Download MendeleyA widely distributed diheme enzyme from Burkholderia that displays an atypically stable bis-Fe(IV) state.
Rizzolo, K., Cohen, S.E., Weitz, A.C., Lopez Munoz, M.M., Hendrich, M.P., Drennan, C.L., Elliott, S.J.(2019) Nat Commun 10: 1101-1101
- PubMed: 30846684
- DOI: https://doi.org/10.1038/s41467-019-09020-4
- Primary Citation of Related Structures:
6NX0 - PubMed Abstract:
Bacterial diheme peroxidases represent a diverse enzyme family with functions that range from hydrogen peroxide (H 2 O 2 ) 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 H 2 O 2 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 H 2 O 2 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 H 2 O 2 turnover in a mechanistically distinct manner.
Organizational Affiliation:
Boston University, Department of Chemistry, Boston, MA, 02215, USA.
