Synthesis, spectroscopic, and structural characterization of mixed thioether–benzimidazole copper complexes

Castillo, Iván; Sánchez-Eguía, Brenda N.; Martínez‐Alanis, Paulina R.; Ugalde‐Saldívar, Víctor M.; Flores-Álamo, Marcos

doi:10.1016/j.poly.2014.10.022

Cited by 9 publications

(1 citation statement)

References 46 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…[31] In the case of [( DMA N 3 S)Cu I ] + , the more negative value of À 470 mV vs Fc + /Fc is likely due to the strongly electron-donating p-Me 2 N-pyridyl groups. [32] For the benzimidazole-based L Ar , Me 2 L Ar and Me 2 L Me , [33,34] CV analysis afforded redox potentials of À 120, À 160 and À 180 [41] mV vs Fc + /Fc. Two trends become apparent from this set of complexes: i) N-methylation of the two benzimidazole donors results in a more negative potential on going from L Ar to Me 2 L Ar by 40 mV; ii) replacement of an S-aryl for an S-Me substituent results in a further negative shift by additional 20 mV.…”

Section: Electrochemical Propertiesmentioning

confidence: 99%

Thioether‐Containing Copper Complexes as PHM, DβM, and TβM Model Systems

Gómez‐Vidales

Castillo

2021

Eur J Inorg Chem

Self Cite

View full text Add to dashboard Cite

This minireview presents efforts of synthetic chemists to mimic the active site of the copper monooxygenase enzymes peptidylglycine α-hydroxylating monooxygenase (PHM), dopamine β-monooxygenase (DβM), and tyramine β-monooxygenase (TβM), all of which feature copper-thioether ligation in their resting states. These monooxygenases are involved in the initial activation of O 2 to generate neurotransmitters by the selective activation of CÀ H bonds of their corresponding substrates, resulting in subsequent hydroxylation. Attempts to emulate the N 2 S donor set provided by the two histidines and the methionine residues that coordinate to copper in the active site employ N 2 S and N 3 S-type ligands, with the latter ones providing the best conditions for testing the reactivity of their Cu I complexes with dioxygen. Identification of Cu II -superoxos as capable agents for CÀ H activation has provided support for these species as the key reactive intermediates in the enzymatic systems. Synthetic end-on [Cu II -η 1 -O 2 * À ] and side-on [Cu II -η 2 -O 2 * À ] cupric superoxos are capable of such transformations, which is related to the open question of whether the methionine Sdonor may act as a hemilabile ligand in biological systems.

show abstract

Section: Electrochemical Propertiesmentioning

confidence: 99%

Thioether‐Containing Copper Complexes as PHM, DβM, and TβM Model Systems

Gómez‐Vidales

Castillo

2021

Eur J Inorg Chem

Self Cite

View full text Add to dashboard Cite

show abstract

Hemilabile Thio– and Selenoethers in Bis(benzimidazolyl)Amine Copper Complexes Relevant to the Active Sites of Copper‐Dependent Monooxygenases

Sánchez‐Eguía,

Hernández‐Toledo,

Lidin

et al. 2024

ChemCatChem

View full text Add to dashboard Cite

Copper complexes supported by benzimidazole‐based tetradentate neutral ligands featuring thio‐ and selenoether donors, resemble the coordination environment of the active site in copper dependent monooxygenases Dopamine‐β‐monooxygenase (DßM) and peptidylglycine‐α‐hydroxylating monooxygenase (PHM). The cuprous complexes react with O2 at low temperature generating a reactive copper‐oxygen species assigned to a side‐on cupric‐superoxo complex, which activates the C‐H bond of dihydroanthracene. Based on structural, 1H and 77Se NMR, and EPR spectroscopic characterization together with DFT computations, the selenoether moiety likely acts as a hemilabile ligand in these scaffolds, which results in an electrophilic cupric‐superoxide intermediate poised for H‐atom transfer, as has been proposed for related bis(benzimidazole)‐thioether analogues and selenoether‐modified enzymatic systems.

show abstract