Reconstitution of [Fe]-hydrogenase using model complexes

Shima, Seigo; Chen, Dafa; Xu, Tao; Wodrich, Matthew D.; Fujishiro, Takashi; Schultz, Katherine M.; Kahnt, Jörg; Ataka, Kenichi; Hu, Xile

doi:10.1038/nchem.2382

Cited by 94 publications

(105 citation statements)

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“…The active site of [Fe]‐hydrogenase comprises of a low‐spin Fe II centre coordinated by one H 2 O and two cis ‐CO molecules, a cysteine thiolate, as well as an acyl carbon and a pyridinyl nitrogen from a guanylylpyridinol ligand (Figure b) . The 2‐OH group of the pyridonol ligand serves as an internal base to facilitate heterolytic H 2 activation upon deprotonation …”

Section: Figurementioning

confidence: 99%

“…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%

“…However, 1 was unstable when treated with a base . 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) .…”

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%

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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“…Their oxygen sensitivity and production costs call for the development of artificial hydrogenases. Several artificial hydrogenases rely on the incorporation of artificial metal cofactors in host proteins (cytochrome c , rubredoxin, ferredoxin) or linking to a polypeptide . In the past decade, the biotin‐streptavidin technology has found widespread use for the assembly of artificial metalloenzymes (ArM) .…”

Section: Introductionmentioning

confidence: 99%

Photo‐Driven Hydrogen Evolution by an Artificial Hydrogenase Utilizing the Biotin‐Streptavidin Technology

Keller

Probst

Heinisch

et al. 2018

Helvetica Chimica Acta

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Photocatalytic hydrogen evolution by an artificial hydrogenase based on the biotin‐streptavidin technology is reported. A biotinylated cobalt pentapyridyl‐based hydrogen evolution catalyst (HEC) was incorporated into different mutants of streptavidin. Catalysis with [Ru(bpy)3]Cl2 as a photosensitizer (PS) and ascorbate as sacrificial electron donor (SED) at different pH values highlighted the impact of close lying amino acids that may act as a proton relay under the reaction conditions (Asp, Arg, Lys). In the presence of a close‐lying lysine residue, both, the rates were improved, and the reaction was initiated much faster. The X‐ray crystal structure of the artificial hydrogenase reveals a distance of 8.8 Å between the closest lying Co‐moieties. We thus suggest that the hydrogen evolution mechanism proceeds via a single Co centre. Our findings highlight that streptavidin is a versatile host protein for the assembly of artificial hydrogenases and their activity can be fine‐tuned via mutagenesis.

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“…The resulting brown solid was further recrystallized at 5 C in CH 2 Cl 2 /hexane (v/v ¼ 1 : 4) to afford 1f (0.209 g, 38%), mp 155-157 C. Anal. calcd for C 52 (3a). A 50 mL three-necked ask equipped with a magnetic stir-bar, two serum caps, and a N 2 inlet tube was charged with 1a$MeOH (0.183 g, 0.20 mmol), Fe(CO) 3 (BDA) (0.114 g, 0.40 mmol), and THF (10 mL).…”

Section: General Commentsmentioning

confidence: 99%

Reactions of dinuclear Ni₂complexes [Ni(RN_PyS₄)]₂(RN_PyS₄= 2,6-bis(2-mercaptophenylthiomethyl)-4-R-pyridine) with Fe(CO)₃(BDA) (BDA = benzylidene acetone) leading to heterodinuclear NiFe and mononuclear Fe complexes related to the active sites of [NiFe]- and [Fe]-hydrogenases

Song

Cao

et al. 2016

RSC Adv.

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While the parent Ni 2 complex [Ni(RN Py S 4 )] 2 (1a, R ¼ H; RN Py S 4 ¼ 2,6-bis(2-mercaptophenylthiomethyl)-4-R-pyridine) cannot react with Fe(CO) 3 (BDA) in THF at room temperature, its substituted derivatives (1b, R ¼ MeO; 1c, Cl; 1d, Br; 1e, i-Pr; 1f, BzO; 1g, MeS) have been found to react with Fe(CO) 3 (BDA) under the same conditions to give the first [RN Py S 4 ] ligand-containing heterodinuclear [NiFe]-hydrogenase model complexes NiFe(RN Py S 4 )(CO) 3 (2b, R ¼ MeO; 2c, Cl; 2d, Br; 2e, i-Pr; 2f, BzO; 2g, MeS) along with the mononuclear [Fe]-hydrogenase model complexes Fe(RN Py S 4 )(CO) (3b, R ¼ MeO; 3c, Cl; 3d, Br; 3e, i-Pr;3f, BzO; 3g, MeS). However, when Ni 2 complexes 1a-1g react with Fe(CO) 3 (BDA) in THF at the higher temperature of 40 C, only the mononuclear complexes 3a-3g are obtained without the corresponding dinuclear complexes 2a-2g being isolated. While all the new complexes are characterized by elemental analysis and spectroscopy, the molecular structures of 1f, 2c, 3f and 3g have been further confirmed by X-ray crystallography. In addition, a possible pathway for the formation of 2a-2g and 3a-3g is suggested, which has been proved by monitoring the reaction course of dinuclear Ni 2 complex 1e with Fe(CO) 3 (BDA) using in situ IR spectroscopy.

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Reconstitution of [Fe]-hydrogenase using model complexes

Cited by 94 publications

References 48 publications

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

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

Photo‐Driven Hydrogen Evolution by an Artificial Hydrogenase Utilizing the Biotin‐Streptavidin Technology

Reactions of dinuclear Ni₂complexes [Ni(RN_PyS₄)]₂(RN_PyS₄= 2,6-bis(2-mercaptophenylthiomethyl)-4-R-pyridine) with Fe(CO)₃(BDA) (BDA = benzylidene acetone) leading to heterodinuclear NiFe and mononuclear Fe complexes related to the active sites of [NiFe]- and [Fe]-hydrogenases

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Reconstitution of [Fe]-hydrogenase using model complexes

Cited by 94 publications

References 48 publications

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

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

Photo‐Driven Hydrogen Evolution by an Artificial Hydrogenase Utilizing the Biotin‐Streptavidin Technology

Reactions of dinuclear Ni2complexes [Ni(RNPyS4)]2(RNPyS4= 2,6-bis(2-mercaptophenylthiomethyl)-4-R-pyridine) with Fe(CO)3(BDA) (BDA = benzylidene acetone) leading to heterodinuclear NiFe and mononuclear Fe complexes related to the active sites of [NiFe]- and [Fe]-hydrogenases

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Reactions of dinuclear Ni₂complexes [Ni(RN_PyS₄)]₂(RN_PyS₄= 2,6-bis(2-mercaptophenylthiomethyl)-4-R-pyridine) with Fe(CO)₃(BDA) (BDA = benzylidene acetone) leading to heterodinuclear NiFe and mononuclear Fe complexes related to the active sites of [NiFe]- and [Fe]-hydrogenases