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

Pan, Hui‐Jie; Hu, Xile

doi:10.1002/ange.201914377

Cited by 9 publications

(3 citation statements)

References 58 publications

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“…The Mn complexes 1-4 showed activity with lower TOF/ TON values than previously reported Mn complexes but improved icat ip values at comparable overpotentials Pan et al, 2019;Pan and Hu, 2020;Yang et al, 2021). The mononuclear Mn complex with heterocyclic (N,S; S,S) and phosphaadamantane ligands (Kaim and Kaur-Ghumaan, 2021) showed activity in both organic and partially aqueous media.…”

Section: Catalytic Activity Of Mono-nuclear Manganese Complexesmentioning

confidence: 67%

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Mononuclear manganese complexes as hydrogen evolving catalysts

Kaim

Joshi²,

Stein³

et al. 2022

Front. Chem.

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Molecular hydrogen (H2) is one of the pillars of future non-fossil energy supply. In the quest for alternative, non-precious metal catalysts for hydrogen generation to replace platinum, biological systems such as the enzyme hydrogenase serve as a blueprint. By taking inspiration from the bio-system, mostly nickel- or iron-based catalysts were explored so far. Manganese is a known oxygen-reducing catalyst but has received much less attention for its ability to reduce protons in acidic media. Here, the synthesis, characterization, and reaction mechanisms of a series of four mono-nuclear Mn(I) complexes in terms of their catalytic performance are reported. The effect of the variation of equatorial and axial ligands in their first and second coordination spheres was assessed pertaining to their control of the turnover frequencies and overpotentials. All four complexes show reactivity and reduce protons in acidic media to release molecular hydrogen H2. Quantum chemical studies were able to assign and interpret spectral characterizations from UV–Vis and electrochemistry and rationalize the reaction mechanism. Two feasible reaction mechanisms of electrochemical (E) and protonation (C) steps were compared. Quantum chemical studies can assign peaks in the cyclic voltammetry to structural changes of the complex during the reaction. The first one-electron reduction is essential to generate an open ligand-based site for protonation. The distorted octahedral Mn complexes possess an inverted second one-electron redox potential which is a pre-requisite for a swift and facile release of molecular hydrogen. This series on manganese catalysts extends the range of elements of the periodic table which are able to catalyze the hydrogen evolution reaction and will be explored further.

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Section: Catalytic Activity Of Mono-nuclear Manganese Complexesmentioning

confidence: 67%

“…The isoelectronic properties of non-native Mn I with the bio-inorganic Fe II suggest that Mn I -based complexes may also be suitable HER catalysts. However, there are very few Mn-based HER catalytic systems reported in the literature Pan et al, 2019;Pan and Hu, 2020;Kaim and Kaur-Ghumaan, 2021;Yang et al, 2021) (see Scheme 1).…”

Section: Introductionmentioning

confidence: 99%

Mononuclear manganese complexes as hydrogen evolving catalysts

Kaim

Joshi²,

Stein³

et al. 2022

Front. Chem.

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“…However, other transition metals are also known to activate or catalyze the production of hydrogen in synthetic chemical systems. Consequently, a non-native metal hydrogenase has been constructed by incorporation of a Mn-complex into the apo-[Fe]-hydrogenase from M. jannaschii heterologously produced in E. coli , resulting in a [Mn]-hydrogenase with a comparable activity to semi-synthetic [Fe]-hydrogenase [ 37 , 47 ]. However, compared to the hydrogenase reconstituted with the native FeGP cofactor the semi-synthetic enzymes showed significant less activity.…”

Section: [Fe]-hydrogenase Production Systemsmentioning

confidence: 99%

Heterologous Hydrogenase Overproduction Systems for Biotechnology—An Overview

Fan

Neubauer

Lenz

et al. 2020

IJMS

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Hydrogenases are complex metalloenzymes, showing tremendous potential as H2-converting redox catalysts for application in light-driven H2 production, enzymatic fuel cells and H2-driven cofactor regeneration. They catalyze the reversible oxidation of hydrogen into protons and electrons. The apo-enzymes are not active unless they are modified by a complicated post-translational maturation process that is responsible for the assembly and incorporation of the complex metal center. The catalytic center is usually easily inactivated by oxidation, and the separation and purification of the active protein is challenging. The understanding of the catalytic mechanisms progresses slowly, since the purification of the enzymes from their native hosts is often difficult, and in some case impossible. Over the past decades, only a limited number of studies report the homologous or heterologous production of high yields of hydrogenase. In this review, we emphasize recent discoveries that have greatly improved our understanding of microbial hydrogenases. We compare various heterologous hydrogenase production systems as well as in vitro hydrogenase maturation systems and discuss their perspectives for enhanced biohydrogen production. Additionally, activities of hydrogenases isolated from either recombinant organisms or in vivo/in vitro maturation approaches were systematically compared, and future perspectives for this research area are discussed.

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Thieme‐IUPAC‐Preis:A. Li / Springer‐Preis für Heterocyclenchemie: C. D. Vanderwal / IACS‐Preise:X. Hu, A. Corma

2020

Angewandte Chemie

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

Cited by 9 publications

References 58 publications

Mononuclear manganese complexes as hydrogen evolving catalysts

Mononuclear manganese complexes as hydrogen evolving catalysts

Heterologous Hydrogenase Overproduction Systems for Biotechnology—An Overview

Thieme‐IUPAC‐Preis:A. Li / Springer‐Preis für Heterocyclenchemie: C. D. Vanderwal / IACS‐Preise:X. Hu, A. Corma

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