The Chemistry of Thiol Oxidation and Detection

Conte, Mauro Lo; Carroll, Kate S.

doi:10.1007/978-94-007-5787-5_1

Cited by 57 publications

(62 citation statements)

References 212 publications

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“…In these experiments, we could not detect a change in the sulfenylation or glutathionylation state of E. coli proteins in response to peroxynitrite stress, in line with our ICAT-based experiments. Nevertheless, these experiments cannot exclude a loss of sulfenylation detection in our experiments based on the methodological limitations typical for iodoacetamide-based probes, especially in light of the fact that these probes can react to some extent with sulfenic acids (43). Therefore we must stress that our approach, as any other focused approach, will not be able to reveal the full extent of every possible modification caused by peroxynitrite or ONOO Ϫ -related reaction products.…”

Section: Discussionmentioning

confidence: 91%

Redox Proteomics Uncovers Peroxynitrite-sensitive Proteins That Help Escherichia coli to Overcome Nitrosative Stress

Lindemann

Lupilova

Müller

et al. 2013

Journal of Biological Chemistry

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Background: Oxidative thiol modifications are thought to be one of the major effects of peroxynitrite on proteins. Results: Quantitative redox proteomics identified proteins thiol-modified by peroxynitrite, and cells lacking these proteins show an impaired recovery. Conclusion: Thiol modifications caused by peroxynitrite in Escherichia coli are highly specific for a small number of selected proteins. Significance: Thiol modifications regulate the activity of proteins under peroxynitrite stress.

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Section: Discussionmentioning

confidence: 91%

Redox Proteomics Uncovers Peroxynitrite-sensitive Proteins That Help Escherichia coli to Overcome Nitrosative Stress

Lindemann

Lupilova

Müller

et al. 2013

Journal of Biological Chemistry

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“…The thiol side-chain of some cysteines can be highly reactive and undergo different modifications under oxidative and nitrosative stresses (15)(16)(17). Thiols can form disulfide bonds as well as sulfenates, sulfinates, and sulfonates under oxidizing conditions, and are susceptible to nitrosylation (16).…”

mentioning

confidence: 99%

“…Thiols can form disulfide bonds as well as sulfenates, sulfinates, and sulfonates under oxidizing conditions, and are susceptible to nitrosylation (16). Because oxidative and nitrosative stresses are relevant to M. tuberculosis biology (18), we wished to determine if splicing might be sensitive to these conditions.…”

mentioning

confidence: 99%

SufB intein of Mycobacterium tuberculosis as a sensor for oxidative and nitrosative stresses

Topilina

Green

Jayachandran

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

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Inteins are mobile genetic elements that self-splice at the protein level. Mycobacteria have inteins inserted into several important genes, including those corresponding to the iron-sulfur cluster assembly protein SufB. Curiously, the SufB inteins are found primarily in mycobacterial species that are potential human pathogens. Here we discovered an exceptional sensitivity of Mycobacterium tuberculosis SufB intein splicing to oxidative and nitrosative stresses when expressed in Escherichia coli. This effect results from predisposition of the intein's catalytic cysteine residues to oxidative and nitrosative modifications. Experiments with a fluorescent reporter system revealed that reactive oxygen species and reactive nitrogen species inhibit SufB extein ligation by forcing either precursor accumulation or N-terminal cleavage. We propose that splicing inhibition is an immediate, posttranslational regulatory response that can be either reversible, by inducing precursor accumulation, or irreversible, by inducing N-terminal cleavage, which may potentially channel mycobacteria into dormancy under extreme oxidative and nitrosative stresses.

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“…One possible explanation for this increased aggregation propensity is that the negatively charged Ga-PP in solution may electrostatically repel the negative β-globin in which Cys 93 (pK a = 8.2) is oxidized to cysteine sulfinic acid (pK a = 2) or sulfonic acid (pK a = -3) [38]. This would exclude partial solvent for β-globins and expose hydrophobic residues, triggering nucleation and irreversible aggregation [39].…”

Section: Production Of Hb Ga and Evaluation Of Its Stabilitymentioning

confidence: 99%

Evaluation of Gallium as a Tracer of Exogenous Hemoglobin–Haptoglobin Complexes for Targeted Drug Delivery Applications

Kaltashov

2016

J. Am. Soc. Mass Spectrom.

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Abstract. Haptoglobin (Hp) is a plasma glycoprotein that generates significant interest in the drug delivery community because of its potential for delivery of antiretroviral medicines with high selectivity to macrophages and monocytes, the latent reservoirs of human immunodeficiency virus. As is the case with other therapies that exploit transport networks for targeted drug delivery, the success of the design and optimization of Hp-based therapies will critically depend on the ability to accurately localize and quantitate Hp-drug conjugates on the varying and unpredictable background of endogenous proteins having identical structure. In this work, we introduce a new strategy for detecting and quantitating exogenous Hp and Hp-based drugs with high sensitivity in complex biological samples using gallium as a tracer of this protein and inductively coupled plasma mass spectrometry (ICP MS) as a method of detection. Metal label is introduced by reconstituting hemoglobin (Hb) with gallium(III)-protoporphyrin IX followed by its complexation with Hp. Formation of the Hp/Hb assembly and its stability are evaluated with native electrospray ionization mass spectrometry. Both stable isotopes of Ga give rise to an abundant signal in ICP MS of a human plasma sample spiked with the metallabeled Hp/Hb complex. The metal label signal exceeds the spectral interferences' contributions by more than an order of magnitude even with the concentration of the exogenous protein below 10 nM, the level that is more than adequate for the planned pharmacokinetic studies of Hp-based therapeutics.

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The Chemistry of Thiol Oxidation and Detection

Cited by 57 publications

References 212 publications

Redox Proteomics Uncovers Peroxynitrite-sensitive Proteins That Help Escherichia coli to Overcome Nitrosative Stress

Redox Proteomics Uncovers Peroxynitrite-sensitive Proteins That Help Escherichia coli to Overcome Nitrosative Stress

SufB intein of Mycobacterium tuberculosis as a sensor for oxidative and nitrosative stresses

Evaluation of Gallium as a Tracer of Exogenous Hemoglobin–Haptoglobin Complexes for Targeted Drug Delivery Applications

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