Cyclometalated AuIII Complexes for Cysteine Arylation in Zinc Finger Protein Domains: towards Controlled Reductive Elimination
With the aim of exploiting the use of organometallic species for the efficient modification of proteins through C‐atom transfer, the gold‐mediated cysteine arylation through a reductive elimination process occurring from the reaction of cyclometalated AuIII C^N complexes with a zinc finger peptide (...
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| Published in | Chemistry : a European journal Vol. 25; no. 32; pp. 7628 - 7634 |
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| Main Authors | , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
Weinheim
Wiley Subscription Services, Inc
07.06.2019
John Wiley and Sons Inc |
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| Abstract | With the aim of exploiting the use of organometallic species for the efficient modification of proteins through C‐atom transfer, the gold‐mediated cysteine arylation through a reductive elimination process occurring from the reaction of cyclometalated AuIII C^N complexes with a zinc finger peptide (Cys2His2 type) is here reported. Among the four selected AuIII cyclometalated compounds, the [Au(CCON)Cl2] complex featuring the 2‐benzoylpyridine (CCON) scaffold was identified as the most prone to reductive elimination and Cys arylation in buffered aqueous solution (pH 7.4) at 37 °C by high‐resolution LC electrospray ionization mass spectrometry. DFT and quantum mechanics/molecular mechanics (QM/MM) studies permitted to propose a mechanism for the title reaction that is in line with the experimental results. Overall, the results provide new insights into the reactivity of cytotoxic organogold compounds with biologically important zinc finger domains and identify initial structure–activity relationships to enable AuIII‐catalyzed reductive elimination in aqueous media.
The mechanism of cysteine arylation of zinc finger protein domains by cyclometalated AuIII C^N complexes was studied by using mass spectrometry and DFT methods. |
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| AbstractList | With the aim of exploiting the use of organometallic species for the efficient modification of proteins through C‐atom transfer, the gold‐mediated cysteine arylation through a reductive elimination process occurring from the reaction of cyclometalated Au
III
C^N complexes with a zinc finger peptide (Cys
2
His
2
type) is here reported. Among the four selected Au
III
cyclometalated compounds, the [Au(C
CO
N)Cl
2
] complex featuring the 2‐benzoylpyridine (C
CO
N) scaffold was identified as the most prone to reductive elimination and Cys arylation in buffered aqueous solution (pH 7.4) at 37 °C by high‐resolution LC electrospray ionization mass spectrometry. DFT and quantum mechanics/molecular mechanics (QM/MM) studies permitted to propose a mechanism for the title reaction that is in line with the experimental results. Overall, the results provide new insights into the reactivity of cytotoxic organogold compounds with biologically important zinc finger domains and identify initial structure–activity relationships to enable Au
III
‐catalyzed reductive elimination in aqueous media. With the aim of exploiting the use of organometallic species for the efficient modification of proteins through C-atom transfer, the gold-mediated cysteine arylation through a reductive elimination process occurring from the reaction of cyclometalated AuIII C^N complexes with a zinc finger peptide (Cys2 His2 type) is here reported. Among the four selected AuIII cyclometalated compounds, the [Au(CCO N)Cl2 ] complex featuring the 2-benzoylpyridine (CCO N) scaffold was identified as the most prone to reductive elimination and Cys arylation in buffered aqueous solution (pH 7.4) at 37 °C by high-resolution LC electrospray ionization mass spectrometry. DFT and quantum mechanics/molecular mechanics (QM/MM) studies permitted to propose a mechanism for the title reaction that is in line with the experimental results. Overall, the results provide new insights into the reactivity of cytotoxic organogold compounds with biologically important zinc finger domains and identify initial structure-activity relationships to enable AuIII -catalyzed reductive elimination in aqueous media.With the aim of exploiting the use of organometallic species for the