ACS Publications. Most Trusted. Most Cited. Most Read
Evidence for a Long-Lived, Cu-Coupled and Oxygen-Inert Disulfide Radical Anion in the Assembly of Metallothionein-3 Cu(I)4-Thiolate Cluster
My Activity

Figure 1Loading Img
    Article

    Evidence for a Long-Lived, Cu-Coupled and Oxygen-Inert Disulfide Radical Anion in the Assembly of Metallothionein-3 Cu(I)4-Thiolate Cluster
    Click to copy article linkArticle link copied!

    • Jenifer S. Calvo
      Jenifer S. Calvo
      Department of Chemistry and Biochemistry, The University of Texas at Dallas, 800 W. Campbell Road, Richardson, Texas 75080, United States
    • Rhiza Lyne E. Villones
      Rhiza Lyne E. Villones
      Department of Chemistry and Biochemistry, The University of Texas at Dallas, 800 W. Campbell Road, Richardson, Texas 75080, United States
    • Nicholas J. York
      Nicholas J. York
      Department of Chemistry and Biochemistry, University of Alabama, 250 Hackberry Lane, Tuscaloosa, Alabama 35401, United States
    • Ewelina Stefaniak
      Ewelina Stefaniak
      Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Pawińskiego 5a, 02-106 Warsaw, Poland
    • Grace E. Hamilton
      Grace E. Hamilton
      Department of Chemistry and Biochemistry, The University of Texas at Dallas, 800 W. Campbell Road, Richardson, Texas 75080, United States
    • Allison L. Stelling
      Allison L. Stelling
      Department of Chemistry and Biochemistry, The University of Texas at Dallas, 800 W. Campbell Road, Richardson, Texas 75080, United States
    • Wojciech Bal
      Wojciech Bal
      Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Pawińskiego 5a, 02-106 Warsaw, Poland
      More by Wojciech Bal
    • Brad S. Pierce
      Brad S. Pierce
      Department of Chemistry and Biochemistry, University of Alabama, 250 Hackberry Lane, Tuscaloosa, Alabama 35401, United States
    • Gabriele Meloni*
      Gabriele Meloni
      Department of Chemistry and Biochemistry, The University of Texas at Dallas, 800 W. Campbell Road, Richardson, Texas 75080, United States
      *Email: [email protected]
    Other Access OptionsSupporting Information (1)

    Journal of the American Chemical Society

    Cite this: J. Am. Chem. Soc. 2022, 144, 2, 709–722
    Click to copy citationCitation copied!
    https://doi.org/10.1021/jacs.1c03984
    Published January 5, 2022
    Copyright © 2022 American Chemical Society

    Abstract

    Click to copy section linkSection link copied!
    Abstract Image

    The human copper-binding protein metallothionein-3 (MT-3) can reduce Cu(II) to Cu(I) and form a polynuclear Cu(I)4-Cys5–6 cluster concomitant with intramolecular disulfide bonds formation, but the cluster is unusually inert toward O2 and redox-cycling. We utilized a combined array of rapid-mixing spectroscopic techniques to identify and characterize the transient radical intermediates formed in the reaction between Zn7MT-3 and Cu(II) to form Cu(I)4Zn(II)4MT-3. Stopped-flow electronic absorption spectroscopy reveals the rapid formation of transient species with absorption centered at 430–450 nm and consistent with the generation of disulfide radical anions (DRAs) upon reduction of Cu(II) by MT-3 cysteine thiolates. These DRAs are oxygen-stable and unusually long-lived, with lifetimes in the seconds regime. Subsequent DRAs reduction by Cu(II) leads to the formation of a redox-inert Cu(I)4-Cys5 cluster with short Cu–Cu distances (<2.8 Å), as revealed by low-temperature (77 K) luminescence spectroscopy. Rapid freeze-quench Raman and electron paramagnetic resonance (EPR) spectroscopy characterization of the intermediates confirmed the DRA nature of the sulfur-centered radicals and their subsequent oxidation to disulfide bonds upon Cu(II) reduction, generating the final Cu(I)4-thiolate cluster. EPR simulation analysis of the radical g- and A-values indicate that the DRAs are directly coupled to Cu(I), potentially explaining the observed DRA stability in the presence of O2. We thus provide evidence that the MT-3 Cu(I)4-Cys5 cluster assembly process involves the controlled formation of novel long-lived, copper-coupled, and oxygen-stable disulfide radical anion transient intermediates.

    Copyright © 2022 American Chemical Society

    Read this article

    To access this article, please review the available access options below.

