MIT Libraries homeMIT Libraries logoDSpace@MIT

MIT
View Item 
  • DSpace@MIT Home
  • MIT Open Access Articles
  • MIT Open Access Articles
  • View Item
  • DSpace@MIT Home
  • MIT Open Access Articles
  • MIT Open Access Articles
  • View Item
JavaScript is disabled for your browser. Some features of this site may not work without it.

A widely distributed diheme enzyme from Burkholderia that displays an atypically stable bis-Fe(IV) state

Author(s)
Drennan, Catherine L; Cohen, Steven E.,Ph. D.Massachusetts Institute of Technology.
Thumbnail
DownloadPublished version (1.459Mb)
Terms of use
Creative Commons Attribution 4.0 International license https://creativecommons.org/licenses/by/4.0/
Metadata
Show full item record
Abstract
Bacterial diheme peroxidases represent a diverse enzyme family with functions that range from hydrogen peroxide (H₂O₂) reduction to post-translational modifications. By implementing a sequence similarity network (SSN) of the bCCP_MauG superfamily, we present the discovery of a unique diheme peroxidase BthA conserved in all Burkholderia. Using a combination of magnetic resonance, near-IR and Mössbauer spectroscopies and electrochemical methods, we report that BthA is capable of generating a bis-Fe(IV) species previously thought to be a unique feature of the diheme enzyme MauG. However, BthA is not MauG-like in that it catalytically converts H₂O₂ to water, and a 1.54-Å resolution crystal structure reveals striking differences between BthA and other superfamily members, including the essential residues for both bis-Fe(IV) formation and H₂O₂ turnover. Taken together, we find that BthA represents a previously undiscovered class of diheme enzymes, one that stabilizes a bis-Fe(IV) state and catalyzes H₂O₂ turnover in a mechanistically distinct manner.
Date issued
2019-03
URI
https://hdl.handle.net/1721.1/126207
Department
Massachusetts Institute of Technology. Department of Chemistry; Massachusetts Institute of Technology. Department of Biology
Journal
Nature Communications
Publisher
Springer Science and Business Media LLC
Citation
Rizzolo, Kimberly et al. “A widely distributed diheme enzyme from Burkholderia that displays an atypically stable bis-Fe(IV) state.” Nature Communications, vol. 10, 2019, article 1101 © 2019 The Author(s)
Version: Final published version
ISSN
2041-1723

Collections
  • MIT Open Access Articles

Browse

All of DSpaceCommunities & CollectionsBy Issue DateAuthorsTitlesSubjectsThis CollectionBy Issue DateAuthorsTitlesSubjects

My Account

Login

Statistics

OA StatisticsStatistics by CountryStatistics by Department
MIT Libraries homeMIT Libraries logo

Find us on

Twitter Facebook Instagram YouTube RSS

MIT Libraries navigation

SearchHours & locationsBorrow & requestResearch supportAbout us
PrivacyPermissionsAccessibility
MIT
Massachusetts Institute of Technology
Content created by the MIT Libraries, CC BY-NC unless otherwise noted. Notify us about copyright concerns.