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Favorable Protonation of the (?-edt)[Fe(2)(PMe(3))(4)(CO)(2)(H-terminal)](+) Hydrogenase Model Complex Over Its Bridging ?-H Counterpart: A Spectroscopic and DFT Study.

ABSTRACT: The mechanism of hydrogen production in [FeFe] hydrogenase remains elusive. However, a species featuring a terminal hydride bound to the distal Fe is thought to be the key intermediate leading to hydrogen production. In this study, density functional theory (DFT) calculations on the terminal (H-term) and bridging (?-H) hydride isomers of (?-edt)-[Fe(2)(PMe(3))(4)(CO)(2)H](+) are presented in order to understand the factors affecting their propensity for protonation. Relative to H-term, ?-H is 12.7 kcal/mol more stable, which contributes to its decreased reactivity towards an acid. Potential energy surface (PES) calculations for the reaction of the H-term isomer with 4-nitropyridinium, a proton source, further reveal a lower activation energy barrier (14.5 kcal/mol) for H-term than for ?-H (29 kcal/mol). Besides these energetic considerations, the H-term isomer displays a key molecular orbital (MO <139>) that has a relatively strong hydride (1s) contribution (23%), which is not present in the ?-H isomer. This indicates a potential orbital control of the reaction of the hydride complexes with acid. The lower activation energy barrier and this key MO together control the overall catalytic activity of (?-edt)[Fe(2)(PMe(3))(4)(CO)(2)(H-term)](+). Lastly, Raman and IR spectroscopy were performed in order to probe the ?(Fe-H) stretching mode of the two isomers and their deuterated counterparts. A ?(Fe-H) stretching mode was observed for the ?-H complex at 1220 cm(-1). However, the corresponding mode is not observed for the less stable H-term isomer.

SUBMITTER: Galinato MG

PROVIDER: S-EPMC3498055 | biostudies-literature | 2011 Mar

REPOSITORIES: biostudies-literature

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Favorable Protonation of the (μ-edt)[Fe(2)(PMe(3))(4)(CO)(2)(H-terminal)](+) Hydrogenase Model Complex Over Its Bridging μ-H Counterpart: A Spectroscopic and DFT Study.

Galinato Mary Grace I MG Whaley C Matthew CM Roberts Dean D Wang Peng P Lehnert Nicolai N

European journal of inorganic chemistry 20110301 7

The mechanism of hydrogen production in [FeFe] hydrogenase remains elusive. However, a species featuring a terminal hydride bound to the distal Fe is thought to be the key intermediate leading to hydrogen production. In this study, density functional theory (DFT) calculations on the terminal (H-term) and bridging (μ-H) hydride isomers of (μ-edt)-[Fe(2)(PMe(3))(4)(CO)(2)H](+) are presented in order to understand the factors affecting their propensity for protonation. Relative to H-term, μ-H is 12 ...[more]

PMID: 23162378

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Project description:In the current work, we found aqueous enzyme phase reaction pathways for the reactivation of the exogenously inhibited [Fe-Fe]-hydrogenases by O2, or OH(-), which metabolizes to H2O(1,2). We used the hybrid quantum mechanics/molecular mechanics (QM/MM) method to study the reactivation pathways of the exogenously inhibited enzyme matrix. The ONIOM calculations performed on the enzyme agree with experimental results(3), i.e., wild-type [Fe-Fe]-hydrogenase H-cluster is inhibited by oxygen metabolites. An enzyme spherical region with a radius of 8 Å (from the distal iron, Fed) has been screened for residues that prevent H2O from leaving the catalytic site and reactivate the [Fe-Fe]-hydrogenase H-cluster. In the screening process, polar residues were removed, one at a time, and frequency calculations provided the change in the Gibbs' energy for the dissociation of water (due to their deletion). When residue deletion resulted in significant Gibbs' energy decrease, further residue substitutions have been carried out. Following each substitution, geometry optimization and frequency calculations have been performed to assess the change in the Gibbs' energy for the elimination H2O. Favorable thermodynamic results have been obtained for both single residue removal (?G?Glu(374) = -1.6 kcal/mol), single substitution (?GGlu(374)His = -3.1 kcal/mol), and combined residue substitutions (?GArg(111)Glu;Thr(145)Val;Glu(374)His;Tyr(375)Phe = -7.5 kcal/mol). Because the wild-type enzyme has only an endergonic step to overcome, i.e., for H2O removal, by eliminating several residues, one at a time, the endergonic step was made to proceed spontaneously. Thus, the most promising residue deletions which enhance H2O elimination are ?Arg(111), ?Thr(145), ?Ser(177), ?Glu(240), ?Glu(374), and ?Tyr(375). The thermodynamics and electronic structure analyses show that the bridging carbonyl (COb) of the H-cluster plays a concomitant role in the enzyme inhibition/reactivation. In gas phase, COb shifts towards Fed to compensate for the electron density donated to oxygen upon the elimination of H2O. However, this is not possible in the wild-type enzyme because the protein matrix hinders the displacement of COb towards Fed, which leads to enzyme inhibition. However, enzyme reactivation can be achieved by means of appropriate amino acid substitutions.

