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.
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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.
DepartmentMassachusetts Institute of Technology. Department of Chemistry; Massachusetts Institute of Technology. Department of Biology
Springer Science and Business Media LLC
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)
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