Conformation of reduced glutathione in aqueous solution by 1H and 13C n.m.r.

York, Michael J.; Beilharz, Georg R.; Kuchel, Philip W.

doi:10.1111/j.1399-3011.1987.tb02294.x

Cited by 31 publications

(17 citation statements)

References 30 publications

(4 reference statements)

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“…In the representative structures we did not obtain any intramolecular hydrogen bonds, except the interaction between the protonated amine and the deprotonated caboxyl group in the γ-glutamic acid (GGL) residue. Furthermore, the representative structures of GSH are in good agreement with the conformations obtained previously by NMR and MD studies [17]–[21].…”

Section: Resultssupporting

confidence: 87%

Glutathione – Hydroxyl Radical Interaction: A Theoretical Study on Radical Recognition Process

et al. 2013

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Non-reactive, comparative (2×1.2 μs) molecular dynamics simulations were carried out to characterize the interactions between glutathione (GSH, host molecule) and hydroxyl radical (OH•, guest molecule). From this analysis, two distinct steps were identified in the recognition process of hydroxyl radical by glutathione: catching and steering, based on the interactions between the host-guest molecules. Over 78% of all interactions are related to the catching mechanism via complex formation between anionic carboxyl groups and the OH radical, hence both terminal residues of GSH serve as recognition sites. The glycine residue has an additional role in the recognition of OH radical, namely the steering. The flexibility of the Gly residue enables the formation of further interactions of other parts of glutathione (e.g. thiol, α- and β-carbons) with the lone electron pair of the hydroxyl radical. Moreover, quantum chemical calculations were carried out on selected GSH/OH• complexes and on appropriate GSH conformers to describe the energy profile of the recognition process. The relative enthalpy and the free energy changes of the radical recognition of the strongest complexes varied from −42.4 to −27.8 kJ/mol and from −21.3 to 9.8 kJ/mol, respectively. These complexes, containing two or more intermolecular interactions, would be the starting configurations for the hydrogen atom migration to quench the hydroxyl radical via different reaction channels.

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Section: Resultssupporting

confidence: 87%

Glutathione – Hydroxyl Radical Interaction: A Theoretical Study on Radical Recognition Process

et al. 2013

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“…York et al . [16] also report a doublet ( J = 5.2 Hz, pH = 7.3, B 0 = 9.4 T). These observations are confirmed by the kinetic studies of the exchange rates of NH with GSH-Gly CH 2 protons, which demonstrate a much slower rate of exchange of NH with solution H 2 O compared to GSH-Cys residue [17].…”

Section: Discussionmentioning

confidence: 99%

“…Unlike Glu, Gln, and other metabolites for which chemical shifts and J -coupling values are available in the literature [14], there is no consensus about spectral properties of GSH-Gly signal under physiological conditions. The previous NMR studies of the GSH-Gly signal considered it either as a singlet [14–15] or as a doublet (two glycine protons split by an amide proton) [16–17]. Figure 1a (top) compares the high resolution NMR spectrum of GSH to the numerical simulation of GSH-Glu and GSH-Cys residues (Figure 1a, bottom).…”

Section: Introductionmentioning

confidence: 99%

1H MRS detection of glycine residue of reduced glutathione in vivo

Kaiser

Marjańska

Matson

et al. 2010

Journal of Magnetic Resonance

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Glutathione (GSH) is a powerful antioxidant found inside different kinds of cells, including those of the central nervous system. Detection of GSH in the human brain using 1 H MR spectroscopy is hindered by low concentration and spectral overlap with other metabolites. Previous MRS methods focused mainly on the detection of the cysteine residue (GSH-Cys) via editing schemes. This study focuses on the detection of the glycine residue (GSH-Gly), which is overlapped by glutamate and glutamine (Glx) under physiological pH and temperature. The first goal of the study was to obtain the spectral parameters for characterization of the GSH-Gly signal under physiological conditions. The second goal was to investigate a new method of separating GSH-Gly from Glx in vivo. The characterization of the signal was carried out by utilization of numerical simulations as well as experiments over a wide range of magnetic fields (4.0-14 T). The proposed separation scheme utilizes J-difference editing to quantify the Glx contribution to separate it from the GSH-Gly signal. The presented method retains 100% of the GSH-Gly signal. The overall increase in signal to noise ratio of the targeted resonance is calculated to yield a significant SNR improvement compared to previously used methods that target GSH-Cys residue. This allows shorter acquisition times for in vivo human clinical studies.

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“…In addition, depending on the protonation states of the molecule, many differently charged structures are possible in aqueous solution. In particular, total net charge ranges from +1 to À3 [42,43,46].…”

Section: Resultsmentioning

confidence: 99%

“…Reduced GSH is a very flexible molecule whose structure was determined by single-crystal X-ray [38][39][40][41] and NMR [42][43][44][45] techniques, both as a free molecule [38,39,42,43] and bound to various proteins [40,41,44,45].…”

Section: Resultsmentioning

confidence: 99%