A Facially Coordinating Tris‐Benzimidazole Ligand for Nonheme Iron Enzyme Models

Gunasekera, Parami; Abhyankar, Preshit; MacMillan, Samantha N.; Lacy, David C.

doi:10.1002/ejic.202000984

Cited by 2 publications

(2 citation statements)

References 37 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Enzymatic systems and, in particular, metalloenzymes mediate a fascinating array of reactions via a carefully evolved secondary coordination sphere. Enzyme active sites leverage effects such as hydrogen bonding, electron transfer pathways, and electrostatic effects to precisely tune the reactivity of metallocofactors. ,,,− One example illustrating the importance of the secondary coordination sphere is in oxidase chemistry. For example, the terminal oxidant in cytochrome P450 enzymes, Compound I, consists of an Fe(IV)-oxo which is generated from O 2 via the delivery of proton and electron equivalents from cofactors and the protein superstructure.…”

Section: Introductionmentioning

confidence: 99%

Direct Aerobic Generation of a Ferric Hydroperoxo Intermediate Via a Preorganized Secondary Coordination Sphere

et al. 2021

View full text Add to dashboard Cite

Enzymes exert control over the reactivity of metal centers with precise tuning of the secondary coordination sphere of active sites. One particularly elegant illustration of this principle is in the controlled delivery of proton and electron equivalents in order to activate abundant but kinetically inert oxidants such as O 2 for oxidative chemistry. Chemists have drawn inspiration from biology in designing molecular systems where the secondary coordination sphere can shuttle protons or electrons to substrates. However, a biomimetic activation of O 2 requires the transfer of both protons and electrons, and molecular systems where ancillary ligands are designed to provide both of these equivalents are comparatively rare. Here, we report the use of a dihydrazonopyrrole (DHP) ligand complexed to Fe to perform exactly such a biomimetic activation of O 2 . In the presence of O 2 , this complex directly generates a high spin Fe(III)-hydroperoxo intermediate which features a DHP • ligand radical via ligand-based transfer of an H atom. This system displays oxidative reactivity and ultimately releases hydrogen peroxide, providing insight on how secondary coordination sphere interactions influence the evolution of oxidizing intermediates in Fe-mediated aerobic oxidations.

show abstract

Section: Introductionmentioning

confidence: 99%

Direct Aerobic Generation of a Ferric Hydroperoxo Intermediate Via a Preorganized Secondary Coordination Sphere

et al. 2021

View full text Add to dashboard Cite

show abstract

“…Enzyme active sites leverage effects such as hydrogen bonding, electron transfer pathways, and electrostatic effects to precisely tune the reactivity of metallocofactors. [1][2][3][4][5][6][7][8][9][10][11] One example illustrating the importance of the secondary coordination sphere is in oxidase chemistry. For example, the terminal oxidant in cytochrome P450 enzymes, Compound I, consists of an Fe(IV)-oxo which is generated from O2 via the delivery of proton and electron equivalents from cofactors and the protein superstructure.…”

Section: Enzymaticmentioning

confidence: 99%

Direct Aerobic Generation of a Ferric Hydroperoxo Intermediate via a Preorganized Secondary Coordination Sphere

Jesse

Anferov

Collins³

et al. 2021

Preprint

View full text Add to dashboard Cite

Enzymes exert control over the reactivity of metal centers with precise tuning of the secondary coordination sphere of active sites. One particularly elegant illustration of this principle is in the controlled delivery of proton and electron equivalents in order to activate abundant but kinetically inert oxidants such as O2 for oxidative chemistry. Chemists have drawn inspiration from biology in designing molecular systems where the secondary coordination sphere can shuttle protons or electrons to substrates. However, a biomimetic activation of O2 requires the transfer of both protons and electrons, and molecular systems where ancillary ligands are designed to provide both of these equivalents are comparatively rare. Here we report the use of a dihydrazonopyrrole (DHP) ligand complexed to Fe to perform exactly such a biomimetic activation of O2. In the presence of O2, this complex directly generates a high spin Fe(III)-hydroperoxo intermediate which features a DHP • ligand radical via ligand-based transfer of an H-atom. This system displays oxidative reactivity and ultimately releases hydrogen peroxide, providing insight on how secondary coordination sphere interactions influence the evolution of oxidizing intermediates in Fe-mediated aerobic oxidations.

show abstract

A Facially Coordinating Tris‐Benzimidazole Ligand for Nonheme Iron Enzyme Models

Cited by 2 publications

References 37 publications

Direct Aerobic Generation of a Ferric Hydroperoxo Intermediate Via a Preorganized Secondary Coordination Sphere

Direct Aerobic Generation of a Ferric Hydroperoxo Intermediate Via a Preorganized Secondary Coordination Sphere

Direct Aerobic Generation of a Ferric Hydroperoxo Intermediate via a Preorganized Secondary Coordination Sphere

Contact Info

Product

Resources

About