A widely distributed diheme enzyme from Burkholderia that displays an atypically stable bis-Fe(IV) state
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s41467-019-09020-4.pdf
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Published version
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1.46 MB
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Author(s)
Drennan, Catherine L
Cohen, Steven E.,Ph. D.Massachusetts Institute of Technology.
Date Issued
March 2019
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
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.
MIT Department
Massachusetts Institute of Technology. Department of Chemistry
Massachusetts Institute of Technology. Department of Biology
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Creative Commons Attribution 4.0 International license
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DOI of Published Version
https://doi.org/10.1038/S41467-019-09020-4
