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


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2019-12

AUTHORS

Kimberly Rizzolo, Steven E. Cohen, Andrew C. Weitz, Madeline M. López Muñoz, Michael P. Hendrich, Catherine L. Drennan, Sean J. Elliott

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. More... »

PAGES

1101

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/s41467-019-09020-4

DOI

http://dx.doi.org/10.1038/s41467-019-09020-4

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1112605353

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/30846684


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