Project description:Research on simple [FeFe] hydrogenase model systems of type (mu-S(2)R)[Fe(CO)(3)](2) (R = C(2)H(4) (edt), C(3)H(6) (pdt)) which have been shown to function as robust electrocatalysts for proton reduction, provides a reference to understand the electronic and vibrational properties of the active site of [FeFe] hydrogenases and of more sophisticated model systems. In this study, the solution and solid state Raman spectra of (mu-edt)[Fe(CO)(3)](2) and of the corresponding (13)CO-labeled complex are presented and analyzed in detail, with focus on the nu(C=O) and nu(Fe-CO)/delta(Fe-C=O) vibrational regions. These regions are specifically important as vibrations involving CO ligands serve as probes for the "electron richness" of low-valent transition metal centers and the geometric structures of the complexes. The obtained vibrational spectra have been completely assigned in terms of the nu(C=O), nu(Fe-CO), and delta(Fe-C=O) modes, and the force constants of the important C=O and Fe-CO bonds have been determined using our Quantum Chemistry Centered Normal Coordinate Analysis (QCC-NCA). In the 400-650 cm(-1) region, fifteen mixed nu(Fe-CO)/delta(Fe-C=O) modes have been identified. The most prominent Raman peaks at 454, 456, and 483 cm(-1) correspond to a combination of nu(Fe-CO) stretching and delta(Fe-C=O) linear bending modes. The less intense peaks at 416 cm(-1) and 419 cm(-1) correspond to pure delta(Fe-C=O) linear bends. In the nu(C=O) region, the nu(C=O) normal modes at lower energy (1968 and 1964 cm(-1)) are almost pure equatorial (eq) nu(C=O)(eq) stretching vibrations, whereas the remaining four nu(C=O) normal modes show dominant (C=O)(eq) (2070 and 1961 cm(-1)) and (C=O)(ax) (2005 and 1979 cm(-1); ax = axial) contributions. Importantly, an inverse correlation between the f(C=O)(ax/eq) and f(Fe-CO)(ax/eq) force constants is obtained, in agreement with the idea that the Fe(I)-CO bond in these types of complexes is dominated by pi-backdonation. Compared to the reduced form of [FeFe] hydrogenase (H(red)), the nu(C=O) vibrational frequencies of (mu-edt)[Fe(CO)(3)](2) are higher in energy, indicating that the dinuclear iron core in (mu-edt)[Fe(CO)(3)](2) is less electron rich compared to H(red) in the actual enzyme. Finally, quantum yields for the photodecomposition of (mu-edt)[Fe(CO)(3)](2) have been determined.

