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New Insights Into Fe–H and Fe–H Bonding of A Theoretical Chemistry Accounts (2019) 138:76 https://doi.org/10.1007/s00214-019-2463-9 REGULAR ARTICLE − New insights into Fe–H2 and Fe–H bonding of a [NiFe] hydrogenase mimic: a local vibrational mode study Małgorzata Z. Makoś1 · Marek Freindorf1 · Daniel Sethio1 · Elf Kraka1 Received: 6 March 2019 / Accepted: 15 May 2019 / Published online: 24 May 2019 © Springer-Verlag GmbH Germany, part of Springer Nature 2019 Abstract H− H In this work, we investigated the strength of the and 2 interaction with the Fe atom of a [NiFe] hydrogenase mimic, H− H and how this interaction can be modulated by changing the Fe ligand in trans-position relative to and 2 . We used as a quantitative measure of bond strength local vibrational force constants derived from the Konkoli–Cremer local mode analysis, complemented by the topological analysis of the electronic density and the natural bond orbital analysis. Seventeen CH− diferent ligands were investigated utilizing density functional theory calculations, including -donor ligands such as 3 , C H− NH H O Cl− F− OH− CN− 2 5 , 3 , and 2 , -donor ligands such as , , and , and -donor/ -acceptor ligands such as and CO. According to the local mode analysis, Fe–H interactions are strengthened by -donor or -donor ligands and weakened by H -donor/ -acceptor ligands. In contrast, the H–H bond of 2 is weakened by -donor or -donor ligands and strengthened by -donor/-acceptor ligands. We also present a new metal–ligand electronic parameter (MLEP) for Fe–H ligands which can be generally applied to evaluate the Fe–H bond strength in iron complexes and iron hydrides. These results form a valu- able basis for future [NiFe] hydrogenase-based catalyst design and fne tuning, as well as for the development of efcient H biomimetic catalysts for 2 generation. Keywords [NiFe] Hydrogenase mimic · [NiFe] Hydrogen · Hydride complexes · Local vibrational mode analysis · Local mode force constants · Metal–ligand electronic parameter (MLEP) 1 Introduction [Fe], [FeFe], and [NiFe] hydrogenases [86]. [FeFe] and [NiFe] hydrogenases are active catalysts, while [Fe] hydro- Hydrogenases are metalloenzymes that efciently catalyze genases are only activated in the presence of methenyltet- the reversible oxidative cleavage of molecular hydrogen into rahydromethanopterin [44]. Due to their unique hetero-binu- two protons and two electrons [37, 85, 94, 109]. They are clear active site and superior oxygen tolerance, considerable present in nature and widely found in bacteria, archaea, and attention has been directed toward the [NiFe] hydrogenases some eukaryotes [136]. According to the metal atoms in the [10, 14, 82]. active site, hydrogenases can be classifed into three types: [NiFe] hydrogenases have been extensively investigated due to their importance in putative future hydrogen-based economy, such as bio-fuel, power cells, photocatalytic water Published as part of the special collection of articles derived splitting, and hydrogen sensors technologies [19, 32, 52, 61, from the 11th Congress on Electronic Structure: Principles and 137]. They have remarkable catalytic properties, particularly Applications (ESPA-2018). low-over potential and high turnover power [30, 43, 108]. A Electronic supplementary material The online version of this signifcant number of computational studies have focused article (https ://doi.org/10.1007/s0021 4-019-2463-9) contains on the structural characterization [103], the catalytic mecha- supplementary material, which is available to authorized users. nism [31, 47, 106, 107, 127, 134, 135], in particular, proton reduction [128], and the electronic structure [57, 122, 138] * Elf Kraka [email protected] and oxidation states [11, 123] of the [NiFe] hydrogenase active site. Also, several models of the [NiFe] active site 1 Computational and Theoretical Chemistry Group (CATCO), have been discussed that can mimic the chemical functions Department of Chemistry, Southern Methodist University, of the hydrogenase enzyme [59, 112]. 