• Login
    View Item 
    •   Home
    • Department of molecular bacteriology (MOBA)
    • publications of the research group genomeanalytics (GMAK)
    • View Item
    •   Home
    • Department of molecular bacteriology (MOBA)
    • publications of the research group genomeanalytics (GMAK)
    • View Item
    JavaScript is disabled for your browser. Some features of this site may not work without it.

    Browse

    All of HZICommunitiesTitleAuthorsIssue DateSubmit DateSubjectsJournalTypesSubject (MeSH)This CollectionTitleAuthorsIssue DateSubmit DateSubjectsJournalTypesSubject (MeSH)

    My Account

    LoginRegister

    Local Links

    About: PolicyHelmholtz-Zentrum für Infektionsforschung HomepageHZI-Library HomepageContact usOpen AccessPublishing ApproachGetting StartedEditing ProfileBrowsing OptionsUsing SearchSubmitting ContentLicenced Journals & access details here

    Statistics

    Display statistics

    The mycobacterial thioredoxin peroxidase can act as a one-cysteine peroxiredoxin.

    • CSV
    • RefMan
    • EndNote
    • BibTex
    • RefWorks
    Thumbnail
    Name:
    Trujillo et al_final.pdf
    Size:
    961.8Kb
    Format:
    PDF
    Description:
    original document
    Download
    Average rating
     
       votes
    Cast your vote
    You can rate an item by clicking the amount of stars they wish to award to this item. When enough users have cast their vote on this item, the average rating will also be shown.
    Star rating
     
    Your vote was cast
    Thank you for your feedback
    Authors
    Trujillo, Madia
    Mauri, PierLuigi
    Benazzi, Louise
    Comini, Marcelo
    De Palma, Antonella
    Flohé, Leopold
    Radi, Rafael
    Stehr, Matthias
    Singh, Mahavir
    Ursini, Fulvio
    Jaeger, Timo
    Show allShow less
    Issue Date
    2006-07-21
    
    Metadata
    Show full item record
    Abstract
    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.
    Citation
    The mycobacterial thioredoxin peroxidase can act as a one-cysteine peroxiredoxin. 2006, 281 (29):20555-66 J. Biol. Chem.
    Affiliation
    Departamento de Bioquímica, Facultad de Medicina, Universidad de la República, Avda. General Flores 2125, UY-11800 Montevideo, Uruguay.
    Journal
    The Journal of biological chemistry
    URI
    http://hdl.handle.net/10033/15372
    DOI
    10.1074/jbc.M601008200
    PubMed ID
    16682410
    Type
    Article
    Language
    en
    ISSN
    0021-9258
    ae974a485f413a2113503eed53cd6c53
    10.1074/jbc.M601008200
    Scopus Count
    Collections
    publications of the research group genomeanalytics (GMAK)

    entitlement

     

    DSpace software copyright © 2002-2023  DuraSpace
    Quick Guide | Kontakt | Feedback abschicken
    Open Repository is a service operated by 
    Atmire NV
     

    Export search results

    The export option will allow you to export the current search results of the entered query to a file. Different formats are available for download. To export the items, click on the button corresponding with the preferred download format.

    By default, clicking on the export buttons will result in a download of the allowed maximum amount of items.

    To select a subset of the search results, click "Selective Export" button and make a selection of the items you want to export. The amount of items that can be exported at once is similarly restricted as the full export.

    After making a selection, click one of the export format buttons. The amount of items that will be exported is indicated in the bubble next to export format.