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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.

Author information

1
Boston University, Department of Chemistry, Boston, MA, 02215, USA.
2
Massachusetts Institute of Technology, Department of Chemistry, Cambridge, MA, 02139, USA.
3
Carnegie Mellon University, Department of Chemistry, Pittsburgh, PA, 15213, USA.
4
Massachusetts Institute of Technology, Department of Biology, Cambridge, MA, 02139, USA.
5
Howard Hughes Medical Institute, Cambridge, MA, 02139, USA.
6
Boston University, Department of Chemistry, Boston, MA, 02215, USA. elliott@bu.edu.

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.

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