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

Author

Listed:
  • Kimberly Rizzolo

    (Boston University, Department of Chemistry)

  • Steven E. Cohen

    (Massachusetts Institute of Technology, Department of Chemistry)

  • Andrew C. Weitz

    (Carnegie Mellon University, Department of Chemistry)

  • Madeline M. López Muñoz

    (Boston University, Department of Chemistry)

  • Michael P. Hendrich

    (Carnegie Mellon University, Department of Chemistry)

  • Catherine L. Drennan

    (Massachusetts Institute of Technology, Department of Chemistry
    Massachusetts Institute of Technology, Department of Biology
    Howard Hughes Medical Institute)

  • Sean J. Elliott

    (Boston University, Department of Chemistry)

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.

Suggested Citation

  • Kimberly Rizzolo & Steven E. Cohen & Andrew C. Weitz & Madeline M. López Muñoz & Michael P. Hendrich & Catherine L. Drennan & Sean J. Elliott, 2019. "A widely distributed diheme enzyme from Burkholderia that displays an atypically stable bis-Fe(IV) state," Nature Communications, Nature, vol. 10(1), pages 1-10, December.
    • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-09020-4
    DOI: 10.1038/s41467-019-09020-4
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