Structural characterization of gas-phase cysteine and cysteine methyl ester complexes with zinc and cadmium dications by infrared multiple photon dissociation spectroscopy

Coates, Rebecca A.; McNary, Christopher P.; Boles, Georgia C.; Berden, Giel; Armentrout, P. B.

doi:10.1039/c5cp01500f

Cited by 39 publications

(91 citation statements)

References 42 publications

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“…The unambiguous and detailed characterization of the structural and dynamic behavior of these transient intermediates in isolated environments, in which external interferences are absent, will help to reveal intrinsic properties relevant to their biological activity. The inherent bonding and conformational features of cysteine in its (de)protonated, nitrosated, and metal‐tagged forms have been previously interrogated both in the free amino acid and in the residue embodied in the glutathione peptide by a joint computational and experimental infrared multiple photon dissociation (IRMPD) assay. IRMPD spectroscopy, coupled with ESI tandem mass spectrometry (MS/MS), is a pivotal tool to provide direct structural clues about gaseous (bio)molecular ions, including (de)protonation site, metal‐binding patterns, and local intramolecular interactions in both native and modified amino acids and peptides, DNA/RNA bases and nucleotides, cluster ions, and fragmentation products …”

Section: Introductionmentioning

confidence: 99%

“…[18] Recently,avariety of mass spectrometric studies have been able to identify the reactive intermediates formed by (interfacial) ozonolysis of deprotonated cysteineatthe air-liquid interface, [5,19] to probe the stability and fragmentation behavior of intact and modified sulfinyl radical ions, [20,21] and elucidate the intrinsic mechanism involved in the formationo fc ysteine oxo forms [cysSO x ] À (x = 1, 2, 3) and sulfenate radicala nions in the gas phase. [22] The unambiguous and detailed characterization of the structurala nd dynamic behavior of theset ransient intermediates in isolated environments, in which external interferences are absent,w ill help to reveali ntrinsic properties rele-vant to their biological activity.T he inherentb onding and conformationalf eatureso fc ysteine in its (de)protonated, [23,24] nitrosated, [25] and metal-tagged [26] forms have been previously interrogated both in the free amino acid and in the residue embodied in the glutathione peptide [27] by aj oint computational and experimental infrared multiple photon dissociation (IRMPD) assay.I RMPD spectroscopy,c oupled with ESI tandem mass spectrometry (MS/MS), is ap ivotalt ool to provide direct structural clues about gaseous (bio)molecular ions, [28][29][30][31][32][33] including (de)protonations ite, metal-binding patterns,a nd local intramolecular interactions in both native and modified amino acids and peptides, [34][35][36][37][38][39][40][41][42] DNA/RNA bases and nucleotides, [43][44][45] cluster ions, [46] and fragmentation products. [47] We now examine the intrinsic chemical properties and geometric features of the conjugate bases of cysteine sulfenic, sulfinic, and sulfonica cids, [cysSO x ] À (x = 1, 2, 3), by meanso fE SI/ MS-IRMPD spectroscopy in the highly informativem id-IR spectral range (750-1900 cm À1 )i nc ombination with ab initio...…”

Section: Introductionmentioning

confidence: 99%

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Amino Acid Oxidation: A Combined Study of Cysteine Oxo Forms by IRMPD Spectroscopy and Simulations

Scuderi

Bodo

Chiavarino

et al. 2016

Chemistry A European J

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The redox activity of cysteine sulfur allows numerous post-translational protein modifications involved in the oxidative regulation of metabolism, in metal binding, and in signal transduction. A combined approach based on infrared multiple photon dissociation spectroscopy at the Centre Laser Infrarouge d'Orsay (CLIO) free electron laser facility, calculations of IR frequencies, and finite temperature ab initio molecular dynamics simulations has been employed to characterize the gas-phase structures of deprotonated cysteine sulfenic, sulfinic, and sulfonic acids, [cysSO ] (x=1, 2, 3, representing the number of S-bound oxygen atoms), which are key intermediates in the redox-switching chemistry of proteins. The ions show different structural motifs owing to preferential binding of the proton to either the carboxylate or sulfur-containing group. Due to the decreasing basicity of the sulfenic, sulfinic, and sulfonic terminals, the proton bound to SO in [cysSO] migrates to the carboxylate in [cysSO ] , whereas it turns out to be shared in [cysSO ] . Evidence is gathered that a mixture of close-lying low-energy conformers is sampled for each cysteine oxo form in a Paul ion trap at room temperature.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Amino Acid Oxidation: A Combined Study of Cysteine Oxo Forms by IRMPD Spectroscopy and Simulations

