Dataset Information

Facile C=O Bond Splitting of Carbon Dioxide Induced by Metal-Ligand Cooperativity in a Phosphinine Iron(0) Complex.

ABSTRACT: New iron complexes [Cp*FeL]^- (1-? and 1-?, Cp*=C₅ Me₅ ) containing the chelating phosphinine ligand 2-(2'-pyridyl)-4,6-diphenylphosphinine (L) have been prepared, and found to undergo facile reaction with CO₂ under ambient conditions. The outcome of this reaction depends on the coordination mode of the versatile ligand L. Interaction of CO₂ with the isomer 1-?, in which L binds to Fe through the phosphinine moiety in an ?⁵ fashion, leads to the formation of 3-?, in which CO₂ has undergone electrophilic addition to the phosphinine group. In contrast, interaction with 1-?-in which L acts as a ?-chelating [P,N] ligand-leads to product 3-? in which one C=O bond has been completely broken. Such CO₂ cleavage reactions are extremely rare for late 3d metals, and this represents the first such example mediated by a single Fe centre.

SUBMITTER: Leitl J

PROVIDER: S-EPMC6856682 | biostudies-literature | 2019 Oct

REPOSITORIES: biostudies-literature

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Publications

Facile C=O Bond Splitting of Carbon Dioxide Induced by Metal-Ligand Cooperativity in a Phosphinine Iron(0) Complex.

Leitl Julia J Marquardt Michael M Coburger Peter P Scott Daniel J DJ Streitferdt Verena V Gschwind Ruth M RM Müller Christian C Wolf Robert R

Angewandte Chemie (International ed. in English) 20190913 43

New iron complexes [Cp*FeL]- (1-σ and 1-π, Cp*=C5 Me5 ) containing the chelating phosphinine ligand 2-(2'-pyridyl)-4,6-diphenylphosphinine (L) have been prepared, and found to undergo facile reaction with CO2 under ambient conditions. The outcome of this reaction depends on the coordination mode of the versatile ligand L. Interaction of CO2 with the isomer 1-π, in which L binds to Fe through the phosphinine moiety in an η5 fashion ...[more]

PMID: 31441566

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Project description:Aspartate carbamoyltransferase (ATCase) is a large dodecameric enzyme with six active sites that exhibits allostery: its catalytic rate is modulated by the binding of various substrates at distal points from the active sites. A recently developed method, bond-to-bond propensity analysis, has proven capable of predicting allosteric sites in a wide range of proteins using an energy-weighted atomistic graph obtained from the protein structure and given knowledge only of the location of the active site. Bond-to-bond propensity establishes if energy fluctuations at given bonds have significant effects on any other bond in the protein, by considering their propagation through the protein graph. In this work, we use bond-to-bond propensity analysis to study different aspects of ATCase activity using three different protein structures and sources of fluctuations. First, we predict key residues and bonds involved in the transition between inactive (T) and active (R) states of ATCase by analysing allosteric substrate binding as a source of energy perturbations in the protein graph. Our computational results also indicate that the effect of multiple allosteric binding is non linear: a switching effect is observed after a particular number and arrangement of substrates is bound suggesting a form of long range communication between the distantly arranged allosteric sites. Second, cooperativity is explored by considering a bisubstrate analogue as the source of energy fluctuations at the active site, also leading to the identification of highly significant residues to the T???R transition that enhance cooperativity across active sites. Finally, the inactive (T) structure is shown to exhibit a strong, non linear communication between the allosteric sites and the interface between catalytic subunits, rather than the active site. Bond-to-bond propensity thus offers an alternative route to explain allosteric and cooperative effects in terms of detailed atomistic changes to individual bonds within the protein, rather than through phenomenological, global thermodynamic arguments.

Dataset Information

Facile C=O Bond Splitting of Carbon Dioxide Induced by Metal-Ligand Cooperativity in a Phosphinine Iron(0) Complex.

Publications

Facile C=O Bond Splitting of Carbon Dioxide Induced by Metal-Ligand Cooperativity in a Phosphinine Iron(0) Complex.

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