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Nat Commun. 2019 Mar 7;10(1):1101. doi: 10.1038/s41467-019-09020-4.

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

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Boston University, Department of Chemistry, Boston, MA, 02215, USA.
Massachusetts Institute of Technology, Department of Chemistry, Cambridge, MA, 02139, USA.
Carnegie Mellon University, Department of Chemistry, Pittsburgh, PA, 15213, USA.
Massachusetts Institute of Technology, Department of Biology, Cambridge, MA, 02139, USA.
Howard Hughes Medical Institute, Cambridge, MA, 02139, USA.
Boston University, Department of Chemistry, Boston, MA, 02215, USA.


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.

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