IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v8y2017i1d10.1038_s41467-017-00896-8.html
   My bibliography  Save this article

Biogenic manganese oxide nanoparticle formation by a multimeric multicopper oxidase Mnx

Author

Listed:
  • Christine A. Romano

    (Oregon Health & Science University)

  • Mowei Zhou

    (Pacific Northwest National Laboratory)

  • Yang Song

    (Ohio State University)

  • Vicki H. Wysocki

    (Ohio State University)

  • Alice C. Dohnalkova

    (Pacific Northwest National Laboratory)

  • Libor Kovarik

    (Pacific Northwest National Laboratory)

  • Ljiljana Paša-Tolić

    (Pacific Northwest National Laboratory)

  • Bradley M. Tebo

    (Oregon Health & Science University)

Abstract

Bacteria that produce Mn oxides are extraordinarily skilled engineers of nanomaterials that contribute significantly to global biogeochemical cycles. Their enzyme-based reaction mechanisms may be genetically tailored for environmental remediation applications or bioenergy production. However, significant challenges exist for structural characterization of the enzymes responsible for biomineralization. The active Mn oxidase in Bacillus sp. PL-12, Mnx, is a complex composed of a multicopper oxidase (MCO), MnxG, and two accessory proteins, MnxE and MnxF. MnxG shares sequence similarity with other, structurally characterized MCOs. MnxE and MnxF have no similarity to any characterized proteins. The ~200 kDa complex has been recalcitrant to crystallization, so its structure is unknown. Here, we show that native mass spectrometry defines the subunit topology and copper binding of Mnx, while high-resolution electron microscopy visualizes the protein and nascent Mn oxide minerals. These data provide critical structural information for understanding Mn biomineralization by such unexplored enzymes.

Suggested Citation

  • Christine A. Romano & Mowei Zhou & Yang Song & Vicki H. Wysocki & Alice C. Dohnalkova & Libor Kovarik & Ljiljana Paša-Tolić & Bradley M. Tebo, 2017. "Biogenic manganese oxide nanoparticle formation by a multimeric multicopper oxidase Mnx," Nature Communications, Nature, vol. 8(1), pages 1-8, December.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_s41467-017-00896-8
    DOI: 10.1038/s41467-017-00896-8
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-017-00896-8
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/s41467-017-00896-8?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_s41467-017-00896-8. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.