3215 Daniel Avenue, Dallas, TX 75275-0314, USA Vol.:(0123456789)1 3 76 Page 2 of 18 Theoretical Chemistry Accounts (2019) 138:76 H First [NiFe] hydrogenase models that exhibited 2 pro- be used as a valuable basis for the design and fne tuning of ducing activity were reported in 2005 [143]. More recent future [NiFe] biomimetic catalysts. examples of [NiFe] hydrogenase models are structures To answer these questions, we studied Ogo’s [NiFe] with phosphines ligands on Ni that evolve hydrogen [7, mimic, which we simplifed by changing the three triethyl- P(OEt) PH 8, 15] and structures with thiolate ligands bonded to Ni phosphite ( 3 ) groups to phosphine ( 3 ) ligands. Fe PH leading to reversible protonation [139] in the presence of and its ligands form a quasi-octahedron with the two 3 PH a strong acid. Additional [NiFe] complexes [42, 125] and groups in a horizontal plane, one 3 group in a trans-posi- H H− [NiFeSe] complexes [141] have been suggested in recent tion relative to the 2 ligand in complex A and the ligand PH years. The frst fully functional [NiFe] hydrogenase mimic in complex B. As shown in Fig. 2, the 3 in trans-posi- H that can perform both 2 evolution and oxidation under tion, (complex A5 and B5, respectively) was systematically normal conditions was published by Ogo et al. [95]. The replaced in our calculations by 16 diferent ligands, (com- structure of this complex is characterized by triethylphos- plexes A1–A4, A6–A17 and complexes B1–B4, B7–B17, phite ligands attached to iron. Neutron-scattering analysis respectively) selected from the spectroscopic series [20, 121] revealed that in Ogo’s complex the hydride binds to the Fe and the trans efect series in transition metal complexes [17, and not to the Ni atom. 18, 41, 104] to cover a wide range of ligands with diferent Morokuma et al. [47] recently reported a detailed mecha- electronic character. The ligands were ordered according to nistic study of the electron/hydride transfer of Ogo’s [NiFe] their infuence of the H–H bond strength in complexes A, mimic. Figure 1 shows the catalytic cycle proposed by e.g., ligand L1 leads to complex A1 with the strongest H–H Morokuma and co-workers, which starts with the removal bond and ligand L17 to complex A17 with the weakest H–H of acetonitrile from Fe. The resulting [NiFe] complex can bond investigated in this work. H accommodate the binding of 2 to Fe (complex A). Complex Computational methods frequently determine the strength undergoes a heterolytic H–H bond cleavage with the help of a chemical bond via molecular orbital approaches [45, 58, A − of the Lewis base MeO , forming an intermediate hydride 81], dissociation energies [33, 71, 91], or energy decomposi- complex (complex B). The catalytic cycle completes with tion methods [83, 126]. However, these approaches provide hydride transfer from complex B. However, there are some more qualitative rather than quantitative results [25, 145]. important open questions with regard to the key factors Therefore, we used local vibrational force constants based determining the catalytic efciency, (1) how strong are the on the local mode analysis of Konkoli and Cremer [66, 144, Fe ⋯ H Fe ⋯ H− 2 interaction in complex A and the interac- 145] to quantitatively assess the intrinsic bond strength of tion in B; and (2) can the Fe ligands, in particular, the ligand the Fe–H and H–H bonds in complexes A1–A17 and that H H− in trans-position to 2 and infuence the strength of these of the Fe–H bond in complexes B1–B17. The local mode interactions; (3) can these ligands also infuence the strength analysis has been successfully applied to characterize cova- H of the H–H bond of 2 in complex A? This information can lent bonds [54, 74, 76, 78, 114, 120, 144] and weak chemical Fig. 1 Catalytic cycle of the MeCN 2+ [NiFe] hydrogenase mimic used N PH Me 3 H in study. This catalytic cycle is a N 2 NiII FeII PH3 modifed version of the catalytic C 2+ S N S L cycle proposed by Morokuma N PH3 Complex A et al. [47] being based on Ogo’s N PH P(OEt) NiII FeII 3 mimic (the three 3 groups S H 2+ L Hb of Ogo’s mimic were replaced S N PH PH Ha 3 with 3 ligands). Complex A N NiII FeII PH3 S and complex B, the focus of 2+ S L this work are shown in the red N H H PH3 boxes. a is the H atom closer N NiII FeII PH3 MeO- to Ni and forming the hydride S Me bond with Fe in complex B. For S L O + a defnition of ligands L, see Fig. 2 Hb N Ha e- Complex B PH3 N NiII FeII PH3 + S N Ha PH3 S L N NiII FeII PH3 S S L MeOH 1 3 Theoretical Chemistry Accounts (2019) 138:76 Page 3 of 18 76 Fig. 2 Defnition of ligands L used in this work for complexes A1– to the complex with the strongest and L17 to the complex with the A17 and B1–B17. The ligands are numbered according to decreas- weakest H–H bond ing H–H bond strength in complexes A1–A17, e.g., L1 corresponds interactions such as halogen [96, 98, 99], chalcogen [97, cc-pVTZ basis set [142] using an ultrafne integral grid [40]. 100, 118], pnicogen [115–117], and tetrel interactions [113] The efective performance of the BP86 functional for transi- as well as H bonding [35, 53, 55, 129]. Local vibrational tion metal complexes was discussed in a recent study of Bühl force constants could also clearly illustrate that a shorter and Kabrede [13] who showed that BP86 provides the best bond is not always a stronger bond [27, 67, 68, 74].
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