IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v427y2004i6974d10.1038_nature02280.html
   My bibliography  Save this article

Crystal structure and mechanism of a bacterial fluorinating enzyme

Author

Listed:
  • Changjiang Dong

    (The University of St Andrews)

  • Fanglu Huang

    (University Chemical Laboratory)

  • Hai Deng

    (The University of St Andrews)

  • Christoph Schaffrath

    (The University of St Andrews)

  • Jonathan B. Spencer

    (University Chemical Laboratory)

  • David O'Hagan

    (The University of St Andrews)

  • James H. Naismith

    (The University of St Andrews)

Abstract

Fluorine is the thirteenth most abundant element in the earth's crust, but fluoride concentrations in surface water are low and fluorinated metabolites are extremely rare1,2. The fluoride ion is a potent nucleophile in its desolvated state, but is tightly hydrated in water and effectively inert. Low availability and a lack of chemical reactivity have largely excluded fluoride from biochemistry: in particular, fluorine's high redox potential precludes the haloperoxidase-type mechanism3,4 used in the metabolic incorporation of chloride and bromide ions. But fluorinated chemicals are growing in industrial importance, with applications in pharmaceuticals, agrochemicals and materials products5,6,7. Reactive fluorination reagents requiring specialist process technologies are needed in industry and, although biological catalysts for these processes are highly sought after, only one enzyme that can convert fluoride to organic fluorine has been described8. Streptomyces cattleya can form carbon–fluorine bonds9 and must therefore have evolved an enzyme able to overcome the chemical challenges of using aqueous fluoride. Here we report the sequence and three-dimensional structure of the first native fluorination enzyme, 5′-fluoro-5′-deoxyadenosine synthase, from this organism. Both substrate and products have been observed bound to the enzyme, enabling us to propose a nucleophilic substitution mechanism for this biological fluorination reaction.

Suggested Citation

  • Changjiang Dong & Fanglu Huang & Hai Deng & Christoph Schaffrath & Jonathan B. Spencer & David O'Hagan & James H. Naismith, 2004. "Crystal structure and mechanism of a bacterial fluorinating enzyme," Nature, Nature, vol. 427(6974), pages 561-565, February.
  • Handle: RePEc:nat:nature:v:427:y:2004:i:6974:d:10.1038_nature02280
    DOI: 10.1038/nature02280
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature02280
    File Function: Abstract
    Download Restriction: Access to the full text of the articles in this series is restricted.

    File URL: https://libkey.io/10.1038/nature02280?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
    ---><---

    As the access to this document is restricted, you may want to search for a different version of it.

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    Cited by:

    1. Randy B. Stockbridge & Lawrence P. Wackett, 2024. "The link between ancient microbial fluoride resistance mechanisms and bioengineering organofluorine degradation or synthesis," Nature Communications, Nature, vol. 15(1), pages 1-12, December.
    2. Ningning Li & Bingjing Hu & Anming Wang & Huimin Li & Youcheng Yin & Tianyu Mao & Tian Xie, 2020. "Facile Bioinspired Preparation of Fluorinase@Fluoridated Hydroxyapatite Nanoflowers for the Biosynthesis of 5′-Fluorodeoxy Adenosine," Sustainability, MDPI, vol. 12(1), pages 1-15, January.

    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:nature:v:427:y:2004:i:6974:d:10.1038_nature02280. 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.