Scuderi

Bodo

Chiavarino

et al. 2016

Chemistry A European J

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show abstract

“…Peptide/amino acid metal ion binding using model systems has been studied in the literature (including using ESI MS; Coates et al ., , ). Based on interactions with 2 and 4, it is speculated that sulphur atoms in sulfoxide molecules were able to form more effective bonds with metal ions.…”

Section: Resultsmentioning

confidence: 99%

“…Peptide/amino acid metal ion binding using model systems has been studied in the literature (including using ESI MS;Coates et al, 2015Coates et al, , 2016. Based on Characterisation of metal binding linusorbs in flaxseed P. D. Jadhav et al…”

Section: Comparison Of Binding Ability Between 1 3 Andmentioning

confidence: 99%

Metal binding novel flaxseed peptides (linusorbs)

Jadhav

Zuo

Shim

et al. 2018

Int J of Food Sci Tech

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Summary Linusorbs (LOs; a.k.a. cyclolinopeptides) are naturally occurring orbitides derived from flaxseed. These compounds consist of 8–10 amino acid residues, which are linked via an N‐ to C‐terminal peptide bond with molecular masses of approximately 1 kDa. The LO circular structure makes them candidates for metal binding studies. Flaxseed extracts are known to suppress Pb and Cd toxicity. Hence, four metal salts surveyed include Zn(CH3COO)2, ZnSO4, Pb(CH3COO)2 and Cd(NO3)2 with pure LOs 1–5. Proton NMR spectra indicated interaction of LOs with metal salts in solution and were used to determine impacts of methionine oxidation on interactions with metal ions. The methyl group of methionine S,S‐dioxide of related LOs did not show the same shift in the presence of Zn(CH3COO)2 and Pb(CH3COO)2 observed in their methionine S‐oxide analogues. Metal complexes were observed forming at 10−2 m to 10−4 m but not at lower concentrations (10−5 m to 10−8 m). Mass spectrometry data confirmed that metal binding strength varied by metal in the order Zn(CH3COO)2

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“…Recently, Armentrout's group studied complexes of Zn 2+ and Cd 2+ with deprotonated Cys, [Cys‐H+M] + , by IRMPD spectroscopy . Whereas the [Cys‐H+Zn] + and [Cys‐H+Cd] + complexes, deprotonated at sulfur, have closed‐shell electronic structures with formal M 2+ /S − interactions, their geometric features are remarkably similar to those of the open‐shell radical cations [Cys‐H+M] .+ , in which there is formally an M + /S .…”

Section: Resultsmentioning

confidence: 99%

Cysteine Radical/Metal Ion Adducts: A Gas‐Phase Structural Elucidation and Reactivity Study

et al. 2016

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The formation and investigation of sulfur‐based cysteine radicals cationized by a group 1A metal ion or Ag+ in the gas phase are reported. Gas‐phase ion–molecule reactions (IMR) and infrared multiple‐photon dissociation (IRMPD) spectroscopy revealed that the Li+, Na+, and K+ adducts of the cysteine radical remain S‐based radicals as initially formed. Theoretical calculations for the three alkali metal ions found that the lowest‐energy isomers are Cα‐based radicals, but they are not observed experimentally owing to the barriers associated with the hydrogen‐atom transfer. A mechanism for the S‐to‐Cα radical rearrangement in the metal ion complexes was proposed, and the relative energies of the associated energy barriers were found to be Li+>Na+>K+ at all levels of theory. Relative to the B3LYP functional, other levels of calculation gave significantly higher barriers (by 35–40 kJ mol−1 at MP2 and 44–47 kJ mol−1 at the CCSD level) using the same basis set. Unlike the alkali metal adducts, the cysteine radical/Ag+ complex rearranged from the S‐based radical to an unreactive species as indicated by IMRs and IRMPD spectroscopy. This is consistent with the Ag+/cysteine radical complex having a lower S‐to‐Cα radical conversion barrier, as predicted by the MP2 and CCSD levels of theory.

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Structural characterization of gas-phase cysteine and cysteine methyl ester complexes with zinc and cadmium dications by infrared multiple photon dissociation spectroscopy

Cited by 39 publications

References 42 publications

Amino Acid Oxidation: A Combined Study of Cysteine Oxo Forms by IRMPD Spectroscopy and Simulations

Amino Acid Oxidation: A Combined Study of Cysteine Oxo Forms by IRMPD Spectroscopy and Simulations

Metal binding novel flaxseed peptides (linusorbs)

Cysteine Radical/Metal Ion Adducts: A Gas‐Phase Structural Elucidation and Reactivity Study

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