[Fe]‐Hydrogenase Models Featuring Acylmethylpyridinyl Ligands

Chen, Dafa; Scopelliti, Rosario; Hu, Xile

doi:10.1002/anie.201004579

Cited by 91 publications

(86 citation statements)

References 26 publications

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“…Theelucidation of the crystal structure in 2009 [2] (Figure 1, left) galvanized the development of synthetic model complexes of Hmd inspired by its distinct organometallic binding motifs-especially the fac arrangement of the C acyl ,N pyridone , and S Cys176 donors.S tructural analogues reported by Hu, [3] Pickett, [4] and Song [5] replicate the biomimetic coordination including an Fe À Co rganometallic bond, with several containing an exogenous thiolate ligand. However,d espite their structural similarity,s uch complexes have not been reported to exhibit both functionality and stability,possibly because of the absence of as ingle chelating ligand.…”

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confidence: 55%

Functional Hydride Transfer by a Thiolate‐Containing Model of Mono‐Iron Hydrogenase featuring an Anthracene Scaffold

et al. 2018

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Figure 3. Stacked 2 HNMR (a-e) and 1 HNMR (f)spectra from the reactions of a) D 2 + [MeO t Bu 2 PhO]NEt 4 + CH3 Im + ;b)1 + D 2 + CH3 Im + ;c)1 + D 2 + [MeO t Bu 2 PhO]NEt 4 ;d)1 + D 2 + [MeO t Bu 2 PhO]NEt 4 + CH3 Im + ;e ) CH3 Im + + NaBD 4 ;and f) CH3 Im + + NaBH 4 .Additional peaks in (f)correspond to methylene -CH 2 peaks in CH3 Im-H. Scheme 2. Reactivity scheme for 1 catalyzinghydride transfer to CH3 Im + under D 2 to form the hydride transfer product, CH3 Im-D.Scheme 3. Proposed reactivity scheme indicatingthe observed stoichiometrich ydride transfer to form CH3 Im-H and the corresponding return to compound 1. Angewandte ChemieCommunications 2857

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confidence: 55%

Functional Hydride Transfer by a Thiolate‐Containing Model of Mono‐Iron Hydrogenase featuring an Anthracene Scaffold

et al. 2018

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“…The IR spectra of 1−4 showed two absorption bands in the region 2036−1955 cm −1 for their two cis terminal CO ligands, one band in the range 1680−1660 cm −1 for their acyl groups and one band in the region 3380− 3305 cm −1 for their hydroxy groups. 21,24 The 1 H NMR spectra of 1−4 displayed one singlet in the range 5−15 ppm for their hydroxy group and one singlet or two doublets in the region 4.02−4.83 ppm for their CH 2 CO groups dependent upon if the two H atoms in each of the CH 2 CO groups are diastereotopic or not under the determined conditions. The 13 C{ 1 H} NMR spectra of 1−4 exhibited a signal in the range 253−264 ppm for their acyl C atoms and two signals in the region 207−213 ppm for their terminal carbonyl C atoms.…”

Section: ■ Results and Discussionmentioning

confidence: 99%

Several New [Fe]Hydrogenase Model Complexes with a Single Fe Center Ligated to an Acylmethyl(hydroxymethyl)pyridine or Acylmethyl(hydroxy)pyridine Ligand

Song

Zhao

et al. 2014

Organometallics

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We have developed two novel synthetic methods, by which two types of mononuclear Fe model complexes for the active site of [Fe]hydrogenase are successfully synthesized. The first type of 2-acylmethyl-6-hydroxymethylpyridine-containing complexes, [2-COCH 2 -6-HOCH 2 C 5 H 3 N]Fe(CO) 2 G (1, G = PhCO 2 ; 2, PhCOS; 3, PhCS 2 ; 4, 2-S-6-MeC 5 H 3 N), were prepared by a "one-pot" method involving reaction of 2-TsO-6-HOCH 2 C 5 H 3 N (Ts = 4-MeC 6 H 4 SO 2 ) with Na 2 Fe(CO) 4 followed by treatment of the resulting Fe(0) intermediate [Na(2-CH 2 -6-HOCH 2 C 5 H 3 N)Fe(CO) 4 ] (M1) with (PhCO 2 ) 2 , (PhCOS) 2 , (PhCS 2 ) 2 , and (2-S-6-MeC 5 H 3 N) 2 in 49−72% yields, respectively. The second type of 2-acylmethyl-6-hydroxypyridine-containing complexes, (2-COCH 2 -6-HOC 5 H 3 N)Fe(CO) 2 (2-SCO-6-RC 5 H 3 N) (9a, R = MeO; 9b, R = PhS), could be prepared via a multiple-step synthetic method. This method involves (i) treatment of 2-ClCO-6-RC 5 H 3 N (R = MeO, PhS) with NaSH followed by acidification with diluted HCl to give 2-HSCO-6-RC 5 H 3 N (5a, R = MeO; 5b, R = PhS); (ii) further treatment of 5a,b with KOH to afford 2-KSCO-6-RC 5 H 3 N (6a, R = MeO; 6b, R = PhS); (iii) treatment of 2-TsOCH 2 -6-PMBOC 5 H 3 N (PMB = 4-MeOC 6 H 4 CH 2 ) with Na 2 Fe(CO) 4 followed by treatment of the resulting Fe(0) intermediate [Na(2-CH 2 -6-PMBOC 5 H 3 N)Fe(CO) 4 ] (M2) with Br 2 or I 2 to produce (2-COCH 2 -6-PMBOC 5 H 3 N)Fe(CO) 3 X (7a, X = Br; 7b, X = I); (iv) further treatment of 7a,b with 6a,b to yield (2-COCH 2 -6-PMBOC 5 H 3 N)Fe(CO) 2 (2-S-6-RC 5 H 3 N) (8a, R = MeO; 8b, R = PhS); and (v) finally, removal of the PMB groups from 8a,b under the action of deprotecting reagent CF 3 CO 2 H/EtSH to give complexes 9a,b. All compounds 1−4 and 5a,b−9a,b with the exception of 7b are new and have been characterized by elemental analysis, spectroscopy, and, particularly for 1, 4, and 7a−9a, X-ray crystallography.

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“…408–410 In the synthesis of [ 58 ], Fe instead serves as an electrophile, with [Fe(CO) 5 ] undergoing addition of 2-picolide anion such that a CO ligand is converted to an acyl. 407 …”

Section: [Fe]-h2asesmentioning

confidence: 99%

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

et al. 2016

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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.

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[Fe]‐Hydrogenase Models Featuring Acylmethylpyridinyl Ligands

Abstract: Where is my iron? The synthesis, structure, and reactivity of small‐molecule models of [Fe]‐hydrogenase are described. These models feature the intriguing acylmethylpyridinyl ligands found exclusively in the enzyme.

Cited by 91 publications

References 26 publications

Functional Hydride Transfer by a Thiolate‐Containing Model of Mono‐Iron Hydrogenase featuring an Anthracene Scaffold

Functional Hydride Transfer by a Thiolate‐Containing Model of Mono‐Iron Hydrogenase featuring an Anthracene Scaffold

Several New [Fe]Hydrogenase Model Complexes with a Single Fe Center Ligated to an Acylmethyl(hydroxymethyl)pyridine or Acylmethyl(hydroxy)pyridine Ligand

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

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