Biologically relevant chemical properties of peroxymonophosphate (O3POOH)

Labutti, Jason; Gates, Kent S.

doi:10.1016/j.bmcl.2008.10.133

Cited by 17 publications

(19 citation statements)

References 34 publications

(46 reference statements)

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“…That reaction is typical for hypohalous ions and nucleophilic peroxy oxidants (Fig. 7) [53,55,56]. A few years ago, we demonstrated that boronates react rapidly with hypochlorite and peroxynitrite anions [51,53] (Fig.…”

Section: Introductionmentioning

confidence: 75%

Toward selective detection of reactive oxygen and nitrogen species with the use of fluorogenic probes – Limitations, progress, and perspectives

Dębowska

Dębski

Hardy

et al. 2015

Pharmacological Reports

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Over the last forty years, there has been tremendous progress in understanding the biological reactions of reactive oxygen species (ROS) and reactive nitrogen species (RNS). It is widely accepted that the generation of ROS and RNS is involved in physiological and pathophysiological processes. To understand the role of ROS and RNS in a variety of pathologies, the specific detection of ROS and RNS is fundamental. Unfortunately, the intracellular detection and quantitation of ROS and RNS remains a challenge. In this short review, we have focused on the mechanistic and quantitative aspects of their detection with the use of selected fluorogenic probes. The challenges, limitations and perspectives of these methods are discussed.

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Section: Introductionmentioning

confidence: 75%

Toward selective detection of reactive oxygen and nitrogen species with the use of fluorogenic probes – Limitations, progress, and perspectives

Dębowska

Dębski

Hardy

et al. 2015

Pharmacological Reports

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“…LaButii et al reported peroxymonophosphate ( 2− O 3 POOH) as an exceptional inactivator of PTP1B with K I = 6.6 × 10 −7 M and k inact = 0.043 s −1.90 As a result, peroxymonophosphate ( k inact / K I = 65,553 M −1 s −1 ) is approximately 7,000 times more potent than hydrogen peroxide, an endogenous regulator of PTP1B. 91 Like hydrogen peroxide, peroxymonophosphate is also an active-site directed and thiol reversible inactivator of PTP1B. In a recent study, Meng & Zhang showed that hydroxyl radical could also be a viable oxidizing agent for the PTP active site under physiological conditions.…”

Section: Covalent Ptp Inhibitorsmentioning

confidence: 99%

Covalent inhibition of protein tyrosine phosphatases

Ruddraraju

Zhang

2017

Mol. BioSyst.

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Protein tyrosine phosphatases (PTPs) are a large family of 107 signaling enzymes that catalyze the hydrolytic removal of phosphate groups from tyrosine residues in a target protein. The phosphorylation status of tyrosine residues on proteins serve as a ubiquitous mechanism for cellular signal transduction. Aberrant function of PTPs can lead to many human diseases, such as diabetes, obesity, cancer, and autoimmune diseases. As the number of disease relevant PTPs increases, there is urgency in developing highly potent inhibitors that are selective towards specific PTPs. Most current efforts have been devoted to the development of active site-directed and reversible inhibitors for PTPs. This review summarizes recent progress made in the field of covalent inhibitors to target PTPs. Here, we discuss the in vivo and in vitro inactivation of various PTPs by small molecule-containing electrophiles, such as Michael acceptors, α-halo ketones, epoxides, and isothiocyanates, etc. as well as oxidizing agents. We also suggest potential strategies to transform these electrophiles into isozyme selective covalent PTP inhibitors.

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“…Because of the crosstalk between PTPs and kinases in regulation of diverse biological processes, studies have also emerged in understanding the nature of endogenous oxidants responsible for the inactivation of this class of enzymes. For instance, relatively stable H2O2 inactivates PTP1B at ~1,000-fold slower rates than peroxymonophosphate (PMP), when the reactions were performed under similar conditions [99,100]. There is the question of whether PMP is actually formed in vivo as potential metabolizing enzymes such as catalase were found ineffective towards this reactive species.…”

Section: Redox Regulation Of Signalingmentioning

confidence: 99%

Biological chemistry and functionality of protein sulfenic acids and related thiol modifications

Devarie‐Baez

Lopez

Furdui

2015

Free Radical Research

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Selective modification of proteins at cysteine residues by reactive oxygen, nitrogen or sulfur species formed under physiological and pathological states is emerging as a critical regulator of protein activity impacting cellular function. This review focuses primarily on protein sulfenylation (-SOH), a metastable reversible modification connecting reduced cysteine thiols to many products of cysteine oxidation. An overview is first provided on the chemistry principles underlining synthesis, stability and reactivity of sulfenic acids in model compounds and proteins, followed by a brief description of analytical methods currently employed to characterize these oxidative species. The following chapters present a selection of redox-regulated proteins for which the -SOH formation was experimentally confirmed and linked to protein function. These chapters are organized based on the participation of these proteins in the regulation of signaling, metabolism and epigenetics. The last chapter discusses the therapeutic implications of altered redox microenvironment and protein oxidation in disease.

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Biologically relevant chemical properties of peroxymonophosphate (O3POOH)

Cited by 17 publications

References 34 publications

Toward selective detection of reactive oxygen and nitrogen species with the use of fluorogenic probes – Limitations, progress, and perspectives

Toward selective detection of reactive oxygen and nitrogen species with the use of fluorogenic probes – Limitations, progress, and perspectives

Covalent inhibition of protein tyrosine phosphatases

Biological chemistry and functionality of protein sulfenic acids and related thiol modifications

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