Oxidative decarboxylation of tris-(p-carboxyltetrathiaaryl)methyl radical EPR probes by peroxidases and related hemeproteins: Intermediate formation and characterization of the corresponding cations

Decroos, Christophe; Li, Yun; Soltani, Asma; Frapart, Yves-Michel; Mansuy, Daniel; Boucher, Jean‐Luc

doi:10.1016/j.abb.2010.07.002

Cited by 29 publications

(51 citation statements)

References 35 publications

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“…The crude product was composed of the known trityl 11 and asymmetrical monosubstituted trityl 15 , which was easily detectable by the characteristic hyperfine splitting in the ESR spectrum, that is, a quartet and broad triplet, respectively (see Supporting Information). Trityls 11 and 15 were isolated in 47% and 42% yields, respectively, and their ratio was close to the predicted 1:1 ratio (see Scheme 5 for a summary of the arguments stated above and the literature data [19,20] ).…”

Section: Resultssupporting

confidence: 83%

“…Very recently C. Decroos et al reported the formation of trityl radicals through an electron transfer (ET) reaction between intermediate methylenecyclohexa-2,5-dienes and trityl cations, which were generated in situ by oxidation of trityl 5 either by potassium hexachloroiridate(IV) [19] or hydrogen peroxide in the presence of peroxidases (horse radish peroxidase, lactoperoxidase, prostaglandin synthase, and other hemeproteins). [20] …”

Section: Resultsmentioning

confidence: 99%

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Generation of Trityl Radicals by Nucleophilic Quenching of Tris(2,3,5,6‐tetrathiaaryl)methyl Cations and Practical and Convenient Large‐Scale Synthesis of Persistent Tris(4‐carboxy‐2,3,5,6‐tetrathiaaryl)methyl Radical

et al. 2013

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Tris(2,3,5,6-tetrathiaaryl)methyl cations, which were generated from the corresponding triarylmethanols in the presence of strong acids, underwent reaction with nucleophiles to give trityl radicals, as the product of a one-electron reduction of the carbocation. Depending on the nature of the nucleophile, the only byproducts were either diamagnetic quinone methides or asymmetrical monosubstituted trityl radicals. Herein, we report a protocol for the large-scale synthesis of the Finland trityl, which has the advantage of high overall yield and reproducibility.

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Section: Resultssupporting

confidence: 83%

Section: Resultsmentioning

confidence: 99%

Generation of Trityl Radicals by Nucleophilic Quenching of Tris(2,3,5,6‐tetrathiaaryl)methyl Cations and Practical and Convenient Large‐Scale Synthesis of Persistent Tris(4‐carboxy‐2,3,5,6‐tetrathiaaryl)methyl Radical

et al. 2013

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“…While intensive efforts have focused on the functionality of these trityl radicals (as mentioned above) as well as the synthesis of their analogues, 23–25 few studies have been performed to characterize the interaction of trityl radicals with biological macromolecules. 26,27 …”

Section: Introductionmentioning

confidence: 99%

Characterization of the binding of the Finland trityl radical with bovine serum albumin

Song

Liu

et al. 2014

RSC Adv.

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Understanding the interactions of trityl radicals with proteins is required to expand their biomedical applications. In this work, we demonstrate that the Finland trityl radical CT-03 binds to bovine serum albumin (BSA) in aqueous solution. Upon binding with BSA, CT-03 exhibits a much broader electron paramagnetic resonance (EPR) signal and this line broadening can be reversed by proteolysis of the BSA. The binding induces a red-shift of the maximal UV-Vis absorbance wavelength of CT-03 around 470 nm, likely due to localization of CT-03 in the relatively hydrophobic region of the protein. The interaction between CT-03 and BSA is driven by a hydrophobic interaction with an estimated binding constant of 2.18 ×105 M−1 at 298 K. Furthermore, only one CT-03 is bound to each molecule of BSA and the binding site is determined to be the sub-domain IIA (Sudlow’s site I). This protein binding of the trityl probe to albumin can be used to study the structure and function of albumin and also must be considered for its use as an in vivo imaging agent or spin label.

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“…Recent study of the metabolism of CT-03 has shown that the EPR signal can decay due to reduction of the radical under anaerobic conditions [15] by liver microsomes followed by protonation of the anion or by oxidation to cation by some peroxidases or related hemeproteins [16]. The resulting cation can subsequently react with C-, S-, -P or N- nucleophiles [17, 18].…”

mentioning

confidence: 99%

Poly-arginine conjugated triarylmethyl radical as intracellular spin label

Driesschaert

Bobko

Eubank

et al. 2016

Bioorganic & Medicinal Chemistry Letters

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Oxidative decarboxylation of tris-(p-carboxyltetrathiaaryl)methyl radical EPR probes by peroxidases and related hemeproteins: Intermediate formation and characterization of the corresponding cations

Cited by 29 publications

References 35 publications

Generation of Trityl Radicals by Nucleophilic Quenching of Tris(2,3,5,6‐tetrathiaaryl)methyl Cations and Practical and Convenient Large‐Scale Synthesis of Persistent Tris(4‐carboxy‐2,3,5,6‐tetrathiaaryl)methyl Radical

Generation of Trityl Radicals by Nucleophilic Quenching of Tris(2,3,5,6‐tetrathiaaryl)methyl Cations and Practical and Convenient Large‐Scale Synthesis of Persistent Tris(4‐carboxy‐2,3,5,6‐tetrathiaaryl)methyl Radical

Characterization of the binding of the Finland trityl radical with bovine serum albumin

Poly-arginine conjugated triarylmethyl radical as intracellular spin label

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