Ligand Rearrangements at Fe/S Cofactors: Slow Isomerization of a Biomimetic [2Fe‐2S] Cluster

Bergner, Marie; Roy, Lisa; Dechert, Sebastian; Neese, Frank; Ye, Shengfa; Meyer, Franc

doi:10.1002/anie.201612621

Cited by 15 publications

(18 citation statements)

References 40 publications

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“…We describe bond strength in terms of bond orders, , also calculated by DFT (see Tables S6 and S9). More facile ligand exchange in [2Fe–2S] proteins is observed in weaker bonds . Consistently with the BOCs analysis, the Fe–N δ bond orders decreases (from 0.61 to 0.49, see Table S6) upon histidine protonation.…”

Section: Resultssupporting

confidence: 81%

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Molecular Dynamics Simulations of the [2Fe–2S] Cluster-Binding Domain of NEET Proteins Reveal Key Molecular Determinants That Induce Their Cluster Transfer/Release

et al. 2017

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The NEET proteins are a novel family of iron–sulfur proteins characterized by an unusual three cysteine and one histidine coordinated [2Fe–2S] cluster. Aberrant cluster release, facilitated by the breakage of the Fe–N bond, is implicated in a variety of human diseases, including cancer. Here, the molecular dynamics in the multi-microsecond timescale, along with quantum chemical calculations, on two representative members of the family (the human NAF-1 and mitoNEET proteins), show that the loss of the cluster is associated with a dramatic decrease in secondary and tertiary structure. In addition, the calculations provide a mechanism for cluster release and clarify, for the first time, crucial differences existing between the two proteins, which are reflected in the experimentally observed difference in the pH-dependent cluster reactivity. The reliability of our conclusions is established by an extensive comparison with the NMR data of the solution proteins, in part measured in this work.

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Section: Resultssupporting

confidence: 81%

“…More facile ligand exchange in [2Fe−2S] proteins is observed in weaker bonds. 66 Consistently with the BOCs analysis, the Fe−N δ bond orders decreases (from 0.61 to 0.49, see Table S6) upon histidine protonation. Similar results are also obtained for mNT (Tables S7−S9).…”

Section: Calculated Structural Features and Flexibility Of Naf-1 And ...supporting

confidence: 79%

Molecular Dynamics Simulations of the [2Fe–2S] Cluster-Binding Domain of NEET Proteins Reveal Key Molecular Determinants That Induce Their Cluster Transfer/Release

et al. 2017

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“…Many biomimetic [2Fe–2S] clusters have been investigated in order to gain information on their electronic structures and electron-transfer processes. − A few biomimetic [2Fe–2S] clusters supported by N,N-bidentate ligands have emerged recently (Chart ). Meyer and co-workers isolated and crystallographically characterized a series of [2Fe–2S] n + clusters ( n = 2, 1, 0) supported by two 2,2′-(phenylmethylene)bis(benzimidazolide) ligands. − Analogous [2Fe–2S] complexes have also shown proton-coupled electron-transfer reactivity. − Driess and Holland reported a series of [2Fe–2S] n + ( n = 2, 1, 0) clusters supported by β-diketiminate ligands. , Remarkably, the [2Fe–2S] + clusters with diethylphenyl-substituted β-diketiminato ligands CH[CMeN(2,6-Et 2 C 6 H 3 )] 2 are extensively delocalized, as suggested by the 57 Fe Mössbauer and X-ray absorption spectroscopy/X-ray emission spectroscopy spectroscopic data and density functional theory calculations .…”

Section: Introductionmentioning

confidence: 99%

[2Fe–2S] Cluster Supported by Redox-Active o-Phenylenediamide Ligands and Its Application toward Dinitrogen Reduction

et al. 2021

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As prevalent cofactors in living organisms, iron−sulfur clusters participate in not only the electron-transfer processes but also the biosynthesis of other cofactors. Many synthetic iron−sulfur clusters have been used in model studies, aiming to mimic their biological functions and to gain mechanistic insight into the related biological systems. The smallest [2Fe−2S] clusters are typically used for one-electron processes because of their limited capacity. Our group is interested in functionalizing small iron−sulfur clusters with redox-active ligands to enhance their electron storage capacity, because such functionalized clusters can potentially mediate multielectron chemical transformations. Herein we report the synthesis, structural characterization, and catalytic activity of a diferric [2Fe− 2S] cluster functionalized with two o-phenylenediamide ligands. The electrochemical and chemical reductions of such a cluster revealed rich redox chemistry. The functionalized diferric cluster can store up to four electrons reversibly, where the first two reduction events are ligand-based and the remainder metal-based. The diferric [2Fe−2S] cluster displays catalytic activity toward silylation of dinitrogen, affording up to 88 equiv of the amine product per iron center.

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“…Analogous studies on binuclear cores of iron are scare [14,15], whereas preparation of molecular model structures involves ligand exchange at a preformed [Fe2(µ-S)2] core [4,[16][17][18][19][20][21][22]. According to recent mechanistic work, the ligand environment and the overall oxidation state determine the structural dynamics of the [Fe2(µ-S)2] core, for which S = S 2− [23]. Gaining a quantitative understanding of the (dis)assembly of [M2(µ-S)2] sites is of fundamental interest.…”

Section: Introductionmentioning

confidence: 99%

Understanding Factors that Control the Structural (Dis)Assembly of Sulphur-Bridged Bimetallic Sites

et al. 2019

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Bimetallic structures of the general type [M2(µ-S)2] are omnipresent in nature, for biological function [M2(µ-S)2] sites interconvert between electronically distinct, but isostructural, forms. Different from structure-function relationships, the current understanding of the mechanism of formation and persistence of [M2(µ-S)2] sites is poorly developed. This work reports on bimetallic model compounds of nickel that interconvert between functional structures [Ni2(µ-S)2]+/2+ and isomeric congeners [2{κ-S–Ni}]2+/+, S = Aryl-S−, in which the nickel ions are geometrically independent. Interconversion of the two sets of structures was studied quantitatively by UV–VIS absorption spectroscopy and cyclic voltammetry. Assembly of the [Ni2(µ-S)2]+ core from [2{κ-S–Ni}]+ is thermodynamically and kinetically highly preferred over the disassembly of [Ni2(µ-S)2]2+ into [2{κ-S–Ni}]2+. Labile Ni-η2/3-bonding to aromatic π-systems of the primary thiophenol ligand is critical for modeling (dis)assembly processes. A phosphine coligand mimics the role of anionic donors present in natural sites that saturate metal coordination. Three parameters have been identified as critical for structure formation and persistence. These are, first, the stereoelectronic properties of the metals ions, second, the steric demand of the coligand, and, third, the properties of the dative bond between nickel and coligand. The energies of transition states connecting functional and precursor forms have been found to depend on these parameters.

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Ligand Rearrangements at Fe/S Cofactors: Slow Isomerization of a Biomimetic [2Fe‐2S] Cluster

Cited by 15 publications

References 40 publications

Molecular Dynamics Simulations of the [2Fe–2S] Cluster-Binding Domain of NEET Proteins Reveal Key Molecular Determinants That Induce Their Cluster Transfer/Release

Molecular Dynamics Simulations of the [2Fe–2S] Cluster-Binding Domain of NEET Proteins Reveal Key Molecular Determinants That Induce Their Cluster Transfer/Release

[2Fe–2S] Cluster Supported by Redox-Active o-Phenylenediamide Ligands and Its Application toward Dinitrogen Reduction

Understanding Factors that Control the Structural (Dis)Assembly of Sulphur-Bridged Bimetallic Sites

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