Hydrogen-activating models of hydrogenases

Xu, Tao; Chen, Dafa; Hu, Xile

doi:10.1016/j.ccr.2015.05.007

Cited by 72 publications

(49 citation statements)

References 78 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…26 Before these examples are described, two less-biomimetic situations are addressed, in which model complexes instead accept either a H + or a H • from H 2 .…”

Section: [Nife]-h2asesmentioning

confidence: 99%

See 1 more Smart Citation

Hydrogenase Enzymes and Their Synthetic Models: The Role of Metal Hydrides

et al. 2016

View full text Add to dashboard Cite

Hydrogenase enzymes efficiently process H2 and protons at organometallic FeFe, NiFe, or Fe active sites. Synthetic modeling of the many H2ase states has provided insight into H2ase structure and mechanism, as well as afforded catalysts for the H2 energy vector. Particularly important are hydride-bearing states, with synthetic hydride analogues now known for each hydrogenase class. These hydrides are typically prepared by protonation of low-valent cores. Examples of FeFe and NiFe hydrides derived from H2 have also been prepared. Such chemistry is more developed than mimicry of the redox-inactive monoFe enzyme, although functional models of the latter are now emerging. Advances in physical and theoretical characterization of H2ase enzymes and synthetic models have proven key to the study of hydrides in particular, and will guide modeling efforts toward more robust and active species optimized for practical applications.

show abstract

“…26 Before these examples are described, two less-biomimetic situations are addressed, in which model complexes instead accept either a H + or a H • from H 2 .…”

Section: [Nife]-h2asesmentioning

confidence: 99%

“…This may indicate that secondary interactions involving the [Fe]-H 2 ase pocket, the inclusion of methenyl-H 4 MPT + , and the presence of a more substituted pyridyl ligand are important factors in the activation of H 2 . 26 …”

Section: [Fe]-h2asesmentioning

confidence: 99%

Hydrogenase Enzymes and Their Synthetic Models: The Role of Metal Hydrides

et al. 2016

View full text Add to dashboard Cite

show abstract

“…[242,243] The intermetallic NiÀFe distance in O 2 -tolerant Desulfovibrio vulgaris Miyazaki is 2.80 (oxidizeds tate) À2.69 (reduced state). [244,245] In the activated state of the enzyme( Ni-SI a )alow-spin Fe II and Ni II center is present. [246] A1 H + /1 e À transfer subsequently leads to aN i I state (Ni-L) and protonation of ac ysteine.…”

Section: Hydrogene Volution and Consumption-[fefe]-and [Nife]-hydrogementioning

confidence: 99%

From Enzymes to Functional Materials—Towards Activation of Small Molecules

Möller

Piontek

Miller

et al. 2017

Chemistry A European J

View full text Add to dashboard Cite

The design of non-noble metal-containing heterogeneous catalysts for the activation of small molecules is of utmost importance for our society. While nature possesses very sophisticated machineries to perform such conversions, rationally designed catalytic materials are rare. Herein, we aim to raise the awareness of the overall common design and working principles of catalysts incorporating aspects of biology, chemistry, and material sciences.

show abstract

“…Among the catalystsf or H 2 activation, hydrogenasesh ave attractedi ncreasing attentions in recent years becauset hey are efficient catalysts for the reversible oxidationo fH 2 with only the base metalsi ron and nickel at their actives ites. Thea ctive site structures [8] and catalytic reaction mechanisms of [Fe], [9] [FeFe], [10] and [NiFe]h ydrogenases [11] have been well elucidated. Inspired by the active site structure of [Fe] hydrogenase, [12] we have computationally designed as eries of iron complexes with experimentally ready-made acylmethylpyridinola nd aliphatic PNPp incer ligands fort he catalytich ydrogenation of CO 2 to formic acid.…”

Section: Introductionmentioning

confidence: 99%

Computational Design of Iron Diphosphine Complexes with Pendant Amines for Hydrogenation of CO₂ to Methanol: A Mimic of [NiFe] Hydrogenase

Chen

Jing

Yang

2016

Chemistry A European J

View full text Add to dashboard Cite

Inspired by the active-site structure of the [NiFe] hydrogenase, we have computationally designed the iron complex [P(tBu) 2 N(tBu) 2 )Fe(CN)2 CO] by using an experimentally ready-made diphosphine ligand with pendant amines for the hydrogenation of CO2 to methanol. Density functional theory calculations indicate that the rate-determining step in the whole catalytic reaction is the direct hydride transfer from the Fe center to the carbon atom in the formic acid with a total free energy barrier of 28.4 kcal mol(-1) in aqueous solution. Such a barrier indicates that the designed iron complex is a promising low-cost catalyst for the formation of methanol from CO2 and H2 under mild conditions. The key role of the diphosphine ligand with pendent amine groups in the reaction is the assistance of the cleavage of H2 by forming a Fe-H(δ-) ⋅⋅⋅H(δ+) -N dihydrogen bond in a fashion of frustrated Lewis pairs.

show abstract

Hydrogen-activating models of hydrogenases

Cited by 72 publications

References 78 publications

Hydrogenase Enzymes and Their Synthetic Models: The Role of Metal Hydrides

Hydrogenase Enzymes and Their Synthetic Models: The Role of Metal Hydrides

From Enzymes to Functional Materials—Towards Activation of Small Molecules

Computational Design of Iron Diphosphine Complexes with Pendant Amines for Hydrogenation of CO₂ to Methanol: A Mimic of [NiFe] Hydrogenase

Contact Info

Product

Resources

About

Hydrogen-activating models of hydrogenases

Cited by 72 publications

References 78 publications

Hydrogenase Enzymes and Their Synthetic Models: The Role of Metal Hydrides

Hydrogenase Enzymes and Their Synthetic Models: The Role of Metal Hydrides

From Enzymes to Functional Materials—Towards Activation of Small Molecules

Computational Design of Iron Diphosphine Complexes with Pendant Amines for Hydrogenation of CO2 to Methanol: A Mimic of [NiFe] Hydrogenase

Contact Info

Product

Resources

About

Computational Design of Iron Diphosphine Complexes with Pendant Amines for Hydrogenation of CO₂ to Methanol: A Mimic of [NiFe] Hydrogenase