Structural highlights
Publication Abstract from PubMed
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 Mossbauer 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-A 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.
A widely distributed diheme enzyme from Burkholderia that displays an atypically stable bis-Fe(IV) state.,Rizzolo K, Cohen SE, Weitz AC, Lopez Munoz MM, Hendrich MP, Drennan CL, Elliott SJ Nat Commun. 2019 Mar 7;10(1):1101. doi: 10.1038/s41467-019-09020-4. PMID:30846684[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Rizzolo K, Cohen SE, Weitz AC, Lopez Munoz MM, Hendrich MP, Drennan CL, Elliott SJ. A widely distributed diheme enzyme from Burkholderia that displays an atypically stable bis-Fe(IV) state. Nat Commun. 2019 Mar 7;10(1):1101. doi: 10.1038/s41467-019-09020-4. PMID:30846684 doi:http://dx.doi.org/10.1038/s41467-019-09020-4