efficient modification of proteins through C-atom transfer, the gold-mediated cysteine arylation through a reductive elimination process occurring from the reaction of cyclometalated AuIII C^N complexes with a zinc finger peptide (Cys2 His2 type) is here reported. Among the four selected AuIII cyclometalated compounds, the [Au(CCO N)Cl2 ] complex featuring the 2-benzoylpyridine (CCO N) scaffold was identified as the most prone to reductive elimination and Cys arylation in buffered aqueous solution (pH 7.4) at 37 °C by high-resolution LC electrospray ionization mass spectrometry. DFT and quantum mechanics/molecular mechanics (QM/MM) studies permitted to propose a mechanism for the title reaction that is in line with the experimental results. Overall, the results provide new insights into the reactivity of cytotoxic organogold compounds with biologically important zinc finger domains and identify initial structure-activity relationships to enable AuIII -catalyzed reductive elimination in aqueous media. With the aim of exploiting the use of organometallic species for the efficient modification of proteins through C‐atom transfer, the gold‐mediated cysteine arylation through a reductive elimination process occurring from the reaction of cyclometalated AuIII C^N complexes with a zinc finger peptide (Cys2His2 type) is here reported. Among the four selected AuIII cyclometalated compounds, the [Au(CCON)Cl2] complex featuring the 2‐benzoylpyridine (CCON) scaffold was identified as the most prone to reductive elimination and Cys arylation in buffered aqueous solution (pH 7.4) at 37 °C by high‐resolution LC electrospray ionization mass spectrometry. DFT and quantum mechanics/molecular mechanics (QM/MM) studies permitted to propose a mechanism for the title reaction that is in line with the experimental results. Overall, the results provide new insights into the reactivity of cytotoxic organogold compounds with biologically important zinc finger domains and identify initial structure–activity relationships to enable AuIII‐catalyzed reductive elimination in aqueous media. With the aim of exploiting the use of organometallic species for the efficient modification of proteins through C‐atom transfer, the gold‐mediated cysteine arylation through a reductive elimination process occurring from the reaction of cyclometalated AuIII C^N complexes with a zinc finger peptide (Cys2His2 type) is here reported. Among the four selected AuIII cyclometalated compounds, the [Au(CCON)Cl2] complex featuring the 2‐benzoylpyridine (CCON) scaffold was identified as the most prone to reductive elimination and Cys arylation in buffered aqueous solution (pH 7.4) at 37 °C by high‐resolution LC electrospray ionization mass spectrometry. DFT and quantum mechanics/molecular mechanics (QM/MM) studies permitted to propose a mechanism for the title reaction that is in line with the experimental results. Overall, the results provide new insights into the reactivity of cytotoxic organogold compounds with biologically important zinc finger domains and identify initial structure–activity relationships to enable AuIII‐catalyzed reductive elimination in aqueous media. The mechanism of cysteine arylation of zinc finger protein domains by cyclometalated AuIII C^N complexes was studied by using mass spectrometry and DFT methods. |
| Author | Bonsignore, Riccardo Casini, Angela Barone, Giampaolo Wenzel, Margot N. Thomas, Sophie R. Bourissou, Didier |
| AuthorAffiliation | 2 CNRS/Université Paul Sabatier Laboratoire Hétérochimie Fondamentale et Appliquée (LHFA, UMR 5069) 118 Route de Narbonne 31062 Toulouse Cedex 09 France 1 School of Chemistry Cardiff University Main Building, Park Place CF10 3AT Cardiff UK 3 Dipartimento di Scienze e Tecnologie Biologiche, Chimiche e Farmaceutiche Università di Palermo Viale delle Scienze, Edificio 17 90128 Palermo Italy |
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| SubjectTerms | Aqueous solutions catalysis Chemistry Communication Communications Cysteine cysteine arylation Cytotoxicity Gold gold complexes Ionization Ions Mass spectrometry Mass spectroscopy Proteins Quantum mechanics reductive elimination Zinc Zinc finger proteins |
| Title | Cyclometalated AuIII Complexes for Cysteine Arylation in Zinc Finger Protein Domains: towards Controlled Reductive Elimination |
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