

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Section: Figurementioning

confidence: 99%

Section: Figurementioning

confidence: 99%

Biomimetic Hydrogenation Catalyzed by a Manganese Model of [Fe]‐Hydrogenase

Pan

2020

Angew Chem Int Ed

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“…[4] Thes tructural and catalytic features of [Fe]-hydrogenases are particularly useful for designing new hydrogenation catalysts. [1,5] Numerous model catalysts that mimic the active site of [Fe]-hydrogenase have been reported. [8] Thes tability of hydrogenases and corresponding model compounds [9] is ac ritical factor for their applications.T he dinuclear metal sites of [NiFe]-and [FeFe]-hydrogenases are redox active,and most of them react with O 2 and are quickly deactivated.…”

Section: Mono-iron Hydrogenase ([Fe]-hydrogenase) Reversibly Catalyzementioning

confidence: 99%

“…In the presence of stoichiometric concentrations (26 mm)o fH 2 O 2 ,[ Fe]-hydrogenase was fully deactivated within 5min, but less than 10 %ofH 2 O 2 was lost in the deactivation assay.I nt he case of sub-stoichiometric concentrations of H 2 O 2 (2.6 mm and 0.26 mm H 2 O 2 ), substantial amounts of [Fe]-hydrogenase were decomposed;the residual [Fe]-hydrogenase activity was only 30 %a nd 60 %w ithin 10 min (Supporting Information, Figure S7) Figure S9), the most probable reductant is an iron hydride.T he proposed type of metal-hydride-driven hydrogenation reaction has precedent in inorganic ruthenium complex chemistry; [15] thereby increasing the plausibility of the mechanism. Metal-hydride formation in the [Fe]-hydrogenase reaction was already postulated on the basis of calculations [8c, 16] and modelcomplex studies [5,17] but experimental evidence was,t hus far, not provided. If our conclusions are correct, [Fe]-hydrogenase stabilizes ah ydride on its iron center in the catalytic cycle.…”

Section: Angewandte Chemiementioning

confidence: 99%

Dioxygen Sensitivity of [Fe]‐Hydrogenase in the Presence of Reducing Substrates

et al. 2018

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Mono-iron hydrogenase ([Fe]-hydrogenase) reversibly catalyzes the transfer of a hydride ion from H to methenyltetrahydromethanopterin (methenyl-H MPT ) to form methylene-H MPT. Its iron guanylylpyridinol (FeGP) cofactor plays a key role in H activation. Evidence is presented for O sensitivity of [Fe]-hydrogenase under turnover conditions in the presence of reducing substrates, methylene-H MPT or methenyl-H MPT /H . Only then, H O is generated, which decomposes the FeGP cofactor; as demonstrated by spectroscopic analyses and the crystal structure of the deactivated enzyme. O reduction to H O requires a reductant, which can be a catalytic intermediate transiently formed during the [Fe]-hydrogenase reaction. The most probable candidate is an iron hydride species; its presence has already been predicted by theoretical studies of the catalytic reaction. The findings support predictions because the same type of reduction reaction is described for ruthenium hydride complexes that hydrogenate polar compounds.

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“…Enzymes can make the chemical reactions in organisms more efficient and accurate under extremely mild conditions. Hydrogenase, found in a variety of microorganisms, can efficiently catalyze the reduction of protons to hydrogen, and can be classified into [Fe]‐hydrogenase, [NiFe]‐hydrogenase and [FeFe]‐hydrogenase . Due to the excellent catalytic properties, more and more research has been directed towards the exploration of biomimetic enzymes …”

Section: Introductionmentioning

confidence: 99%

Catalytic reduction of 1,4‐benzoquinone to hydroquinone via [FeFe]‐hydrogenase model complexes under mild conditions

Wang

Zhang

Jiang

et al. 2020

J of Chemical Tech & Biotech

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BACKGROUND Hydroquinone (HQ) is an important fine chemical raw material and intermediate, which is widely used in chemistry industry. It is great significance to develop a new environmentally‐friendly synthesis method to produce HQ. RESULTS Three [FeFe]‐hydrogenase model complexes (μ‐budt)[Fe(CO)3]2[1; budt = SCH(CH3)CH2CH2)S], (μ‐budt)[Fe(CO)3][Fe(CO)2PPh3](2), and (μ‐bust)[Fe(CO)3]2 [3; bust = SCH(CH3)CH2CH2)S(O)] were synthesized by direct CO/L substitution or sulfur based oxygenation. The synthesized new complexes were fully characterized by FT‐IR, 1H NMR, 13C NMR and X‐ray crystallography. The electrochemical properties of these model complexes were investigated by cyclic voltammetry in CH2CI2 to evaluate the redox properties of the iron atoms. It was indicated that these new complexes are not only electrochemical catalysts for proton reduction of hydrogen, but also efficient catalysts for catalytic the transfer hydrogenation of BQ (1, 4‐benzoquinone) to prepare HQ under mild conditions. Especially,complex 2 exhibited the highest catalytic activity for reduction of BQ with methanol as the proton source, which gave a BQ conversion of 91 % and 72 % selectivity for HQ. CONCLUSIONS The complex 2 can be a new type catalyst for catalytic reduction of BQ to HQ under mild reaction conditions. In addition, the Kinetics and mechanism were also investigated for a proposed transfer hydrogenation process. © 2019 Society of Chemical Industry

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A Functional Model of [Fe]-Hydrogenase

Cited by 67 publications

References 51 publications

Biomimetic Hydrogenation Catalyzed by a Manganese Model of [Fe]‐Hydrogenase

Biomimetic Hydrogenation Catalyzed by a Manganese Model of [Fe]‐Hydrogenase

Dioxygen Sensitivity of [Fe]‐Hydrogenase in the Presence of Reducing Substrates

Catalytic reduction of 1,4‐benzoquinone to hydroquinone via [FeFe]‐hydrogenase model complexes under mild conditions

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