Dataset Information

Rational Design of Azothiophenes-Substitution Effects on the Switching Properties.

ABSTRACT: A series of substituted azothiophenes was prepared and investigated toward their isomerization behavior. Compared to azobenzene (AB), the presented compounds showed red-shifted absorption and almost quantitative photoisomerization to their (Z) states. Furthermore, it was found that electron-withdrawing substitution on the phenyl moiety increases, while electron-donating substitution decreases the thermal half-lives of the (Z)-isomers due to higher or lower stabilization by a lone pair-? interaction. Additionally, computational analysis of the isomerization revealed that a pure singlet state transition state is unlikely in azothiophenes. A pathway via intersystem crossing to a triplet energy surface of lower energy than the singlet surface provided a better fit with experimental data of the (Z)?(E) isomerization. The insights gained in this study provide the necessary guidelines to design effective thiophenylazo-photoswitches for applications in photopharmacology, material sciences, or solar energy harvesting applications.

SUBMITTER: Heindl AH

PROVIDER: S-EPMC7702042 | biostudies-literature | 2020 Oct

REPOSITORIES: biostudies-literature

ACCESS DATA

Publications

Rational Design of Azothiophenes-Substitution Effects on the Switching Properties.

Heindl Andreas H AH Wegner Hermann A HA

Chemistry (Weinheim an der Bergstrasse, Germany) 20200924 60

A series of substituted azothiophenes was prepared and investigated toward their isomerization behavior. Compared to azobenzene (AB), the presented compounds showed red-shifted absorption and almost quantitative photoisomerization to their (Z) states. Furthermore, it was found that electron-withdrawing substitution on the phenyl moiety increases, while electron-donating substitution decreases the thermal half-lives of the (Z)-isomers due to higher or lower stabilization by a lone pair-π interact ...[more]

PMID: 32330338

Similar Datasets

Project description:The M centers of the mononuclear monooxygenases peptidylglycine monooxygenase (PHM) and dopamine β-monooxygenase bind and activate dioxygen en route to substrate hydroxylation. Recently, we reported the rational design of a protein-based model in which the CusF metallochaperone was repurposed via a His to Met mutation to act as a structural and spectroscopic biomimic. The PHM M site exhibits a number of unusual attributes, including a His2Met ligand set, a fluxional Cu(I)-S(Met) bond, tight binding of exogenous ligands CO and N3-, and complete coupling of oxygen reduction to substrate hydroxylation even at extremely low turnover rates. In particular, mutation of the Met ligand to His completely eliminates the catalytic activity despite the propensity of CuI-His3 centers to bind and activate dioxygen in other metalloenzyme systems. Here, we further develop the CusF-based model to explore methionine variants in which Met is replaced by selenomethionine (SeM) and histidine. We examine the effects on coordinate structure and exogenous ligand binding via X-ray absorption spectroscopy and electron paramagnetic resonance and probe the consequences of mutations on redox chemistry via studies of the reduction by ascorbate and oxidation via molecular oxygen. The M-site model is three-coordinate in the Cu(I) state and binds CO to form a four-coordinate carbonyl. In the oxidized forms, the coordination changes to tetragonal five-coordinate with a long axial Met ligand that like the enzymes is undetectable at either the Cu or Se K edges. The EXAFS data at the Se K edge of the SeM variant provide unique information about the nature of the Cu-methionine bond that is likewise weak and fluxional. Kinetic studies document the sluggish reactivity of the Cu(I) complexes with molecular oxygen and rapid rates of reduction of the Cu(II) complexes by ascorbate, indicating a remarkable stability of the Cu(I) state in all three derivatives. The results show little difference between the Met ligand and its SeM and His congeners and suggest that the Met contributes to catalysis in ways that are more complex than simple perturbation of the redox chemistry. Overall, the results stimulate a critical re-examination of the canonical reaction mechanisms of the mononuclear copper monooxygenases.

Dataset Information

Rational Design of Azothiophenes-Substitution Effects on the Switching Properties.

Publications

Rational Design of Azothiophenes-Substitution Effects on the Switching Properties.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

Tweets