University Library
  • Login
A gateway to Melbourne's research publications
Minerva Access is the University's Institutional Repository. It aims to collect, preserve, and showcase the intellectual output of staff and students of the University of Melbourne for a global audience.
View Item 
  • Minerva Access
  • Science
  • School of Chemistry
  • School of Chemistry - Research Publications
  • View Item
  • Minerva Access
  • Science
  • School of Chemistry
  • School of Chemistry - Research Publications
  • View Item
JavaScript is disabled for your browser. Some features of this site may not work without it.

    Unification of the Copper(I) Binding Affinities of the Metallo-chaperones Atx1, Atox1, and Related Proteins DETECTION PROBES AND AFFINITY STANDARDS

    Thumbnail
    Citations
    Scopus
    Web of Science
    Altmetric
    159
    151
    Author
    Xiao, Z; Brose, J; Schimo, S; Ackland, SM; La Fontaine, S; Wedd, AG
    Date
    2011-04-01
    Source Title
    Journal of Biological Chemistry
    Publisher
    AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
    University of Melbourne Author/s
    Xiao, Zhiguang; BROSE, JENS; Wedd, Anthony
    Affiliation
    Chemistry
    Metadata
    Show full item record
    Document Type
    Journal Article
    Citations
    Xiao, Z., Brose, J., Schimo, S., Ackland, S. M., La Fontaine, S. & Wedd, A. G. (2011). Unification of the Copper(I) Binding Affinities of the Metallo-chaperones Atx1, Atox1, and Related Proteins DETECTION PROBES AND AFFINITY STANDARDS. JOURNAL OF BIOLOGICAL CHEMISTRY, 286 (13), pp.11047-11055. https://doi.org/10.1074/jbc.M110.213074.
    Access Status
    Access this item via the Open Access location
    URI
    http://hdl.handle.net/11343/29081
    DOI
    10.1074/jbc.M110.213074
    Open Access at PMC
    http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3064159
    Description

    C1 - Journal Articles Refereed

    Abstract
    Literature estimates of metal-protein affinities are widely scattered for many systems, as highlighted by the class of metallo-chaperone proteins, which includes human Atox1. The discrepancies may be attributed to unreliable detection probes and/or inconsistent affinity standards. In this study, application of the four Cu(I) ligand probes bicinchoninate, bathocuproine disulfonate, dithiothreitol (Dtt), and glutathione (GSH) is reviewed, and their Cu(I) affinities are re-estimated and unified. Excess bicinchoninate or bathocuproine disulfonate reacts with Cu(I) to yield distinct 1:2 chromatophoric complexes [Cu(I)L(2)](3-) with formation constants β(2) = 10(17.2) and 10(19.8) m(-2), respectively. These constants do not depend on proton concentration for pH ≥7.0. Consequently, they are a pair of complementary and stable probes capable of detecting free Cu(+) concentrations from 10(-12) to 10(-19) m. Dtt binds Cu(I) with K(D) ∼10(-15) m at pH 7, but it is air-sensitive, and its Cu(I) affinity varies with pH. The Cu(I) binding properties of Atox1 and related proteins (including the fifth and sixth domains at the N terminus of the Wilson protein ATP7B) were assessed with these probes. The results demonstrate the following: (i) their use permits the stoichiometry of high affinity Cu(I) binding and the individual quantitative affinities (K(D) values) to be determined reliably via noncompetitive and competitive reactions, respectively; (ii) the scattered literature values are unified by using reliable probes on a unified scale; and (iii) Atox1-type proteins bind Cu(I) with sub-femtomolar affinities, consistent with tight control of labile Cu(+) concentrations in living cells.
    Keywords
    Bioinorganic Chemistry; Expanding Knowledge in the Chemical Sciences

    Export Reference in RIS Format     

    Endnote

    • Click on "Export Reference in RIS Format" and choose "open with... Endnote".

    Refworks

    • Click on "Export Reference in RIS Format". Login to Refworks, go to References => Import References


    Collections
    • Minerva Elements Records [52443]
    • School of Chemistry - Research Publications [572]
    Minerva AccessDepositing Your Work (for University of Melbourne Staff and Students)NewsFAQs

    BrowseCommunities & CollectionsBy Issue DateAuthorsTitlesSubjectsThis CollectionBy Issue DateAuthorsTitlesSubjects
    My AccountLoginRegister
    StatisticsMost Popular ItemsStatistics by CountryMost Popular Authors