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

Kimberly Rizzolo, Steven E. Cohen, Andrew C. Weitz, Madeline M. López Muñoz, Michael P. Hendrich, Catherine L. Drennan and Sean J. Elliott ()
Additional contact information
Kimberly Rizzolo: Boston University, Department of Chemistry
Steven E. Cohen: Massachusetts Institute of Technology, Department of Chemistry
Andrew C. Weitz: Carnegie Mellon University, Department of Chemistry
Madeline M. López Muñoz: Boston University, Department of Chemistry
Michael P. Hendrich: Carnegie Mellon University, Department of Chemistry
Catherine L. Drennan: Massachusetts Institute of Technology, Department of Chemistry
Sean J. Elliott: Boston University, Department of Chemistry

Nature Communications, 2019, vol. 10, issue 1, 1-10

Abstract: 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.

Date: 2019
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/s41467-019-09020-4 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-09020-4

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-019-09020-4

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().