Reversible Oxidation States Research Articles

Redox Regulation of SH2-Domain-Containing Protein Tyrosine Phosphatases by Two Backdoor Cysteines

Protein tyrosine phosphatases (PTPs) are known to be regulated by phosphorylation, localization, and protein-protein interactions. More recently, redox-dependent inactivation has emerged as a critical factor in attenuating PTP activity in response to cellular stimuli. The tandem Src homology 2 domain-containing PTPs (SHPs) belong to the family of nonreceptor PTPs whose activity can be modulated by reversible oxidation in vivo. Herein we have investigated in vitro the kinetic and mechanistic details of reversible oxidation of SHP-1 and SHP-2. We have confirmed the susceptibility of the active site cysteines of SHPs to oxidative inactivation, with rate constants for oxidation similar to other PTPs (2-10 M(-1) s(-1)). Both SHP-1 and SHP-2 can be reduced and reactivated with the reductants DTT and gluthathione, whereas only the catalytic domain of SHP-2 is subject to reactivation by thioredoxin. Stabilization of the reversible oxidation state of the SHPs proceeds via a novel mechanism unlike for other PTPs wherein oxidation yields either a disulfide between the catalytic cysteine and a nearby "backdoor" cysteine or a sulfenylamide bond with the amide backbone nitrogen of the adjacent amino acid. Instead, in the reversibly oxidized and inactivated SHPs, the catalytic cysteine is rereduced while two conserved backdoor cysteines form an intramolecular disulfide. Formation of this backdoor-backdoor disulfide is dependent on the presence of the active site cysteine and can proceed via either active site cysteine-backdoor cysteine intermediate. Removal of both backdoor cysteines leads to irreversible oxidative inactivation, demonstrating that these two cysteines are necessary and sufficient for ensuring reversible oxidation of the SHPs. Our results extend the mechanisms by which redox regulation of PTPs is used to modulate intracellular signaling pathways.

Preparation of CeO2-ZrO2 mixed oxide with high surface area and high thermal stability

Ceria-zirconia solid particles have been recognized as a key material of the automotive exhaust catalysts since they can release and uptake oxygen owing to the rapid reversible oxidation states of cerium between Ce3+ and Ce4+. Several methods have recently been described to prepare the CeO2-ZrO2 solid particles used in the catalysts. In this paper, a new coprecipitation method is used to prepare the CeO2-ZrO2 solid particles. The Ce-Zr alcogel is dried and calcined in flowing N2 not in flowing air under atmospheric pressure. The results show that the ceria-zirconia sample calcined at 650 °C has high surface area over 90 m2g−1, which drops to 40 m2g−1 following treatment at 900°C.

The Mycobacterial Thioredoxin Peroxidase Can Act as a One-cysteine Peroxiredoxin

Thioredoxin peroxidase (TPx) has been reported to dominate the defense against H(2)O(2), other hydroperoxides, and peroxynitrite at the expense of thioredoxin (Trx) B and C in Mycobacterium tuberculosis (Mt). By homology, the enzyme has been classified as an atypical 2-C-peroxiredoxin (Prx), with Cys(60) as the "peroxidatic" cysteine (C(P)) forming a complex catalytic center with Cys(93) as the "resolving" cysteine (C(R)). Site-directed mutagenesis confirms Cys(60) to be C(P) and Cys(80) to be catalytically irrelevant. Replacing Cys(93) with serine leads to fast inactivation as seen by conventional activity determination, which is associated with oxidation of Cys(60) to a sulfinic acid derivative. However, in comparative stopped-flow analysis, WT-MtTPx and MtTPx C93S reduce peroxynitrite and react with TrxB and -C similarly fast. Reduction of pre-oxidized WT-MtTPx and MtTPx C93S by MtTrxB is demonstrated by monitoring the redox-dependent tryptophan fluorescence of MtTrxB. Furthermore, MtTPx C93S remains stable for 10 min at a morpholinosydnonimine hydrochloride-generated low flux of peroxynitrite and excess MtTrxB in a dihydrorhodamine oxidation model. Liquid chromatography-tandem mass spectrometry analysis revealed disulfide bridges between Cys(60) and Cys(93) and between Cys(60) and Cys(80) in oxidized WT-MtTPx. Reaction of pre-oxidized WT-MtTPx and MtTPx C93S with MtTrxB C34S or MtTrxC C40S yielded dead-end intermediates in which the Trx mutants are preferentially linked via disulfide bonds to Cys(60) and never to Cys(93) of the TPx. It is concluded that neither Cys(80) nor Cys(93) is required for the catalytic cycle of the peroxidase. Instead, MtTPx can react as a 1-C-Prx with Cys(60) being the site of attack for both the oxidizing and the reducing substrate. The role of Cys(93) is likely to conserve the oxidation equivalents of the sulfenic acid state of C(P) as a disulfide bond to prevent overoxidation of Cys(60) under a restricted supply of reducing substrate.

Synthesis and study of multiple cationic salts of hexamethoxytriphenylene (HMTP)

2,3,6,7,10,11-Hexamethoxytriphenylene (HMTP) is known to exhibit multiple reversible oxidation states. We report on the synthesis and the physical properties of stable monocation, dication, and alloy salts between HMTP and ClO 4 −. The monocation salt, HMTP-ClO 4, is a half-filled band, quasi one-dimensional semiconductor with a possible spin-Peierls transition at 240K. The dication is also found to be a semiconductor.

Synthesis, characterization, and electrochemistry of a new platinum "tetrathiolene" cluster, tetrakis(triphenylphosphine)tetrathionaphthalenediplatinum(II,II): a novel system with five reversible oxidation states

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTSynthesis, characterization, and electrochemistry of a new platinum "tetrathiolene" cluster, tetrakis(triphenylphosphine)tetrathionaphthalenediplatinum(II,II): a novel system with five reversible oxidation statesBoon-Keng Teo, F. Wudl, J. H. Marshall, and A. KrugerCite this: J. Am. Chem. Soc. 1977, 99, 7, 2349–2350Publication Date (Print):March 1, 1977Publication History Published online1 May 2002Published inissue 1 March 1977https://doi.org/10.1021/ja00449a060RIGHTS & PERMISSIONSArticle Views139Altmetric-Citations21LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InReddit PDF (253 KB) Get e-Alerts Get e-Alerts