    Get instant access

    Purchase Access

    Read this article for 48 hours. Check out below using your ACS ID or as a guest.

    Recommended

    Access through Your Institution

    You may have access to this article through your institution.

    Your institution does not have access to this content. Add or change your institution or let them know you’d like them to include access.

    Supporting Information

    Click to copy section linkSection link copied!

    The Supporting Information is available free of charge at https://pubs.acs.org/doi/10.1021/jacs.1c03984.

    • Experimental methods and supplementary figures (PDF)

    Terms & Conditions

    Most electronic Supporting Information files are available without a subscription to ACS Web Editions. Such files may be downloaded by article for research use (if there is a public use license linked to the relevant article, that license may permit other uses). Permission may be obtained from ACS for other uses through requests via the RightsLink permission system: http://pubs.acs.org/page/copyright/permissions.html.

    Cited By

    Click to copy section linkSection link copied!

    This article is cited by 7 publications.

    1. Bei Zhang, Stefanie D. Boyd, Dannie Zhabilov, Morgan Ullrich, Ninian J. Blackburn, Duane D. Winkler. Pathogenic R163W Variant of the Copper Chaperone for Sod1 (Ccs) Functions as an Anti-chaperone. Biochemistry 2024, 63 (16) , 2051-2062. https://doi.org/10.1021/acs.biochem.4c00223
    2. Manuel David Peris-Díaz, Alicja Orzeł, Sylwia Wu, Karolina Mosna, Perdita E. Barran, Artur Krężel. Combining Native Mass Spectrometry and Proteomics to Differentiate and Map the Metalloform Landscape in Metallothioneins. Journal of Proteome Research 2024, 23 (8) , 3626-3637. https://doi.org/10.1021/acs.jproteome.4c00271
    3. Manuel David Peris-Díaz, Sylwia Wu, Karolina Mosna, Ellen Liggett, Alexey Barkhanskiy, Alicja Orzeł, Perdita Barran, Artur Krężel. Structural Characterization of Cu(I)/Zn(II)-metallothionein-3 by Ion Mobility Mass Spectrometry and Top-Down Mass Spectrometry. Analytical Chemistry 2023, 95 (29) , 10966-10974. https://doi.org/10.1021/acs.analchem.3c00989
    4. Enrico Falcone, Alessandra G. Ritacca, Sonja Hager, Hemma Schueffl, Bertrand Vileno, Youssef El Khoury, Petra Hellwig, Christian R. Kowol, Petra Heffeter, Emilia Sicilia, Peter Faller. Copper-Catalyzed Glutathione Oxidation is Accelerated by the Anticancer Thiosemicarbazone Dp44mT and Further Boosted at Lower pH. Journal of the American Chemical Society 2022, 144 (32) , 14758-14768. https://doi.org/10.1021/jacs.2c05355
    5. Rabina Lakha, Carla Hachicho, Matthew R. Mehlenbacher, Dean E. Wilcox, Rachel N. Austin, Christina L. Vizcarra. Metallothionein-3 attenuates the effect of Cu2+ ions on actin filaments. Journal of Inorganic Biochemistry 2023, 242 , 112157. https://doi.org/10.1016/j.jinorgbio.2023.112157
    6. Chenchen Qu, Peng Cai, Kaixiang Shi, Wenli Chen, Jinzhao Chen, Chunhui Gao, Yichao Wu, Qiaoyun Huang. Methods and mechanisms of the interactions between biomacromolecules and heavy metals. Chinese Science Bulletin 2022, 67 (35) , 4192-4205. https://doi.org/10.1360/TB-2022-0636
    7. Matthew R. Mehlenbacher, Rahma Elsiesy, Rabina Lakha, Rhiza Lyne E. Villones, Marina Orman, Christina L. Vizcarra, Gabriele Meloni, Dean E. Wilcox, Rachel N. Austin. Metal binding and interdomain thermodynamics of mammalian metallothionein-3: enthalpically favoured Cu + supplants entropically favoured Zn 2+ to form Cu 4 + clusters under physiological conditions. Chemical Science 2022, 13 (18) , 5289-5304. https://doi.org/10.1039/D2SC00676F

    Journal of the American Chemical Society

    Cite this: J. Am. Chem. Soc. 2022, 144, 2, 709–722
    Click to copy citationCitation copied!
    https://doi.org/10.1021/jacs.1c03984
    Published January 5, 2022
    Copyright © 2022 American Chemical Society

    Article Views

    2686

    Altmetric

    -

    Citations

    Learn about these metrics

    Article 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.