Scaffold-based [Fe]-hydrogenase model: H₂ activation initiates Fe(0)-hydride extrusion and non-biomimetic hydride transfer

Abstract

We report the synthesis and reactivity of a model of [Fe]-hydrogenase derived from an anthracene-based scaffold that includes the endogenous, organometallic acyl(methylene) donor.

Current State of [Fe]‐Hydrogenase and Its Biomimetic Models

“…This dimeric complex is also competent for H 2 activation. [58] The Rose group found out that a methylene-acyl-containing complex 27 with mer-C,N,S (pincer) geometry could also activate hydrogen. After incubation of this complex under D 2 in the presence of a base dBPhONEt 4 , a new resonance at 5.39 ppm corresponding to the dBPhOD appeared in 2 H NMR within 30 min, indicating activation of D 2 .…”

“…[61] Figure 11. (a) Complexes reported by Rose et al [56][57][58][59] (b) D 2 activation and the generation of HD by 24 (left); CÀ H hydride illustration from ImÀ H and H 2 evolution by 24 (right). [56] (c) D 2 activation and hydride transfer by 25.…”

“…Deprotonation of 26 with NEt 4 [MeOtBu 2 ArO] generated a dimeric complex in which iron centers bridged via the formation of a new Fe−C bond (with the deprotonated methine‐C). This dimeric complex is also competent for H 2 activation [58] …”

Structural and functional biomimetics of [Fe]-hydrogenase featuring a mono-, di- or tetrasubstituted pyridine ligand with a fac-C, N, and S ligation

“…To date, a large number of biomimetic models for the active site of [Fe]-H 2 ase have been prepared, [18][19][20][21][22][23][24][25][26][27][28][29][30][31] but very few of them have H 2 activation and hydride transfer functions. In 2016, Hu and coworkers prepared an acyl [Fe]-H 2 ase model complex A (Fig.…”

Biomimetic models of [Fe]-hydrogenase featuring a 2-acylphenylthiomethyl-6-R-pyridine (R = H or OMe) ligand

“…5 Motivated by the active site structure and the catalytic function of [Fe]-H 2 ase, synthetic chemists have prepared a wide variety of biomimetic models for the active site of [Fe]-H 2 ase, but very few of them have a biomimetic fac-C, N, S coordination motif and the enzyme-like H 2 activation function. [6][7][8][9][10][11][12][13][14][15][16][17][18][19][20][21] Therefore, the structural and functional modeling study of [Fe]-H 2 ase has remained a great challenge. Recently, Rose and coworkers reported the first two [Fe]-H 2 ase models [(AnthÁC NH NS)-Fe(CO) 2 (I)] (A) 15 and [(AnthÁpy NH ÁS)Fe(CO) 2 (PhCN)] (B) 16 with a biomimetic fac-carbamoyl C, pyridyl N, thioether or thiolate S coordination motif (Fig.…”