Project description:Treatment of cis-Me2Fe(PMe3)4 with di-1,2-(E-2-(pyridin-2-yl)vinyl)benzene ((bdvp)H2), a tetradentate ligand precursor, afforded (bdvp)Fe(PMe3)2 (1-PMe3) and 2 equiv. CH4, via C-H bond activation. Similar treatments with tridentate ligand precursors PhCH 0000000000000000000000000000000000 0000000000000000000000000000000000 0000000000000000000000000000000000 0000000000000000000000000000000000 0000000000000000000000000000000000 0000000000000000000000000000000000 0000000000000000000000000000000000 0000000000000000000000000000000000 0000000000000000000000000000000000 0000000000000000000000000000000000 0000000000000000000000000000000000 0000000000000000000000000000000000 0000000000000000000000000000000000 0000000000000000000000000000000000 0000000000000000000000000000000000 1111111111111111111111111111111111 1111111111111111111111111111111111 0000000000000000000000000000000000 0000000000000000000000000000000000 0000000000000000000000000000000000 0000000000000000000000000000000000 1111111111111111111111111111111111 1111111111111111111111111111111111 0000000000000000000000000000000000 0000000000000000000000000000000000 0000000000000000000000000000000000 0000000000000000000000000000000000 0000000000000000000000000000000000 0000000000000000000000000000000000 0000000000000000000000000000000000 0000000000000000000000000000000000 0000000000000000000000000000000000 0000000000000000000000000000000000 0000000000000000000000000000000000 NCH2(E-CHCHPh) ((pipp)H2) and PhCHN(2-CCMe-Ph) ((pipa)H) under dinitrogen provided trans-(pipp)Fe(PMe3)2N2 (2) and trans-(pipvd)Fe(PMe3)2N2 (3), respectively; the latter via one C-H bond activation, and a subsequent insertion of the alkyne into the remaining Fe-Me bond. All three Fe(ii) vinyl species were protonated with H[BArF4] to form the corresponding Fe(iv) alkylidene cations, [(bavp)Fe(PMe3)2][BArF4] (4-PMe3), [(piap)Fe(PMe3)3][BArF4] (5), and [(pipad)Fe(PMe3)3][BArF4] (6). Mössbauer spectroscopic measurements on the formally Fe(ii) and Fe(iv) derivatives revealed isomer shifts within 0.1 mm s-1, reflecting the similarity in their bond distances.

Project description:The mixed-valence triiron complexes [Fe3(CO)7-x (PPh3) x (μ-edt)2] (x = 0-2; edt = SCH2CH2S) and [Fe3(CO)5(κ2-diphosphine)(μ-edt)2] (diphosphine = dppv, dppe, dppb, dppn) have been prepared and structurally characterized. All adopt an anti arrangement of the dithiolate bridges, and PPh3 substitution occurs at the apical positions of the outer iron atoms, while the diphosphine complexes exist only in the dibasal form in both the solid state and solution. The carbonyl on the central iron atom is semibridging, and this leads to a rotated structure between the bridged diiron center. IR studies reveal that all complexes are inert to protonation by HBF4·Et2O, but addition of acid to the pentacarbonyl complexes results in one-electron oxidation to yield the moderately stable cations [Fe3(CO)5(PPh3)2(μ-edt)2]+ and [Fe3(CO)5(κ2-diphosphine)(μ-edt)2]+, species which also result upon oxidation by [Cp2Fe][PF6]. The electrochemistry of the formally Fe(I)-Fe(II)-Fe(I) complexes has been investigated. Each undergoes a quasi-reversible oxidation, the potential of which is sensitive to phosphine substitution, generally occurring between 0.15 and 0.50 V, although [Fe3(CO)5(PPh3)2(μ-edt)2] is oxidized at -0.05 V. Reduction of all complexes is irreversible and is again sensitive to phosphine substitution, varying between -1.47 V for [Fe3(CO)7(μ-edt)2] and around -1.7 V for phosphine-substituted complexes. In their one-electron-reduced states, all complexes are catalysts for the reduction of protons to hydrogen, the catalytic overpotential being increased upon successive phosphine substitution. In comparison to the diiron complex [Fe2(CO)6(μ-edt)], [Fe3(CO)7(μ-edt)2] catalyzes proton reduction at 0.36 V less negative potentials. Electronic structure calculations have been carried out in order to fully elucidate the nature of the oxidation and reduction processes. In all complexes, the HOMO comprises an iron-iron bonding orbital localized between the two iron atoms not ligated by the semibridging carbonyl, while the LUMO is highly delocalized in nature and is antibonding between both pairs of iron atoms but also contains an antibonding dithiolate interaction.

Dataset Information

Favorable Protonation of the (?-edt)[Fe(2)(PMe(3))(4)(CO)(2)(H-terminal)](+) Hydrogenase Model Complex Over Its Bridging ?-H Counterpart: A Spectroscopic and DFT Study.

Publications

Favorable Protonation of the (μ-edt)[Fe(2)(PMe(3))(4)(CO)(2)(H-terminal)](+) Hydrogenase Model Complex Over Its Bridging μ-H Counterpart: A Spectroscopic and DFT Study.

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